| {"protein": "MILVEGKVAGKKYREPFSKGVLARSLTRSGMDPTDAYLLAAEVESYLKKEKKKIVTIDELVKIVYNKLKEKDEKIAEKYIRWRKIREYKEPLILLIAGASGVGTSSIAFEVANRLGIRNMISTDMIREVMRKMISKELIPSLHESTFTAYKSLRTPAPVEFDEVLVGFRDHVNVVTVGIEAVIERALTEGISIVIEGAHLVPGFIREELINKNNVAMFVLTVPDEKMHRSRFYSRCRQKWARRPLERYLKYFWAIRRIHDYIEMQARKHNIPIIENIDVVTTIDSIVKSLTEDLVHKDVGKYKG", "text": "FUNCTION: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3- diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3- bisphosphoglycerate, a thermoprotectant. SIMILARITY: Belongs to the 2-phosphoglycerate kinase family."} | |
| {"protein": "MAVQKHTVALFLAVALVAGPAASYAADAGYAPATPATPAAPATAATPATPATPATPAAVPSGKATTEEQKLIEKINAGFKAAVAAAAVVPPADKYKTFVETFGTATNKAFVEGLASGYADQSKNQLTSKLDAALKLAYEAAQGATPEAKYDAYVATLTEALRVIAGTLEVHAVKPAAEEVKVGAIPAAEVQLIDKVDAAYRTAATAANAAPANDKFTVFENTFNNAIKVSLGAAYDSYKFIPTLVAAVKQAYAAKQATAPEVKYTVSETALKKAVTAMSEAEKEATPAAAATATPTPAAATATATPAAAYATATPAAATATATPAAATATPAAAGGYKV", "text": "SUBCELLULAR LOCATION: Note=Starch granule. SIMILARITY: Belongs to the Poa p IX/Phl p VI allergen family."} | |
| {"protein": "MRPIILQGHERPLTQIKYNHDGDLLFSCAKDKVINVWFSHNGERLGTYEGHTGAIWTCDINKSSTLMVSGAADNTMRLWDVKTGKQLYKWEFPTAVKRVEFNEDDTRILAVTEERMGYAGTVTVFRVPISESDAAAETPLYVITTRESKATVAGWSYLSKFLFTGHEDGSVSRYDAITGEFVESKQVHNSGSTITDLQFYPDRTYFITSCKDTTAKAIDVDSFEVIKTYLTDTPLNTSSFTPVQDFVILGGGQEARDVTTTAARQGKFEARFYHAILEEELGRVKGHFGPINTIAVHPKGTGYASGGEDGYVRVHFFDKNYFDFKYTL", "text": "FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the eIF-3 subunit I family."} | |
| {"protein": "QLRAFVCRLSSVIFYETMYVGIVLLGLIAFDRFLKIIRPLRNIFLKKTVFAKTVSVFIWSFFFFISLPNMILSNKEATPSSVKKCASLKGPLGLKWHQIVNNISQFIFWTVFVLMLVFYVVIAKKVYDSYRKSKSKDRKNNKKLEGKVFVVVAVFFVCFAPFHFTRVPYTYSQTNNKTDCRLQNQLFIAKETTLFLAATNICMDPLIYIFLCKKFTEKLPCMRGRKTIASSQENQSSQTDNITLG", "text": "FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."} | |
| {"protein": "MAGGAMVQTVGGKTYPGKMTAFVFFTCLVASSGGLIFGYDIGISGGVTSMDSFLSEFFPSVYAQAKASKDTNQYCKFDSQLLTLFTSSLYLAALATSFVAAWVTRVFGRKWSMFCGGVTFLAGSALNGAATDVMMLILGRILLGIGVGFANQSVPLYLSEMAPANLRGMLNIGFQLMTTIGILSANLINYATSSIEGGWGWRIGLGLAGVPALIITLGALVLPDTPNSLIARGYAGDAKRVLVKIRGTDDVHDEYDDMVAASEEAASIEHPWRNILHRKYRPQLTIAILIPCFQQLTGINVIMFYAPVLFLTIGFAGDASLMSAVITGLVNMFATVVSIISVDRLGRRVLFLQGGTQMFISQVVVGTLIALQFGVAGVGEMSRSYAILLVLFICMYVAGFAWSWGPLGWLVPSEVFALEIRSAGQSIAVCVNMMLTFVIGQAFLTMLCHLKFGLFYFFAGWMLVMTTFVALFLPETKGVPIEEMNHVWSRHWFWGSYVTAHDVAGAGAGGGGNRRSHNV", "text": "FUNCTION: Mediates active uptake of hexoses by sugar:proton symport. Can transport glucose, xylose and 3-O-methylglucose (PubMed:12723603). May play a role at the early stage of seed development (Ref.5). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family."} | |
| {"protein": "MAGLPVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGESISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLISGNPQPVHVAGPGSGPNVSMNQQNPQAPQAQSLGGMHVNGAPPMMQASMPGGVPAPVQMAAAVGGPGPGSLAPAGVMQAQVGMQGAGPVPMERGQVPMQDPRAAMQRGALPTNVPTPRGLLGDAPNDPRGGTLMTVTGDVEPRAYLGPPPPPHQGPPMHHVPGHEGRGPPPHDMRGGPLAEPRPLMAEPRGPMLDQRGPPLDARGGRDPRGLDARGMEARAMEARGLDARGLEARAMEARAMEARAMEARAMEARAMEARAMEARGMDTRGPVPGPRGPMPSGIQGPNPMNMGAVVPQGSRQVPVMQGAGMQGASMQGGSQPGGFSPGQSQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP", "text": "FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localized with DDX1 in cleavage bodies."} | |
| {"protein": "MSDIEQRVKKIVSEQLGANEADVKNESSFVDDLGADSLDTVELVMALEEEFDCEIPDEEAEKITTVQQAIDYVNANLK", "text": "FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acyl carrier protein (ACP) family."} | |
| {"protein": "MKRLGSVQRKMPCVFVTEVKEEPSSKREHQPFKVLATETISHKALDADIYSAIPTEKVDGTCCYVTTYKDQPYLWARLDRKPNKQAEKRFKNFLHSKENAKEFFWNVEEDFKPAPECWIPAKEIEQINGNPVPDENGHIPGWVPVEKNNKQYCWHSSVVNYEFEIALVLKHHPDDSGLLEISAVPLSDLLEQTLELVGTNINGNPYGLGSKKHPLHLLIPHGAFQIRNLPSLKHNDLLSWFEGCKEGKIEGIVWHCSDGCLIKVHRHHLGLCWPIPDTYMNSRPVIINMNLNKCDSAFDIKCLFNHFLKIDNQKFARLKDIIFDV", "text": "FUNCTION: Functions as an RNA ligase, in vitro. The ligation reaction entails three nucleotidyl transfer steps. In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate. In step 2, the ligase-AMP binds to the nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated intermediate. In step 3, the RNA ligase directs the attack of the 3'-OH on the 5'- phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP. Exhibits selectivity for single-stranded RNA substrates and may not have nick-sealing activity on double-stranded DNA-RNA hybrids. May play a role in maintaining RNA integrity under stress conditions, for example in response to reactive oxygen species (ROS)."} | |
| {"protein": "MEVLPGLLRLLAALVVAERWARDTSGAESLGLWPLPFAVDISPRSLHLSPNNFFFGHSPTSKAGSSCEILQEAFRRYYDFIFGFYKWHQGSYQLCFGTELQQLQVHVESECDTFPSISSNESYVLHVKGPEALLRANTVWGALRGLETFSQLIYQDSYGTFTVNESEIIDFPRFPHRGILIDTGRHFLSVKTIFKTLDAMAFNKFNVLHWHIVDDQSFPYQSINFGVLSSKGSYSLSHVYTPNDVRMVIEYARIRGIRVMPEFDTPGHSRSWGKGQKDLLTPCYRKQVLSGTFGPINPILNTTYNFLSKFFKEISTVFPDEFIHIGGDEVDFDCWASNSEILQFMQEKGFSQISLNSNLCTVFKISNMISAMKKRPIVWQEAFDGRDKFMPGTVVQVWKIEDYKWEQSLITKAGFPVILSAPWYLDLISYGQDWKNYYEVEPQDFPGSDKERKRVLGGEACLWGEYVDATNLTPRLWPRASAVGERLWSHKDVRDIHDAYSRLTIHRCRMVRRGIAAEPLFTGYCNHEHRM", "text": "FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (By similarity). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity). SUBCELLULAR LOCATION: Lysosome Cytoplasmic vesicle, secretory vesicle, Cortical granule. SIMILARITY: Belongs to the glycosyl hydrolase 20 family."} | |
| {"protein": "MFQISNLLLAADFSSEVANNSAVGMIGSFIAAALLIVIPATAFLIFVSQKDSLNRTSTGRR", "text": "FUNCTION: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbX family. Type 2 subfamily."} | |
| {"protein": "MESLSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVLEEETRRSQQAARDKQSPNQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQISNLGSTETLEETPSGLQDKSALSGHKHLTVEELFGTSLPKEQPTVVGLESEEVEKLPGDASQKEPSSFLPFSFEPSGGGPQSENMGIRPAAHHSVQPEVTTPVLITPASITQSSEKQAPSYAIPLHPVLSPTLPAEASTAQAPPSLPRSTTMMQAVKTTPRQRSPLSSQPVPELSQASLAASQSPFRAPLNVTNTASTSLPSVDLLQKLRLTQQHDQIQTQSLGKGAVAPSFSPAAGQLATPESFIEPPPKTAAARASASLSNMVLAPLQSMQQNQDPEVFAQPKVLSSAIPVAGPALVTATTSAVSSVLLSPSVFQQTVTRSSDLERKASSPSPLTVGTSENQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL", "text": "FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity). Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body Nucleus Note=Co-localizes with NANOS3 in the processing bodies (By similarity). Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). SIMILARITY: Belongs to the DCP1 family."} | |
| {"protein": "MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM", "text": "FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans- signaling'. Alternatively, 'cluster signaling' occurs when membrane- bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable). FUNCTION: IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (Probable). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin- secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal- center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity). FUNCTION: Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability (PubMed:17075861, PubMed:12794819). Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF (PubMed:12794819). Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (PubMed:20823453). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis (By similarity). Mediates, through GLP-1, crosstalk between insulin- sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (Probable). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (PubMed:15124018). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily."} | |
| {"protein": "MTYAAEDFDYEGLPIGSPMYAHLLAGAFSGILEHSVMYPVDAIKTRMQMLNGVSRSVSGNIVNSVIKISSTEGVYSLWRGISSVIMGAGPSHAIYFSVLEFFKSKINASPDRPLASALAGACAITISDAFMTPFDVIKQRMQLPSRKYKSALHCATTVFRNEGLGAFYISYPTCIAMSIPFTAIQVATYDTCMSFLNPNAVYDPTSHIISGGLSGAIASSLTTPLDVVKTLLQTRGSSSIPEVRKCKGSLDVVRFIYNYGGIPSFFKGIRPRMVVAMPATAVSWAAYEAGKEILIRVSKTSQA", "text": "SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family."} | |
| {"protein": "MAEQHSTPEQAAAGKSHGGLGGSYKVIVYEMENFQGKRCELTAECPNLTESLLEKVGSIQVESGPWLAFERRAFRGEQYVLEKGDYPRWDAWSNSHHSDSLLSLRPLHIDGPDHKLHLFENPAFGGRKMEIVDDDVPSLWAHGFQDRVASVRAINGTWVGYEFPGYRGRQYVFERGEYRHWNEWDANQPQLQSVRRIRDQKWHKRGVFLSS", "text": "FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SIMILARITY: Belongs to the beta/gamma-crystallin family."} | |
| {"protein": "MSEIKLIVGLGNPGDKYADTRHNAGEWLINRLARQFHFSLTPESKFSGKTARTVINGNEIRFLVPTTFMNLSGKAISSLANFYRIKPEEILVIHDELDLPPGVAKIKQGGGHGGHNGLRDTIAQLGNNKNFYRLRVGIGHPGDKNLVSAYVLNKPSLTDWQLIDKALDEATSCVDILIKDGITKATNRLNAFKA", "text": "FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PTH family."} | |
| {"protein": "MNYQRSFEDLEFNAIKWWPQELSATVAEASVLPILISSQDLFISILKLSGTHPEQIFDVINAAQISANLFLKHLVVLADYGGEMIKRLGKEFQEIFPRMDSTLEYYMNYTFKGEQYTYIFKKLPIKGLDNSKLAIDGKAIIEIKPLSDLYRDMIMILLYGSTTEQFNLAGLEKCEIGTILGKNEIIYTYITQKYLYVSRITNGANTNSLGQIAQTYVCDILSKYLPNDYSVTRNGKILLSDLNSQDSTKTSFDILVEFADKKVGIEVSFQVTTNSTIERKAGQARDRQNRMHAHYYWIAYVIDGAGNFERSGAVRAICRYSDCTVAYSESEIAVLAAFIQEKFNA", "text": "FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGYRCC-3' and cleaves after G-1."} | |
| {"protein": "MLRREARLRREYLYRKAREEAERTAQERKDKVRRALEENRLIPTELRREALALQGSLEFDDAGGEGVTNHVDDEYRWAGVEDPKVMITTSRDPSSRLKMFAKELKLVFPGAQRMNRGRHEVGALVRACKANGVTDLLVVHEHRGTPVGLIVSHLPFGPTAYFTLCNVVMRHDIPDLGTASEAKPHLIMHGFSSRLGKRVSDILRYLFPVPKDDSRRVITFANQDDYISFRHHVYKKTNHRNVELTEVGPRFELKLYMIRLGTLEQEATADVEWRWHPYTNTAHKRVFLSAE", "text": "FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. SUBCELLULAR LOCATION: Nucleus, nucleolus."} | |
| {"protein": "MISDKSPPRLSRPSYGSISSLPGPAPQPAPCRETYLSEKIPIPSADQGTFSLRKLWAFTGPGFLMSIAFLDPGNIESDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEVCHLYYPKVPRILLWLTIELAIVGSDMQEVIGTAISFNLLSAGRIPLWDGVLITIVDTFFFLFLDNYGLRKLEAFFGLLITIMALTFGYEYVVAHPSQGALLKGLVLPTCPGCGQPELLQAVGIVGAIIMPHNIYLHSALVKSREVDRTRRVDVREANMYFLIEATIALSVSFIINLFVMAVFGQAFYQQTNEEAFNICANSSLQNYAKIFPRDNNTVSVDIYQGGVILGCLFGPAALYIWAVGLLAAGQSSTMTGTYAGQFVMEGFLKLRWSRFARVLLTRSCAILPTVLVAVFRDLKDLSGLNDLLNVLQSLLLPFAVLPILTFTSMPAVMQEFANGRMSKAITSCIMALVCAINLYFVISYLPSLPHPAYFGLVALFAIGYLGLTAYLAWTCCIAHGATFLTHSSHKHFLYGLPNEEQGGVQGSG", "text": "FUNCTION: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family."} | |
| {"protein": "MDNRSRSSSLASNVRIKSYSSLSSHSNSNSNSNGRSIEAPAVRRPSDNLLASESKKNELDQDYLNAINLQNHTKSSSCIGSALTGHVVPVKERPISNDSISTRNTDLFSSTSIYTKNSSSEDIFNDGDSNGTDDTSNITSKPENCNYLLNRKESIISEGQITNSTPTPAPTPIPGSNNIYTHHFAPSNPLLRSKTALTPSQQYKLHRVRSDSLLRNIINTNDRNLFNSSNLILQEHDDEDDDNEEVQIDVNNNSLNWNVPMASVSTTSFINSVTNDTDIPTHVKKSKRKNHPTGLYRASTYTSSYTTINGRHTPSYVPESPYDIALPTTPIPGISNVSDLEYMRDTSKSLSALYLQSSGKLSESRLAQRTRSSSLLPLEFKEASDHGMENLLLVSNHKRSFTTTTRPCWLPPKDPMEIKSHEKQISQHLDEVSVFELQRNNSFQDHVHNNKVNQDRLQTIIDRGLTRNSSLKILKEIIWENSLPDDLRLSIWNEILQSSDNLISNNYIESFDSINEIYSNLQFPRSKELEIMKLIDKNIKSKYGDNLEISENLLYLLKLKSLSQQGLVTGDELLFHHFIYDKSFKFSLNDVWTMVNLIQKTCFNDICKDFYDHQIVNGNKVFAQYIGNNEEFSKENNSTCLNYGTLWNILERMDHNIFMWILDIIIIHNSQNFKNSSISKSNINNEITWDIYRTKNVVVNYKILLSFTLLILLKYHFGFNNLSELSLLNDKQFCIPVASKNVQDEWHFTSMFIRKWNYYYKKF", "text": "FUNCTION: With SBE22, is involved in cell wall integrity and polarity processes like bud growth. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the SBE2 family."} | |
| {"protein": "MKLKDLIGKASIHKNKTIAVAHAEDEEVIRAVKLAAEHLSARFLLTGDSKKLNELTSSMQGHQVEIVHANTPEESAKLAVRAVHHKTADVLMKGNVPTSVLLKAVLNRQEGLRSASVLSHVAVFDIPDFDRLMFVTDSAMNIAPSLEELRQILQNAVHVAHAVGNNMPKAAALAAVETVNPKMEATVNAAALAQMYKRGQIKGCIVDGPLALDNAVSQIAAAQKKISGDVAGNADILLVPTIEAGNILYKSLIYFAKASVAAVITGAKAPIALTSRADSAENKLYSIALAICASEEYTH", "text": "FUNCTION: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate. SIMILARITY: Belongs to the phosphate acetyltransferase and butyryltransferase family."} | |
| {"protein": "MRMLLHLSLLALGASYMYAIPTEIPTSALVKETLTLLSTHRTLLIGNETLRIPVPVHKHHQLCTEEIFQGIGTLESQTLQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES", "text": "FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils. Acts also on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation (By similarity). Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB. Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-5 family."} | |
| {"protein": "MTVQRLVAAAVLVALVSLILNNVAAFTSNWVCQTLEDGRRRSVGLWRSCWLVDRTRGGPSPGARAGQVDAHDCEALGWGSEAAGFQESRGTVKLQFDMMRACNLVATAALTAGQLTFLLGLVGLPLLSPDAPCWEEAMAAAFQLASFVLVIGLVTFYRIGPYTNLSWSCYLNIGACLLATLAAAMLIWNILHKREDCMAPRVIVISRSLTARFRRGLDNDYVESPC", "text": "FUNCTION: Can influence paracellular permeability. Appears to be involved in cell-cell interactions through adherens. SUBCELLULAR LOCATION: Cell junction, adherens junction Cell membrane; Multi-pass membrane protein Note=Colocalizes with the beta-catenin adherins."} | |
| {"protein": "MPVEEPLATLSSIPDSSADQAPPLIADEFTLDLPRIPSLELPLNVSTKHSSIQKAIKMCGGIEKVKEAFKEHGPIESQHGLQLYLNDDTDSDGSKSYFNEHPVIGKRVPFRDESVILKVTMPKGTLSKNNNSVKDSIKSLKDSNKLRVTPVSIVDNTIKFREMSDFQIKLDNVPSAREFKSSFGSLEWNNFKSFVNSVPDNDSQPQENIGNLILDRSVKIPSTDFQLPPPPKLSMVGFPLLYKYKANPFAKKKKNGVTEVKGTYIKNYQLFVHDLSDKTVIPSQAHEQVLYDFEVAKKTKVYPGTKSDSKFYESLEECLKILRELFARRPIWVKRHLDGIVPKKIHHTMKIALALISYRFTMGPWRNTYIKFGIDPRSSVEYAQYQTEYFKIERKLLSSPIVKKNVPKPPPLVFESDTPGGIDSRFKFDGKRIPWYLMLQIDLLIGEPNIAEVFHNVEYLDKANELTGWFKELDLVKIRRIVKYELGCMVQGNYEYNKYKLKYFKTMLFVKESMVPENKNSEEGMGVNTNKDADGDINMDAGSQMSSNAIEEDKGIAAGDDFDDNGAITEEPDDAALENEEMDTDQNLKVPASIDDDVDDVDADEEEQESFDVKTASFQDIINKIAKLDPKTAETMKSELKGFVDEVDL", "text": "FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with TFC3 and TFC6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIIC subunit 5 family."} | |
| {"protein": "MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYADGYRRVFSNAGHALIAGQRVPVLGKTSMNTVIVDITSLNNIKPGDEVVFFGKQGNSEITAEEIEDISGALFTEMSILWGATNQRVLVD", "text": "FUNCTION: Amino-acid racemase that catalyzes the interconversion of L- lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers (Ref.1, PubMed:23118975). Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Periplasmic side Periplasm. SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily."} | |
| {"protein": "MANEEQSNTYSTESHQKKSFFQSLFGRFFQGELKNREELVEVIRDSEQNELIDQNTREMIEGVMEIAELRVRDIMIPRSQIVFIHTDQNLDSCLDTIIVSAHSRFPVITDERDNIAGILHAKDLLRFLRSNAEEFDLMPLLRPAVIVPESKRVDRMLKDFRSERFHMAIVVDEFGAVSGLVTIEDILEQIVGDIEDEFDEEEIVNIRQLSRHTYAVRALTDIEDFNQQFNTHFADEEVDTIGGVVMQAFGYLPKRGEEITIENIGFKVTSADSRRLIQLRITVTDEQLAEIEKAEELKED", "text": "FUNCTION: Plays a role in the transport of magnesium and cobalt ions. SIMILARITY: Belongs to the UPF0053 family."} | |
| {"protein": "MFSPCTVKEKRSTLRSVAPNPESSVIPPIPLPSRRYKTRHIDALCSLMHLCLLRKDYPRASRAFSLLLRSKSVDISKLWNIGLEILNKVNPEASSEYMERLIARYPARPSINNSYPNRNAEHFFPAYIMLLIQRQEYNKAMKLLDEYLLLPPYNQNPALHEYSGMLCFELAKEEASESERTKWIEKAKYNFSNAGIDVEL", "text": "FUNCTION: Subunit of a multiprotein complex essential for the initiation of rDNA transcription by RNA polymerase I. Binding to the DNA template is dependent on the initial binding of other factors. SUBCELLULAR LOCATION: Nucleus."} | |
| {"protein": "MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV", "text": "FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Single-pass type I membrane protein Cell projection, lamellipodium Cell projection, filopodium. SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted. SIMILARITY: Belongs to the SCF family."} | |
| {"protein": "MNFKYSILFICFVKVLDNCYAADDLTTLRNGTLDRGITPDCTFNEKDIELHVYSRDKRNGIILKKEILKNYDLFQKSQISHQIAILIHGFLSTGNNENFDAMAKALIEIDNFLVISVDWKKGACNAFASTNDVLGYSQAVGNTRHVGKYVADFTKLLVEQYKVPMSNIRLIGHSLGAHTSGFAGKEVQRLKLGKYKEIIGLDPAGPSFLTNKCPNRLCETDAEYVQAIHTSAILGVYYNVGSVDFYVNYGKSQPGCSEPSCSHTKAVKYLTECIKRECCLIGTPWKSYFSTPKPISQCKRDTCVCVGLNAQSYPAKGSFYVPVDKDAPYCHNEGIKL", "text": "FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (By similarity). May act as an allergen and induce hemolytic activity (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family."} | |
| {"protein": "MRIAGAIKFVVAVALFLLTFYVISQVFEIKSYTNLGNIFVRSAIDTVAHPTTKAPRYRCGISKVCPEKHFAFKIASGAANVVGPKICVDDNILMSGVKNNVGRGINTALVNGKTGALIETTYHDLWGGEVGPFIEFLKKIPDGTIVLMATYDDGATKLNDDARKRISELGSTLINVLAFRDNWVFVGGKGIKTKSPFEQHIKNNKDTNKYEGWPEVVEMEGCIPQKLNE", "text": "FUNCTION: Involved in retinal laminar formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FAM3 family."} | |
| {"protein": "MKIVRYIALFGILSGLAVACTPSTSVIPNDAIRLNQLGYYPNQEKIAVVDSGKVEEFVIWDAVSGEQVFVGKSLYTAKSAWSDKTRTTLDFSAVTTPGKYILKVNGASVTFLIKDSVLSPLADAALKSFYYQRTAMPIEEQYAGQWHRMAGHPDNHVLIHPSAASPDRPAGTIVSSSKGWYDAGDYNKYIVNSGYSIGLMQSIYQLFLDYFSRQKINIPESNNHTPDLLDEMQFNLDWMLTMQDPEDGGVYHKLTTPFFEGFVKPVDCKQQRYVVQKSVTAALDFAAVMAQSSRLFASYEEDYPGFSKRALLAAEKAYAWAEKHPEAYYNQNLLNQKYQPAIATGEYGDTHADDEFFWAASELYFSTGKEIYREEAIKKAPQIYTAPGWGNTFALGIFAWLQPGRELNEADRRFADSLKTELLKYADKVIEGAEQTPFHAPYGNDAKDFFWGCLAEKCMNQGVSLMYAYLQTGKDVYLTNAYRNMDYILGRNATGFCYVTGLGTKSPKHPHHRLSASDDIEDPIPGFLVGGPNPGQQDGAFYPTASPDESYVDTEDSYASNEVAINWNAALVALASSLDALAVYSVK", "text": "FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. May be superfluous in xyloglucan degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan- specific endo-beta-1,4-glucanase. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family."} | |
| {"protein": "MTGVVYAFPWNAPRSAIASSYLTYDQQHRRDRMFAALLHARKVLFLQPECVRFDVYRTAAVLEQNQGSQRANAFLISFCKKALPRLELVAKKYECSGINSNVSAAVFDGHFDTQLMQYLASRMVNMVARFNRLPDMSRADIDLLAADIANFIRAELADIDDTGFSELKTLYTWYMRAGFISLQFNVTPPKWERVTKKYFCEDEIAPAVMRMFNEVWWRGRLRRIAAAWREHLQIAVGNVSKKRHAYASKNCVTDWREQKRRTREFLKGLDLEDEEGNRISLIEKYDGSVANPAIRRCELMARIRGFENICNELGYVGEFYTLTAPSKYHATTKAGYRNSKWNGASPSDTQSYLTGLWARIRAKLHREEIRIFGIRVAEPHHDGTPHWHMLMFMLPEDVERVRLIIRDYAWEEDHYELRSDKAKKARFHAEAIDPEKGSATGYVAKYISKNIDGYALDGETDDESGELLKETAPAVSAWAARWHIRQFQFIGGAPVTVYRELRRMADPETARALSVEFAAVHDAAHYGRWADYVNAQGGPFVRRDDLQVRTLYEPRTEFNQYGEETVCIKGVYDASIGAGSPILTRLTQWKIVPKRAVDLAVDVKGASAPSRSSVNNCTGSESDPPILDLTKPLSRRERRELTNRLRKKKPTTRRKFIHGTDKQNVAITKTIDEIHSDNRHHNQPGRSPAPDGRW", "text": "FUNCTION: Endonuclease which induces a single-strand cut at or near ori. May act by forming a covalent link to the 5'side of the nick. SIMILARITY: Belongs to the phage GPA family."} | |
| {"protein": "MRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEGYQNTIVAGSLITKSNLHAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVADFTPKKEEEESQPAKKTYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTEKEEKEEARSKYKEAKESFQRFLENHEKMTSTTRYKKAEQMFGEMEVWNAISERDRLEIYEDVLFFLSKKEKEQAKQLRKRNWEALKNILDNMANVTYSTTWSEAQQYLMDNPTFAEDEELQNMDKEDALICFEEHIRALEKEEEEEKQKSLLRERRRQRKNRESFQIFLDELHEHGQLHSMSSWMELYPTISSDIRFTNMLGQPGSTALDLFKFYVEDLKARYHDEKKIIKDILKDKGFVVEVNTTFEDFVAIISSTKRSTTLDAGNIKLAFNSLLEKAEAREREREKEEARKMKRKESAFKSMLKQAAPPIELDAVWEDIRERFVKEPAFEDITLESERKRIFKDFMHVLEHECQHHHSKNKKHSKKSKKHHRKRSRSRSGSDSDDDDSHSKKKRQRSESRSASEHSSSAESERSYKKSKKHKKKSKKRRHKSDSPESDAEREKDKKEKDRESEKDRTRQRSESKHKSPKKKTGKDSGNWDTSGSELSEGELEKRRRTLLEQLDDDQ", "text": "FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus speckle Nucleus matrix Note=Colocalizes with AKAP8L in the nuclear matrix. SIMILARITY: Belongs to the PRPF40 family."} | |
| {"protein": "MNWLNQHKKAIILAASAAVFTAIMIFLATGKNKEPVKQAVPTETENTVVKQEANNDESNETIVIDIKGAVQHPGVYEMRTGDRVSQAIEKAGGTSEQADEAQVNLAEILQDGTVVYIPKKGEETAVQQGGGGSVQSDGGKGALVNINTATLEELQGISGVGPSKAEAIIAYREENGRFQTIEDITKVSGIGEKSFEKIKSSITVK", "text": "FUNCTION: Needed for both DNA binding and transport. It is absolutely required for the uptake of transforming DNA but not for binding. Its role in binding may be indirect. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Note=Localizes in a nonuniform, punctate manner in competent cells, unlike some other competence proteins is not localized to the cell poles (PubMed:16009133)."} | |
| {"protein": "MSHHKRRVYPQAQFGLAQAGQTGYQDVQQPGVLPSQANYQEPVPLVTPIQEVLNNQIDQTADSLHNMQLHNVPDFNQPLQGQLNGPQSPALYQNYNENGMNNYNAAFGNGGTSVKQVNQLYPIDLLSDLPPPIKDLGLPPPPINLSPDIMSVPSDKSNASPDYIRSTLNAVPKTNSLLKKTKLPFALVIKPYQHLNDDVNAPPLNEECLIVRCRRCRSYINPFAKFIEQGRRWRCNFCRLANDLPMQFDQSSIDTNIVNRLDRTEIKNAVMEYVAPKEYTVRPPPPSIYTFIIDVSQNAIKNGLFVSTIETLKQQLEYLPNRDNRTKISIILVDHALHILSIPADDVSNKFRILDVADIDEPYIPLPNSLVVSLSRCKQNVQLALEKIKQLFEINVSTKFALGPALRTAQKLIGGVGGKLIVISASLPNAGIGSLQRRNESGVSGTTKESSQLLSCQDSFYKTFTVECSKTQITIDLFLASDDYVDVATLSNLPRYTAGQTHFYPGYNASNISDFNKFTTEFSKHITMDISFETVMRARGSTGLKTSAFYGHFFNRSSDLCAFSTMPRDQSYVFDISIEDTITTDYCYFQVAVLLSLNNGQRRIRVITLALPTTQSISEVFACVDQQAVAAQITQRAVQKANSSSIDDARDLIQKTTLDILSTYKKELVVTNTGGVVPLKLSTNLRILPLLMHALMKHMAFRAGVVPSDHRAYSLNVLESVPIKSLITSIYPSIYSMHDMGDDCGYTDETGNVILPECINDTAILMEKYGLYLIDNGSELFLWVGGEAVPELLSDVFGVPEMSQVPVGKHDLFRVEGSQFNERVCNIIDQLRTSDDTTVYKTLYIVSGPTINDSFSQGTRELASLRMWAATAFVEDNIMKTLSYREFLEKMKKEVSK", "text": "FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily."} | |
| {"protein": "APKNIVLFGATGMTGQVTLGQALE", "text": "FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH- dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles (By similarity). SUBCELLULAR LOCATION: Cytoplasm."} | |
| {"protein": "SGHRHESXBSTBXASXSSKPCCBHCACTKSIPPQCRCSBLRLNSCHSECKGCICTFSIPAQCICTDTNNFCYEPCKSSHGPBBNN", "text": "SIMILARITY: Belongs to the Bowman-Birk serine protease inhibitor family."} | |
| {"protein": "MNSLVATPPVPPHFYETSCRSASYSMSSTNASVNRKRKAEDDCLPSDDTRMSASPSGSPALHPRPLAPRHLKRSRPNVSGRPLSLPRLMETLDTDALRSVLRSLCDRHPEIASEVMHTAPRPSVSAALEVLNNYQSTLQSSFPLGGNPSSDYAYNRVRQHLTNLLEALNDFTPHFLPPNESQPSTSLNYLDGATDIIHRLPRWTTPQHNLEKYAAYEEMSKAWCLVIREAAKRGGGIQLQYGGWDQKLAKHNETAGGKLQDAVNELNQSLGWIGGNVGNPSYPGGSNSQGDMSIRQQLMSGTYGAGLPLKVGPW", "text": "FUNCTION: Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cut8/STS1 family."} | |
| {"protein": "MAALRLLLGIDYGTKQIGVAVGQAITGQARELCTLKAQNGVPDWDKVQALINEWKPDAIVVGLPLNMDGTPSEMSARAEKFSRKLNGRFGVTVYTHDERLTTFEAKGERMARGGQKGSYRDNPVDAIAAALLLQGWLDEHPELLNV", "text": "FUNCTION: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YqgF nuclease family."} | |
| {"protein": "MAERDHYHTIDDPNVPCNFYDTVNLTGHTVFPNGSYDYYGTIVPAELVGTYDYIHSSLTERIEVREHVRGCVCKFKSCLNICCPWRQVFNSEVDGCIIDHSDNRTWPDPPMLNITFRNDSTILVNMFAQFAIQSFRPCPKMFSLQPETSHWDDYLLFENGSMLRVDDQQLIRKNEFCMVPTYVNESDMFYTIHPANCDMQDDNSTVKIINAYAMMFSIPFMMLTIAVYLLIPELRNQHGKSLVCYLVGLTVGYTSLCYVQLYQVDATGDACKVFGYTAYFFFMGAYMWLSVISFDLWHNFRGTRGINRFQEKKRFLFYSLYSWGIAVVFLAFTYIAQELTNLPAYLKPGIGDGVYCWLDMSNWAAMIYFYGPILVIVVANTIMFIMTAIKIHGVQREMARIIASENSTKNLRTEKDKFGLFLRLFLIMGITWLTELISYFVGSDKGWSKLFYISDLANAMQGFLIFMLFVMKKKVKHLITNRCSSVRDGSNQRQSQYSTKTTSSSVANLSLHEKPSVEKPLVISSSVDPQKTTIFR", "text": "FUNCTION: Involved in biological aging and stress response. Essential for adult survival (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily."} | |
| {"protein": "MQLSSTKPSSKTREPSTAQDIVTMQNILEKLYRAESISRQESQALFGAIIRGELEASQLAAALISMKVRGEHPDEIAGAATALLADAQPFPRPDYLFADIVGTGGDGTNSINISTASAFVAASCGLKIAKHGNRSVSSRSGSSDLLSAFGIKLDMSAQDSRQALDDLGVCFLFAPQYHLGFRHAMPVRQQLKTRTVFNVLGPLVNPARPPLALIGVYSPELVRPIAETLKVLGYQRAAVVHGGGMDEVAIHAPTQVAELNNGEIETYELTHRDFGLDTYSLSALQGGTPEENRDILASLLQGKGERAHAAAVAANVALLLRLFGQENLRQNAQQALEVIHSGQAYQRVIALSARG", "text": "FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase family."} | |
| {"protein": "HREEQARYIVKNKPVTMSCAASPATQIYFKCNGEWLHQKAHHIEEREDETTGRSVREVQTDVSRQQVEELFGLEDYWCQCVAWSAAGTSKSRKAYVRLAYLRKNFEQKPLGKYALLDHEVLLHCRPPDAIPQAEVEWLKSEEIIDPVIDQNFYITVDHNLIIKQTRLADSANYTCVAKNLVAKRRSSTATITVYVNGGW", "text": "FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the unc-5 family."} | |
| {"protein": "MGASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDLLRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKNLTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQREDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTETNKIWPHVYAFLQTKLPQRSQETSVTP", "text": "FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily."} | |
| {"protein": "MTDLSEKVRAWGRRLVVGAAAAATLPGLIGIAGGAATANAFSRPGLPVEYLQVPSAGMGRDIKVQFQSGGNGSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSVIMPVGGQSSFYADWYQPACGKAGCSTYKWETFLTSELPQYLASNKGVKSTGSAAVGISMSGSSAMILAVNHPNQFVYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKADAMWGPSSDPAWQRNDPSLQIPALVGNNTRLWVYCGNGTPSELGGANMPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFNANGTHSWEYWGAQLNAMKPDLQSALGASSGGGG", "text": "FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha- trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mycobacterial A85 antigen family."} | |
| {"protein": "MADLAKIEEQLSSLTLMQAAELVKMLEEKWGVSAAAPVAVAAVGAAAPAAEAVAEKTEFEVVLTAAGDKKVEVIKVVKDITGLGLIEAKKLVDEAPKPIKSNVKKAEADEIKGKLEAAGAKVELK", "text": "FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family."} | |
| {"protein": "MAGEQKPSSNLLEQFILLAKGTSGSALTALISQVLEAPGVYVFGELLELANVQELAEGANAAYLQLLNLFAYGTYPDYIANKESLPELSTAQQNKLKHLTIVSLASRMKCIPYSVLLKDLEMRNLRELEDLIIEAVYTDIIQGKLDQRNQLLEVDFCIGRDIRKKDINNIVKTLHEWCDGCEAVLLGIEQQVLRANQYKENHNRTQQQVEAEVTNIKKTLKATASSSAQEMEQQLAERECPPHAEQRQPTKKMSKVKGLVSSRH", "text": "FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF- type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CSN7/EIF3M family. CSN7 subfamily."} | |
| {"protein": "MEADGLGCAVCVLTGASRGFGRALAPQLARLLSPGSVMLVSARSESMLRQLKEELGAQQPDLKVVLAAADLGTEAGVQRLLSAVRELPRPEGLQRLLLINNAATLGDVSKGFLNVNDLAEVNNYWALNLTSMLCLTSGTLNAFQDSPGLSKTVVNISSLCALQPYKGWGLYCAGKAARDMLYQVLAAEEPSVRVLSYAPGPLDNDMQQLARETSKDPELRSKLQKLKSDGALVDCGTSAQKLLGLLQKDTFQSGAHVDFYD", "text": "FUNCTION: Catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sepiapterin reductase family."} | |
| {"protein": "MGFLFTPKHQKLVNQCYPPGRTPDKKPKGSETSYLLYYVNSRRPKLEKVSSYLVKRSTTDLNRRRSGNVSVTLELLAKIVENCNENMNIFIKDFIHIMTLVLNNNNFNNDPTIVGLIERVLEAICNHLDGSLVSGDSEFLELFKNFVTLYFKVANTKLNDTDLVLKGCLDFSKISNLGSIHQWSATAKNCVSIALTKFQERHPIYSEATIDSSFSEPGSPALKKKLTRTQTKVMGLDDVSNTGDYSILALNTFFNTTETDKLTIGLHALIEHLLETPNKELLQFICNGIPVQLRYIVILLFVRPLGTSSEKNMLLILKLISSLLTSAVSIIGLSVIDILRRLITVQLAKSDSTTVVKQIAVTIKDLNRKTYYKQQSSDMFAELSFKFIESGKPHHLELFQLDLDSLISVTSDQCLDLDLFGEFLPYVTDKTQLSKLLYPEAPHQVIFIRFFEKVSTLSKQDTEIAISTSFAYYKAASLLSGLAYYVNNNRPSDGYYAYHHHASKFLGLADYQTQVEFKRKDNDIFTKEDLLNYYSDAGSNIYSEKGRDILLVDHSDQNGTDIDQDTVRYSTPIPLPQISIPPTTTNGIGIKKSSPANDTYVTRSLKHNPVPNVKDLKNLVSSKKDKSNTKTLRGSQSVKSKVTNITFLLDELKNDGDEIKIADPDEEDIIGMEKQDLARSYSLRMNTISSTNSRTLIPSVENAEEHGDDFRDAHEDIEVSSSTRGRLFMV", "text": "SIMILARITY: Belongs to the EFR3 family."} | |
| {"protein": "MSEDIFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTGGRLYAHSLERIIPGFADQAPIERMITHEKLAFMTDNGAMTIDYCNGEDASASQVSYSVLRSKFDAWLMEQAEEAGAQLITGIRVDNVVQRDGKVVGVEADGDILEAKVVILADGVNSLLAEKLGMAKRVEASHVAVGVKELIELPKSVIEDRFQLQGNEGAACLFAGAPTDGLMGGGFLYTNETTLSLGLVCGLHHLKDAKKSVPQMLEDFKQHPAVAPLIAGGKLVEYAAHVVPEAGMNMQPELVGDGVLIAGDAAGMCMNLGFTIRGMDLAISAGEAAAKTVLSAMKRDDFSKQSLGEYRQHLDEGPMRDMRMYQKLPAFLDNPRMFTAYPEMAVSIARDLFTVDGSAPVPMRKKILRHAKKVGFINLMKDGLKGVTVL", "text": "FUNCTION: Could be part of an electron transfer system required for anaerobic carnitine reduction. SIMILARITY: Belongs to the ETF-QO/FixC family."} | |
| {"protein": "MSSRGGGVGGRRGGPGGASSVRGGERGRKRGRGALDAVEPRVPLPRGTGSGPGAGRDGAAAPVPALQPAEADVLSGEVETEMAAGMEAREGASSSSSASAPAVGEVEPPSRAVGALPPTSSKAVVLQARPGFGTVGTSCRVRANHFVVQLADKEIYHYDVAIAPELRSRERNRNIINELLRSHKKYLDGRRSPAYDGRKGMFTAGALPFTDREFVVKIANDPERGNQGEKEFKVTIKCAGAANLYMHSLKQFLAGTYPSQDRFSHKHLDIRILIVALNGGEDISATTFYKAQPVIDFALDYLNMNIRDAYSRFDQDGTRVSVVQYFNRQYSYSLKYINWPCLQAGSDSRPTYLPMEVCRIVKGQRYSRKLNECQVTRMLRLARETPEERENSILEIANENNYGNDYHAREFGIGVTNQLALVDARVLPAPMLKYHDSGQEKVCNPSIGQWNMNNKRMLNGGSINYWACLTFASCVRLAEVRTFCKELVRVCNSIGMQITGEPCVRIRQERQDHLDAAVRDIHRQSAEFLSQQGVIGQQLELLVIVLPDANATVFYGRIKRLCETELGVITQCCLARNVQNVGGRNTVLEDALHRRIPLLTDMPTMIFGADVTHPPAGEDSSPSIAAVVASMDWPEVSKYKCSVSSQSHREEIIADLFTEVKDSQNRLVYGGMIRELIESFRKANGSYKPGRIIFYRDGVSEGQFSQVLLSEMDAIRKACASIEEGYLPPVTFVVVQKRHHTRLFPEDHHARDQMDRSRNILPGTVVDTKICHPSEFDFYLCSHSGIQGTSHPTHYYVLFDENNFSADALQTLTYHLCYTYARCTRSVSIVPPVYYAHLAASRARHYLEEGSLPDHGSSSASAAGGSRRNDRGVPVKPLPEIKENVKQFMFYC", "text": "FUNCTION: Probably involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). SIMILARITY: Belongs to the argonaute family. Ago subfamily."} | |
| {"protein": "MAFFLIFLSSFFGLCIFCTALLRWNQVKYNQKNLPPGTMGWPLFGETTEFLKLGPSFMKNQRARYGSFFKSHILGCPTIVSMDSELNRYILVNEAKGLVPGYPQSMIDILGKCNIAAVNGSAHKYMRGALLSLISPTMIRDQLLPKIDEFMRSHLTNWDNKVIDIQEKTNKMAFLSSLKQIAGIESTSLAQEFMSEFFNLVLGTLSLPINLPNTNYHRGFQARKIIVNLLRTLIEERRASKEIQHDMLGYLMNEEATRFKLTDDEMIDLIITILYSGYETVSTTSMMAVKYLHDHPKVLEELRKEHMAIREKKKPEDPIDYNDYRSMRFTRAVILETSRLATIVNGVLRKTTQDMEINGYIIPKGWRIYVYTRELNYDPRLYPDPYSFNPWRWMDKSLEHQNSFLVFGGGTRQCPGKELGVAEISTFLHYFVTKYRWEEIGGDKLMKFPRVEAPNGLRIRVSAH", "text": "FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids biosynthesis (PubMed:15710611). Converts 6-deoxocastasterone (6- deoxoCS) to castasterone (CS) (PubMed:15710611, PubMed:9990098). May also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3- dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3- dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY), but not castasterone (CS) to brassinolide (BL) (PubMed:15710611). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family."} | |
| {"protein": "MEDDGGERSSFVAGLIENRAKEVGMAAFDLRSASLHLSQYIETSSSYQNTKTLLRFYDPSVIIVPPNKLAADGMVGVSELVDRCYSTVRKVVFARGCFDDTKGAVLIQNLAAEEPLALGLDTYYKQHYLSLAAAAATIKWIEAEKGVIVTNHSLTVTFNGSFDHMNIDATSVENLELIDPFHNALLGTSNKKRSLFQMFKTTKTAGGTRLLRANLLQPLKDIETINTRLDCLDELMSNEQLFFGLSQVLRKFPKETDRVLCHFCFKPKKVTEAVIGFENTRKSQNMISSIILLKTALDALPILAKVLKDAKCFLLANVYKSVCENDRYASIRKKIGEVIDDDVLHARVPFVARTQQCFALKAGIDGFLDIARRTFCDTSEAIHNLASKYREEFNLPNLKLPFNNRQGFFFRIPQKEVQGKLPNKFTQVVKHGKNIHCSSLELASLNVRNKSAAGECFIRTETCLEALMDAIREDISALTLLAEVLCLLDMIVNSFAHTISTKPVDRYSRPELTDSGPLAIDAGRHPILESIHNDFVSNSIFMSEATNMLVVMGPNMSGKSTYLQQVCLVVILAQIGCYVPARFATIRVVDRIFTRMGTMDNLESNSSTFMTEMRETAFIMQNVTNRSLIVMDELGRATSSSDGLAMAWSCCEYLLSLKAYTVFATHMDSLAELATIYPNVKVLHFYVDIRDNRLDFKFQLRDGTLHVPHYGLLLAEVAGLPSTVIDTARIITKRITDKENKRIELNCGKHHEIHRIYRVAQRLICLKYSRQTEDSIRQALQNLNESFTEERL", "text": "FUNCTION: Involved in meiotic recombination in association with MSH5. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation. SUBCELLULAR LOCATION: Nucleus Note=In pollen mother cells during meiosis, localizes to unsynapsed axes during leptotene and zygotene, but is not present on synapsed regions of zygotene nuclei. SIMILARITY: Belongs to the DNA mismatch repair MutS family."} | |
| {"protein": "MGQQLSWEEAEAAGEMDVAELQEWYKKFVVECPSGTLFMHEFKRFFKVTGNEEASQYVESMFRAFDKNGDNTIDFLEYVAALNLVLRGSLEHKLKWTFKIYDKDRNGCIDRLELLDIVEAIYKLKKACRAELDLEHQGQLLTPEEVVDRIFLLVDENGDGQLSLTEFIEGARRDKWVMKMLQMDINPGCWITQQRRRSAMF", "text": "FUNCTION: Stimulates two retinal guanylyl cyclase (GCs) GUCY2E and GUCY2F when free calcium ions concentration is low, and inhibits GUCY2E and GUCY2F when free calcium ions concentration is elevated (By similarity). This Ca(2+)-sensitive regulation of GCs is a key event in recovery of the dark state of rod photoreceptors following light exposure (By similarity). May be involved in cone photoreceptor response and recovery of response in bright light (PubMed:25673692). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment Note=Subcellular location is not affected by light or dark conditions."} | |
| {"protein": "MAEAAALVWIRGPGFGCKAVRCASGRCTVRDFIHRHCQDQNVPVENFFVKCNGALINTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPKHCFTSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEISENRKRQWPTKSQTDRGASAGKRRCFWLGMEGLETAEGSNSESSDDDSEEAPSTSGMGFHAPKIGSNGVEMAAKFPSGSQRARVVNTDHGSPEQLQIPVTDSGRHILEDSCAELGESKEHMESRMVTETEETQEKKAESKEPIEEEPTGAGLNKDKETEERTDGERVAEVAPEERENVAVAKLQESQPGNAVIDKETIDLLAFTSVAELELLGLEKLKCELMALGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPLKGKKK", "text": "FUNCTION: Inhibits translesion DNA synthesis by preventing monoubiquitination of PCNA, this is necessary to counteract damage due to ultraviolet light-induced replication stress (PubMed:27906959). SDE2 is cleaved following PCNA binding, and its complete degradation is necessary to allow S-phase progression following DNA damage (PubMed:27906959). FUNCTION: Plays a role in ribosome biogenesis by enabling SNORD3- and SNORD118-dependent cleavage of the 47S rRNA precursor (PubMed:34365507). Binds ncRNA (non-coding RNA) including the snoRNAs SNORD3 and SNORD118 (PubMed:34365507). FUNCTION: Plays a role in pre-mRNA splicing by facilitating excision of relatively short introns featuring weak 3'-splice sites (ss) and high GC content (PubMed:34365507). May recruit CACTIN to the spliceosome (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the SDE2 family."} | |
| {"protein": "MQDYKIKIENVVASTQIGENIDLNKISREIKDSEYKPKQFPGLVLRTKEPKAAALVFRSGKVVCTGSKSVEDARRAVKQIVKMLKEIGISVIDEPEVKVQNIVASADLGVDLNLNAIAIGLGLENIEYEPEQFPGLVYRLDNPRVVVLIFGSGKMVVTGGKSPEDARKAVERISEELRTLGLM", "text": "FUNCTION: General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation (By similarity). SIMILARITY: Belongs to the TBP family."} | |
| {"protein": "MVEKIPMTASGYKKLEDELSTLKVKRIDVIEEMRLAAMDKDMRENAPYHAAKEQRGQIEGRIKEIEHELKYADVSEYTDTNTSKVNMGSTVKLRDPKNGECCTYTLVSPKEIEPLKGKISASSPIGKAVFNRNKGEQIEIEVPSGTLQYIIEDISF", "text": "FUNCTION: Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. SIMILARITY: Belongs to the GreA/GreB family."} | |
| {"protein": "MGGAFSTSKPKPAAGEEGGESAVVAVHSKAKWDELWDAHKNTTKLVVIDFSASWCGPCKMMEPVFKEMAGRFTDVAFLKVDVDELAEVARTWRVEAMPTFVLARGGEEVGRIVGADKDELEKTINTLRSSSSSTATTT", "text": "FUNCTION: Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of a number of cytosolic enzymes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily."} | |
| {"protein": "MALFRMLFLCAVLVLLTSKEGMSYEEPENDEGVACTGQYAESFCLNGGTCRYIQSIGEYYCICNGDYTGHRCEKKQV", "text": "FUNCTION: Has both toxic and EGF activity. Its EGF activity consists of rounding cells (morphological change) and inducing tyrosine phosphorylation of the EGFR in A431 cells, but with a lower potency that human EGF. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the EGF domain peptide family."} | |
| {"protein": "MRRFVLIFVLLILPFQFSWAAAARYCQHEKATATWHLGHHEHRHQQPEGKTDAEKKPFVDTDCGVCHLVSLPFVYGQTQDVLIANRVEVTDTQHSSEFSSLNARAPDRPQWQRLA", "text": "FUNCTION: Component of the czc cation-efflux system that confers resistance to cobalt, zinc and cadmium. May have a regulatory function. SUBCELLULAR LOCATION: Periplasm."} | |
| {"protein": "MREKYLLHCPGCGRLFPDNYTLDCPLGCNALLRTVYAEHRLTLRDLPGIFRYSSWLPIEGHLRIDAGPVSYASEGLARELGLSNLTVTFSGYWPERGGRMETCSFKELEAQPTVLRLGEKGAGVLQISSAGNTGRAFCQVSALTGAPVVVVVPASAADRLWTTVPAPNVCLITVEGDYSDSIAFGREVCSLPGIVPEGGAKNVARRDGMGTVMLDAALFAGRLPDAYFQAIGSGTGGIAAWEAAERLVADGRFGSRLPTLHLSQNLPFVPMVRAWEAGRREIVPEVDMPDAEASIVRVSADVLTNRHPPWEVRGGVYDALAASGGRMYAVANDDTRSAGRLFEATEEIDLDPAAAVAVASLIRAAEEGFIGPDDHILLNVTGGGYARAAEDLDRYPVEPYLRVRAGEAFAGDVRDAVRGWLAEQEVVVRA", "text": "FUNCTION: Specifically catalyzes the beta-elimination of phosphate from L-phosphoserine and the beta-addition of sulfite to the dehydroalanine intermediate to produce L-cysteate. SIMILARITY: Belongs to the threonine synthase family. Cysteate synthase subfamily."} | |
| {"protein": "SCKVPFNECKYGADECCKGYVCSKRDGWCKYHIN", "text": "FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 50 (Jztz-F7) subfamily."} | |
| {"protein": "MIEPLDSPASDSDFLDYPSALGNCTDEQISFKMQYLPVIYSIIFLVGFPGNTVAISIYIFKMRPWRGSTVIMLNLALTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFGFHFNLYSSILFLTCFSLFRYVVIIHPMSCFSIQKTRWAVVACAGVWVISLVAVMPMTFLITSTTRTNRSACLDLTSSDDLTTIKWYNLILTATTFCLPLVIVTLCYTTIISTLTHGPRTHSCFKQKARRLTILLLLVFYICFLPFHILRVIRIESRLLSISCSIESHIHEAYIVSRPLAALNTFGNLLLYVVVSNNFQQAFCSIVRCKASGDLEQGKKDSCSNNP", "text": "FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family."} | |
| {"protein": "MGSSILTNRSAMTALQTLRNIDNNLDKSKDRISTGLRIGSASDNTAYWSISSMMKHDSNTMSAVVDAINLGREQVNVAATAVNLTKESLDDIQKSMVSAREKSDDDIMKIQDSIKGNMQNISNAIQSAAFGGKNILSNGGEKVGIAAGYRREGSAVYVDMIEVGGAELNFGVMGPDGTIDMTQGILKGVFGKSDKDIDAGIKTFTEAADKQKGLEDALAKAEAAVAANPNDEAAKTALEEAKKAVEDNKEDWTKAQSDFKVVADSMTLNDFVQMQGVGGLPSVAQSIILNSVQKTVRHAVDVTLTAGSKIGSAVNQVDSQLNFVKRLLDNIEAGIGALVDADMNAESAKLSALQVQQQLGIPRLFLLQIRAARIF", "text": "FUNCTION: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Flagella are an important component in the invasiveness of B.bacilliformis. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the bacterial flagellin family."} | |
| {"protein": "MSRQLSRARPATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFLYSDGQSETILGGLGLRMGSSDCRVKIATKANPWIGNSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSAPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYSATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGTQWAEIYRNHFWKEHHFEGIALVEKALQAAYGASAPSMTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAWHLFAHECPNYFI", "text": "FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity). SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily."} | |
| {"protein": "MESKVEQGVKNLNMENDHQEKEEKEEKPQDANKREPVVALPFEAGEYYVPRGSRRRFRVRQPIAHYRWDLMHRVGEPQGRMREENVQRFGEDMRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP", "text": "FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the BEX family."} | |
| {"protein": "MRSSKNVIKEFMRFKVRMEGTVNGHEFEIEGEGEGRPYEGHNTVKLKVTKGGPLPFAWDILSPQFQYGSKVYVKHPADIPDYKKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGCFIYKVKFIGVNFPSDGPVMQKKTMGWEASTERLYPRDGVLKGEIHKALKLKDGGHYLVEFKSIYMAKKPVQLPGYYYVDSKLDITSHNEDYTIVEQYERTEGRHHLFL", "text": "FUNCTION: Thought to play a role in photoprotection of the coral's resident symbiont microalgae's photosystems from photoinhibition caused by high light levels found near the surface of coral reefs. In deeper water, the fluorescence may be to convert blue light into longer wavelengths more suitable for use in photosynthesis by the microalgal symbionts. SIMILARITY: Belongs to the GFP family."} | |
| {"protein": "MITAADFYHVMTAMVPLYVAMILAYGSVKWWRIFTPDQCSGINRFVALFAVPLLSFHFISTNNPYTMNLRFIAADTLQKLMVLAMLTAWSHLSRRGSLEWTITLFSLSTLPNTLVMGIPLLKGMYGEFSGSLMVQIVVLQCIIWYTLMLFMFEYRGARMLITEQFPDTAANIASIVVDPDVVSLDGRRDAIETETEVKEDGRIHVTVRRSNASRSDIYSRRSMGFSSTTPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMVGRSSNFGAADAFGVRTGATPRPSNYEDDASKPKYPLPASNAAPMAGHYPAPNPAVSSAPKGAKKAATNGQAKGEDLHMFVWSSSASPVSDVFGGGAPDYNDAAAVKSPRKMDGAKDREDYVERDDFSFGNRGVMDRDAEAGDEKAAAAAGADPSKAMAAPTAMPPTSVMTRLILIMVWRKLIRNPNTYSSLIGLIWSLVCFRWNFEMPAIVLKSISILSDAGLGMAMFSLGLFMALQPHIIACGNKVATYAMAVRFLAGPAVMAAASFAVGLRGTLLHVAIVQAALPQGIVPFVFAKEYSVHPSILSTAVIFGMLIALPITLVYYILLGL", "text": "FUNCTION: Acts as a component of the auxin efflux carrier. Seems to be involved in the polar auxin transport which may promote adventitious root emergence and control tillering. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family."} | |
| {"protein": "MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH", "text": "FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells. SUBCELLULAR LOCATION: Host cytoplasm Host cell membrane; Peripheral membrane protein; Cytoplasmic side Virion Note=In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presumably via the interaction with Pr55Gag precursor. Incorporated in virions at a ratio of approximately 7 to 20 molecules per virion. SIMILARITY: Belongs to the primate lentivirus group Vif protein family. SIMILARITY: Belongs to the primate lentivirus group Vif protein family."} | |
| {"protein": "MEGPSLRGPALRLAGLPTQQDCNIQEKIDLEIRMREGIWKLLSLSTQKDQVLHAVKNLMVCNARLMAYTSELQKLEEQIANQTGRCDVKFESKERTACKGKIAISDIRIPLMWKDSDHFSNKERSRRYAIFCLFKMGANVFDTDVVNVDKTITDICFENVTIFNEAGPDFQIKVEVYSCCTEESSITNTPKKLAKKLKTSISKATGKKISSVLQEEDDEMCLLLSSAVFGVKYNLLAHTTLTLESAEDSFKTHNLSINGNEESSFWLPLYGNMCCRLVAQPACMAEDAFAGFLNQQQMVEGLISWRRLYCVLRGGKLYCFYSPEEIEAKVEPALVVPINKETRIRAMDKDAKKRIHNFSVINPVPGQAITQIFAVDNREDLQKWMEAFWQHFFDLSQWKHCCEELMKIEIMSPRKPPLFLTKEATSVYHDMSIDSPMKLESLTDIIQKKIEETNGQFLIGQHEESLPPPWATLFDGNHQMVIQKKVLYPASEPLHDEKGKKRQAPLPPSDKLPFSLKSQSNTDQLVKDNWGKTSVSQTSSLDTKLSTLMHHLQKPMAAPRKLLPARRNRLSDGEHTDTKTNFEAKPVPAPRQKSIKDILDPRSWLQAQV", "text": "FUNCTION: May play an important role in lymphopoiesis."} | |
| {"protein": "MQPDRNLLADLDHIFVDRSLGAVQVPQLLRDAGFRLTTMREHYGETQAQSVSDHKWIAMTAECGWIGFHKDANIRRNAVERRTVLDTGARLFCVPRADILAEQVAARYIASLAAIARAARFPGPFIYTVHPSKIVRVL", "text": "FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. The cognate antitoxin is VapB45."} | |
| {"protein": "MAKKEVVKIAKLQFIAGQAKPGPSLAGVGINMPEFTRQFNEQTRDRGNEPVPVEITAYKDKSFDFRLFTAPASFKILQAIKAKSGSANSKTNIIGTLTLAQLEEIAKYKLPDLNTDDYKVAMHTIAGTAKNMGVLVEGWDDVKKAKEEAKAAKLAQLKAEAKEAALKEAEKELVDSKGKEVEVKLVGEEEQSESENN", "text": "FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL11 family."} | |
| {"protein": "MGKVGNIEHIEERAETELMPPSMYKVILNNDDYTPMDFVIEVLQLFFNKNEQEATDIMLAIHHQGKGICGVFPFGIAETKVAQVNQFARQNQHPLLCSLEKA", "text": "FUNCTION: Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation. SIMILARITY: Belongs to the ClpS family."} | |
| {"protein": "MNGKLYALSTGPGAPDLITVRAARILGSLDILYAPAGRKGGDSLALSIVRDYLGEQTEVRCCHFPMSADGAEKEAVWNEVAAALTAEVEAGKQVGFITLGDAMLFSTWIFLLQRIGCPEWLEIVPGVTSFAAIAARAKMPLAIERQSLAVISCTAPEAEIAQALQQHDSLVLMKVYGRFARIKALLAQAGLLECALMMSEATLPGEQCWRHLHEVNDDRPLPYFSTILVNKQWEYAE", "text": "FUNCTION: Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway. SIMILARITY: Belongs to the precorrin methyltransferase family."} | |
| {"protein": "MFPNSILGRPPFTPNHQQHNNFFALSPSLYSHQQLIDAQFSFHNADLSRAVSLQQLTYGNVSPIQTSTSPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTIVNHIVPLSDERRYSMSPLFHTHYVPDIVRCVPPFREISILEPREITLPEAKDKLSQQILELFEACQQQVSDLKKKELCRTELQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHDINDASRGTLSSYSLVLMVLHYLQTLPEPILPSIQKIYPESFSPSIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNRKDLNSILPLRAAILKR", "text": "FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 subfamily."} | |
| {"protein": "MSLSSLDAVLSLIATSSTLDQDSAKVPQCQVCKRKFANQKTLRTHMKHITCRPGRSNVVNHKFRCENCEKQFTNKPNLKRHQITHSGSKSKKCSTCQRTFFREDQLQRHLHNHLKERSHFDCPVLNCSMQFVFYEGVENHLVNHHHFSYSESAPCGKCHKLFGSPRHLLVHYHFDHKEALRSSAPAPTSSARLSPITVSTSGSPRAQLAISPQEKPPQKLSINLGTSPMIEEFCEQNSATLPNTDQQLSPTLSPNEPRFRNLITSEPTPSFECKHCTIKFHDATMSIMHNALHAPGSPFKCAICGAECGNKIVFTMHIITASHDFGGIGT", "text": "FUNCTION: Together with ehn-3, may play a role in gonadogenesis. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family."} | |
| {"protein": "MVITLLNLNKKHYLLILFFILLNGCSIDKNIILNKKQKQHKIFNLPITHTSKETHNFNYQDNKQSNNNYLEPLFEDYKPRNVGDILTIILQENTSASNSVSNNSIHNGNSNFDIDIGNARAFDDPNGILNKIELNSSIKNNFLGKGSSSANNTFVGLITVIVDRILPNGNLEVSGSKNITINDGIEKICFYGIVNPHTISKNNSVLSTKVANTNITYISSGPINIGSKINWLQRLFVSLFTLSK", "text": "FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family."} | |
| {"protein": "MMQSHIDFALATPEILLLVLALAVLLIDAVSSHPDRKTTYVLSLATLAILTVVSLFQWSNGVSGKTFNGMYVTDSFSHLLKITSYIAVAVTLIYGRVYAQSRDMLRGGELYVLTLLALLGQMVMISAGSLVSVYLGLELMSLALYALIALRRDDVVATEAAMKYFVLGALASGFLLYGMSMVYGSTGHLDLAEISRVIGSGQAKELPLVFGIVFLVAGLAFKLGAVPFHMWVPDVYQGSPTAVTLILGGAPKLAAFAMTLRLLVDGLHGLAADWQSMLMILAVLSLAIGNLTAIVQTNFKRMLAYSTISHMGFVLLGLASGVVVGKAEAASAAYGASLFYMITYVLTTLASFGIVLLLSRQGFECEQIDDLKGLNRRSPWHALIVLLLMFSLAGIPPLVGFYAKLAILQAVIESGHVALAVVAVLFSLIGAFYYLRVVKVVYFDEPVAEDAPLSATCVQRGLLSVNGALILILGILPGGLMALCVQVIKTSFAGL", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family."} | |
| {"protein": "MSAPAQNNAEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWDTAGQEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVASPALAPPEVQVDEQLMHQYQQEMDQATALPLPDEDDADL", "text": "FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Not essential for cell viability. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family."} | |
| {"protein": "MKEGRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM", "text": "FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family."} | |
| {"protein": "MEYEAKKGKKGFVSPIRRLVFPKAARQAAFRSSVSRRPLHSMPLYPPDYLIDPHILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTPEQDSILSLSARCLLLTWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGMDGSPGGSGRDPGPPGAAPEKRRVGTAERRHTICSLDWRVAWGGGAGAEARAAGGGGSLERQRAGARASGSWERRQTFSGSWERRHAGGGAGKPGGSWERRQASGGVGGSWERRHPGPNPLDPQNHSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYRSTPKRPWLSSCTMAPRTHLKRATVAHPHRLSTAPTAAVSTTAAGPSSSYRITWSRCGVSWVLLRSSSLHCCYETIVWGCLSRTTVQVCRNSMGTDGSSFSLECGPSSQIRTSATSRASWRVWVSARAESSLTALAASSAA", "text": "SIMILARITY: Belongs to the CCM2 family."} | |
| {"protein": "MIEPSIIPVLVENTEEKTFKFQPGQVSQWLTGQGLQHQILEPDLLGVELIGVEPSELQKIAEALKSNGFDYLQCQGGYDEGPGGRLVSFYHLIKLGTIADHYLTPNTLPPNSILKEVRLKVFLLRDGNLSVPSLYSIFRGSDWQERETFDMFGISYEGHPHPKRLLMPEDWKGYPLRKDYIQPDFYEMQVAY", "text": "FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 30 kDa subunit family."} | |
| {"protein": "MEPTPEMKRNRLPSMNFEAEILADPHDNSELYVIPSMRSLTAEEYVEAFQSFLDHSTEHQCMDEFNKEVMPHIMAGLGNGKSTINILGVGSGTGEQDLKMIQILQAAHPGVLINNEIIEPNPQHVAAYKELVNRAPDLQGVSFTWHQLTSSEYEQQVKEKNTHKKFDFIHMIQMLYRVEDIPNTIKFFHSCLNHQGKLLIIILSDSSGWASLWKKYRHCLPSTDSGHYITSDSITAVLRKLGIKYHVYEFPSGWDITECFIEGDPAGGHMMDFLTGTKNFLGTAPAALRSRLQEALCQPECSSRKDGRVIFCNNLSMIVAES", "text": "FUNCTION: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family."} | |
| {"protein": "MESDCQFLVAPPQPHMYYDTAAAAVDEAQFLRQMVAAADHHAAAAGRGGGDGDGGGGGGGGGGERKRRFTEEQVRSLETTFHARRAKLEPREKAELARELGLQPRQVAIWFQNKRARWRSKQIEHDYAALRAQYDALHARVESLRQEKLALAAQVDELRGKLNERQDQSGSCDGGGAEGDDDDKRNSVMNASSSGLVEEDYVSCLAVPVVDVSEDGSAACGGSSYEYDHHLDYLGGGQLPDPFCGMPDLWETWPMVEWNAVA", "text": "FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class I subfamily."} | |
| {"protein": "MASSETQPRFGQSVKGLLSDKVTSCSGDVIALTRQVLKGSRSQELLSQAARNMVIQEDAILHSEDSLRKMSIITTHLQYQQEAIQKNVEHSKNLQDQLRHLMK", "text": "FUNCTION: As part of a BORC-like complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, this complex may couple lysosomes to microtubule plus-end-directed kinesin motor. SUBCELLULAR LOCATION: Lysosome membrane. SIMILARITY: Belongs to the BORCS7 family."} | |
| {"protein": "MPTMGAEMNTRNMRYILLTGLLPMASAFGETALQCAALTDNVTRLACYDRIFAAQLPSSAGQEGQESKAVLNLTETVRSSLDKGEAVIVVEKGGDALPADSAGETADIYTPLSLMYDLDKNDLRGLLGVREHNPMYLMPLWYNNSPNYAPGSPTRGTTVQEKFGQQKRAETKLQVSFKSKIAEDLFKTRADLWFGYTQRSDWQIYNQGRKSAPFRNTDYKPEIFLTQPVKADLPFGGRLRMLGAGFVHQSNGQSRPESRSWNRIYAMAGMEWGKLTVIPRVWVRAFDQSGDKNDNPDIADYMGYGDVKLQYRLNDRQNVYSVLRYNPKTGYGAIEAAYTFPIKGKLKGVVRGFHGYGESLIDYNHKQNGIGIGLMFNDLDGI", "text": "FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein Note=One of the very few enzymes located there. SIMILARITY: Belongs to the phospholipase A1 family."} | |
| {"protein": "MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKKADAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRSAGWIIPMGILRPYLSWTESLEPLQGAVAKFFSASCVPCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKECHLAQVPSHAVVARSVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLLFKDSALGFLRIPSKVDSALYLGSRYLTTLKNLRETAEEVKARYTRVVWCAVGPEEQKKCQQWSQQSGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGKCGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRAAHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR", "text": "FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation. FUNCTION: Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). SIMILARITY: Belongs to the transferrin family."} | |
| {"protein": "MSAQTGSAAAIGDKGKGKSAAEPQDVTMGEGGDDSSSEEEVDDDAPPPAEEVEEEASDNEIDKSNIIQGRRTRGKQIDFAAAAKDLPADDDEDEDDDFQSEGEEDDEMGGN", "text": "FUNCTION: Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CHZ1 family."} | |
| {"protein": "MLQALLDSKDFLALTLAHPEQFDSEFSFRLGDHTQVEVWDTGVIVFEPAQNEGKDVVLSCGVHGNETAPIELCNGLIKQLLQQKIIAKQRTLFLIGNPLAINNGTRIIDENMNRLFSGEHSNPPGLVNPERVRAKKLEAYIDRFYTAVADGRQRIHYDLHTAMRASKHEKFAIYPYRPGRAFSGEQIMFLAASGVDTVLFHHEPTTTFSYFSSERYGADAFTIELGKVYPMGQNDMTRFIATHEMFMRLITAKPLELDAFDADKVNLYQVCRVINKHFDDFEFTFATDVENFRSFPKGFVLAREGGQEIKVEHEFESVVFPNAKVPIGNRTVICLIPAVNADVR", "text": "FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily."} | |
| {"protein": "MDSVDRLKTYLATYDNLDSALQDANESEERREDKYLQDLFIEDQGDKPTPSYYQEEESSDSDTDYNAEHLTMLSPDERIDKWEEDLPELEKIDDDIPVTFSDWTQPVMKENGGEKSLSLFPPVGLTKIQTEQWKKTIEAVCESSKYWNLSECQILNLEDSLTLKGRLMTPDCSSSVKSQNSVRRSEPLYSSHSPGPPLKVSESINLWDLKSTEVQLISKRAGVKDMTVKLTDFFGSEEEYYSVCPEGAPDLMGAIIMGLKYKKLFNQARMKYRL", "text": "FUNCTION: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the vesiculovirus protein P family."} | |
| {"protein": "MKKNFRVKREKDFKAIFKEGTSFANRKFVVYQLENQKNHFRVGLSVSKKLGNAVTRNQIKRRIRHIIQNAKGSLVEDVDFVVIARKGVETLGYAEMEKNLLHVLKLSKIYREGNGSEKETKVD", "text": "FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family."} | |
| {"protein": "MVFGQVVIGPPGSGKTTYCNGMSQFLSLMGRKVAIVNLDPANDALPYECGVNIEELIKLEDVMSEHSLGPNGGLVYCMEYLEKNIDWLESKLKPLLKDHYILFDFPGQVELFFIHDSTKNVLTKLIKSLNLRLTAVQLIDSHLCCDPGNYVSSLLLSLSTMLHMELPHVNVLSKIDLIGSYGKLAFNLDFYTDVQDLSYLEHHLSQDPRSAKYRKLTKELCSVIEDYSLVNFTTLDIQDKESVGDLVKLIDKSNGYIFAGIDASVVEYSKIAIGQTDWDYNRVAAVQEKYMEDEEIQD", "text": "FUNCTION: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition (PubMed:17419841). Is crucial for normal development of the plant (PubMed:28475733). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, phragmoplast Note=During interphase, mainly expressed in the cytoplasm and weakly in the nucleus. Associated with microtubules during cell division. SIMILARITY: Belongs to the GPN-loop GTPase family."} | |
| {"protein": "MAHLLEKTRKITSILKRSEEQLQDELPYNAITRQLADIIHCNACIINSKGRLLGYFMRYKTNTDRVEQFFQTKIFPDDYVQGANMIYETEANLPVEHDMSIFPVESRDDFPDGLTTIAPIHVSGIRLGSLIIWRNDKKFEDEDLVLVEIASTVVGIQLLNFQREEDEKNIRRRTAVTMAVNTLSYSELRAVSAILGELNGNEGKLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVLISDIFEEVKKRDY", "text": "FUNCTION: DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CodY family."} | |
| {"protein": "MLQMPKLNEIPPGRGGPGEPWGEGRWAGPTGPEAARPARGARGQARGARARWDSWEHSRLPTHPGPGWDQCSPSFLCAPSSQKLIMESKDEVSDSDSGIILQSGPDSPVSPMKELTNAVRKQQRALEARLEACLEELRRLCLREAELTGTLPAEYPLKPGEKAPKVRRRIGAAYKLDEWALHREDPLSSLERQLALQLQITEAARRLCAEENLSRQARRQRKHAALQEEKKLRDLQRCLGDRRRNSEPPPTTVPSLGRELSASDDSSLSDGLLLEEEDSQAPKPPPESPAPPSRPLPPQSLEGLQPTGPESGGQERAPIQNSPWKETSLDHPYEKPRKSSELSSESSSPATTPQDQPNPSSLWVLDAASYHVVPIRNVPGQRQGRTSAPATPEMQGRRGQSQSLRVDSFRAGAEGRGRSAFPRRRPTHYTVTVPDSCFTPGKPPLPHPACHSCSEDSGSDVSSISHPTSPGSSSPDISFLRPLCLPEPPRHRGAWGPACGRELAPHYSKLLLPAGYFPTGRYVMVAEGHLPPGEWELCRAAVGAAYDEEGAPLRYQRLVPSHSRIVRTPSLKDSPAGRGLSKAAVSEELKWWHERARLRSSRPHSLDRQGAFRVRSLPPGRESFGRASGPRTQVPPVYVLRRSTDGAPVQVFVPENGEIISQV", "text": "FUNCTION: Expressed in peripheral macrophages and intestinal myeloid- derived cells, is required for optimal PRR (pattern recognition receptor)-induced signaling, cytokine secretion, and bacterial clearance. Upon stimulation of a broad range of PRRs (pattern recognition receptor) such as NOD2 or TLR2, TLR3, TLR4, TLR5, TLR7 and TLR9, associates with YWHAQ/14-3-3T, which in turn leads to the recruitment and activation of MAP kinases and NF-kappa-B signaling complexes that amplifies PRR-induced downstream signals and cytokine secretion (By similarity). In the intestine, regulates adherens junction stability by regulating the degradation of CYTH1 and CYTH2, probably acting as substrate cofactor for SCF E3 ubiquitin-protein ligase complexes. Stabilizes adherens junctions by limiting CYTH1- dependent ARF6 activation (PubMed:29420262). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Translocates to the nucleus upon NOD2 stimulation."} | |
| {"protein": "DTHGLPIERAVEKELSKKKIRKESLPKTEFRKLCREYANRYVNIQKEEFIRLGVLGDWENPYLTMSPEYEATEIRELGKFFEKGLAYRSKKPVYWCIYDKTAEGQAEVEYYEKEDPSIYVKFPLKKEIEGKKAYAVIWTTTPWTLPANLGIMVKEDADYSLVEVEGEVWIVAKELLENFFKNIGKTYTRVLKDVKGRDLVGLEYEHPFVDRDELKGYLSEETLKNMWRIYPSEFVSLDTGTGLVHMAPGHGQEDYTVGKRYNLEPYAPLDDSGRFVEPAPEFIRGVRVFDANKLIIALLKEKGYLVHEARIRHSYPHCWRCKNPVIFRATPQWFIGMDIEYEGKTLSGESLEEIEKVKWIPEYGKNRIKSMVENRPDWCISRQRFWGVPITVFYCENCGEVIKDKEVFERIASLVEKHPGGTDVWFEKSPEEILPEGYKCPKCGGTSFRKEEDILDVWFDSGCSHASVIRPLGFEKADLYLEGSDQHRGWFQASLLESVGSYGEAPYRSVLTHGFIVDEQGRKMSKSLV", "text": "FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily."} | |
| {"protein": "MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC", "text": "FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Virion Secreted Host Golgi apparatus membrane Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. SIMILARITY: Belongs to the lentivirus primate group Nef protein family."} | |
| {"protein": "MSIRVGQKAPDFTATAVFDQEFGTIRLSDYLDKRYVVLFFYPLDFTFVCPTEITAFSDRFKEFKELSTEVLGVSVDSEFSHLAWTQIDRKSGGLGELEYPLVSDLKKEISSSYNVLTEDGVALRALFIIDKEGIIQHSTVNNLSFGRNVDEALRTLQAIQYSQENPDEVCPVNWKPGSKTMKPDPVGSKVYFEAI", "text": "FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily."} | |
| {"protein": "MSLRLLIPLLFLPGLALADHRPCPDWPAQRARAEVSQLLKTLSHWDDHYHRQGVALVADELYDQSRQHLRHLQGCFDLASNDAPLATARGQVPHPVPHTGVDKLRDEPAVQRWLQGRQGMWIQPKVDGVAVSLVYQQGQLTQLLSRGDGVLGHDWSRHIPQLGRIVRQLPQPLDTVFQGELYWRLADHVQAEAGSANARGIVAGLLARKQLSDEQGSGIGLFVWDWPAGPGSQAERLAQLTALGFIDSQRFSVAIEGFDAAAHWRQHWYRTALPFATDGVILRQDARPPAQRWRAQAPYWIAAWKYPFSQALAQVRDIHFRIGRTGRITPLLQLEPIQLDDRRISQVSLGSLARWTQLDIRPGDQVAVSLAGLTIPRVESVVHRSPLRAPVLVPDPADHHLLSCWQASPACQEQFLARLAWLGGNKGLDMAGVGSGVWHQLVESGKVATLSDWLELTREDLLEVPGIAQARAERLLQAFSLGRRQPFERWLRGLGLPAPSHFSPGADWSALASRNIEQWLAEPGVGAVRAAQLQAFLSHEQVQALARRLRAHEIEGF", "text": "FUNCTION: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB subfamily."} | |
| {"protein": "MADKEAAFDDAVEERVINEEHKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPNDDAQFDASHYDSEKGEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIATKTPSSDVLVFDYTKHPSKPDPSGECNPDLRLRGHQKEGYGLSWNPNLSGHLLSASDDHTICLWDISAVPKEGKVVDAKTIFTGHTAVVEDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIGEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQVWQMAENIYNDEDPEGSVDPEGQGS", "text": "FUNCTION: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the PRC2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere Note=Localizes to chromatin as part of the PRC2 complex. SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family."} | |
| {"protein": "MKSLIFVLLLGAVFAEEDKIVGGYECTKHSQAHQVSLNSGYHFCGGSLVSKDWVVSAAHCYKSVLRVRLGEHHIRVNEGTEQYISSSSVIRHPNYSSYNINNDIMLIKLTKPATLNQYVHAVALPTECAADATMCTVSGWGNTMSSVADGDKLQCLSLPILSHADCANSYPGMITQSMFCAGYLEGGKDSCQGDSGGPVVCNGVLQGVVSWGYGCAERDHPGVYAKVCVLSGWVRDTMANY", "text": "SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family."} | |
| {"protein": "MKGVDDAFLGVGDKPGLDIWCIMGSNLIAIEKSLHGKFYTGNTYIILSTVELKSGVRQHNVHYWVGEEAKEEDCLTASDKAIELDVALGSNTVQYRETQGEESDKFLSYFKPCIIPIQGSLSSHMRIYGDKSKDTTMFRCEGEHVARVTEVPFSRSSLDHKAVFVVDTESKIFLFSGCNSSMQTRAKALDVVKHLKENRHCGRCEIATIEDGKLVGDSDAGDFWNLFGGYAPIPRDVQDTVMTELMTTSSKKLFWINKRNLVPVETNLLEREMLNSDRNYILDCGTEVFLWMGMTTLVSERRTSVTALEDYVRCEGRQSNARSVILTEGHETVEFKMHFQHWPKNAVPKLYEAGREKVAAIFKHQGYDVTEIPEDKPRHFISCNGSLKVWLVDNGSVTLLCTEEQEQLYNGDCYIIRYSYIEDGKDYHLFFAWSGLNSINEDRVAAASLMSGMIDSVKGHAVVAQVFEGREPEMFFLVFKSLIIFKGGRSMAYKNFVSQRSDANGWYQKNGVALFRVQGLKHDCIRAIQVDLAASSLNSSHCYILQAGGSFFTWLGSLSSPSDHNLLDRMMDKLCPLKQSLLVREGSEPDRFWEALGGRSEYLREKQVKDWPADPHLYTCHFEQGLFKAKEVFSFSQDDLVTEEILILDCVEELHIWVGHQSGVLSKEQALDIGKMFLQAGIHQDGRRPIDTTMYIVTEGDEPRFFTSFFNWDYSKQTMLGNSFERKLAILKGISQKLETPERSLRKSSSSSLPRRSPGTSSSEPTTPEQRAAARTFASASTGKLLRERSPAALSPSLSTPSPSPRSRSSASSSPASWNSTPSTVARRLFPPSLHASAEAVATGTPRRR", "text": "FUNCTION: Ca(2+)-independent actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and protects them from disassembly. Promotes VLN3-mediated MF severing. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family."} | |
| {"protein": "MHLRIHARRSPPRRPAWTLGIWFLFWGCIVSSVWSSSNVASSSSTSSSPGSHSQHEHHFHGSKHHSVPISIYRSPVSLRGGHAGATYIFGKSGGLILYTWPANDRPSTRSDRLAVGFSTTVKDGILVRIDSAPGLGDFLQLHIEQGKIGVVFNIGTVDISIKEERTPVNDGKYHVVRFTRNGGNATLQVDNWPVNEHYPTGRQLTIFNTQAQIAIGGKDKGRLFQGQLSGLYYDGLKVLNMAAENNPNIKINGSVRLVGEVPSILGTTQTTSMPPEMSTTVMETTTTMATTTTRKNRSTASIQPTSDDLVSSAECSSDDEDFVECEPSTGGELVIPLLVEDPLATPPIATRAPSITLPPTFRPLLTIIETTKDSLSMTSEAGLPCLSDQGSDGCDDDGLVISGYGSGETFDSNLPPTDDEDFYTTFSLVTDKSLSTSIFEGGYKAHAPKWESKDFRPNKVSETSRTTTTSLSPELIRFTASSSSGMVPKLPAGKMNNRDLKPQPDIVLLPLPTAYELDSTKLKSPLITSPMFRNVPTANPTEPGIRRVPGASEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYQVDETRNYISNSAQSNGTLMKEKQQSSKSGHKKQKNKDREYYV", "text": "FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity). SUBCELLULAR LOCATION: Presynaptic cell membrane; Single- pass type I membrane protein. SIMILARITY: Belongs to the neurexin family."} | |