lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MASLYTLNKKLVAAGIVAALSTLNLALPFSAPGEVCYNSMDGEKKDRKHPVLLLPIEMEKTESSQTVIEGIQLGFLGYMITVSAFVAEVYCLIESGHIWRVFGYMILSIGLSFGLGTLVYSTCLDQGLLFY
The following text describes a protein:
Function:
Probable multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal chelators which control many aspects of cell physiology (By similarity). May have a dual substrate specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering glycolytic bypass.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MMVKIKNIIILFCIFGLLSNVSSLSSSSSSSQSSDNNGNLSPIQDYDLEFLSKHLTTKTPYWILTKNGDSNSQGDGSSGNSNSNSNSNSNSNSNSDSSNEPPEQCKLISIDFIARHGSRMPVLNSIEKLKEMTTSILEYKEQVNQGFNWIFNYSVPYPSDIAGNLILQGQYEHYNISKRLLKKYPLFFEPMKYKPQSYSITSTAISRTGISASAFSYGLLQGTGSLGVDGFQPVFIETASLDQDILLRFFATCNQYVDQLKNGTLINKDEQTKWNQMVFPNISNEISERLGLSDIWLPTSNVISDIFEACAYEISINNISDHWCSLLSKQNILDWEYSQDLSNYWLKSYGHEINYQIATPLLNDILSGFDIYINNNNNGSSSSSSSSSSNNGDNSGSNGSSGSGSSTSTSSNDNGSTNNNDNKVEPTSILRFGHAETIIPFISLLGLYKDEQKLFANSSTEQIENRKFRTSVVSPYASNIAMFLFDCGSAADGFKILVQHNELPVLVPGCDEIYCDYQQFKSIFKQGIDNFKWNSYCNINDDDSGSSGGDSGNGNGNDSHSKKSSYFLAIFIPITFLVGGTIGGIFTYFSYEKIMQVKNRKKLTQYGNDEFISSPKSKSFSFKPTKFDSRSPLIQ
The following text describes a protein:
Function:
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Atg-2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an atg-18-PtdIns3P interaction. Atg-2 then extracts phospholipids from the membrane source using its NR and transfers them to atg-9 to the IM through its predicted beta-sheet-rich structure for membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MSFFYRSFANSLLPKQLLRFILARLDLLDSQALDLDNLNFALGRNTVLEFRDVGLILSKLEALTNLPPTFKIQKAKVLLLRITIPVDIYNSPIIVEVEGVDTRIRVASKQEQDEQTAKNKKGTHKDGDEVVPTAADLAQSFLQTEIPTDEQRRLEKALAEEAQEALSESMSDSETDDDGSFATFGTGQGLSLPTFLTNFLQGILDRLQIRIHKVTFQLDMQVPVEPGLSTIELVTFQLALDEVIAEGVTAPGQQKDGSPAIVPREGKRHILLDNLRAFLITEANVFSSLLPTQSAQSLVKPQGPAPHDVPSTLRDMSGSMQSSVGGLDMSISPDQMEALDMLAQSQYEVRDSEDALNIPYESDTQYPEAEENVAGSSPLSTPRASMYQEHDTPMLQDHANSAIMQHQPELWSSYERGIRSEPSLHPPTSFQPQTMPSGAVSPAPSEPSSSASSVRSDDDTPSADTEDLAQSHLYSHEEAESMYMSAFSDAHSTLMPGAYMPGGWGAESEGGESASERDLSTTHPVAGEPQSSTPVVSELASPTPIPEQNPTAQGYEPQHEDTSTPRGITRMVKEIVSLDSISVYVPSTRKQVLAPVTNLAKSNPNLPGAFSVHQSFHSSTTDQSTLLTPENLKEDRQDYAIEIVLKPLTLRFDSSVGFLLAMVVTRLLEAFKGSSDEGAEVKPSSTESILPDIKVCLEQVTMQFLEELTGVADSAKRIYETQKPNFGSDVLLEASLTNLNAFTHQSGSQTEVNVSIEKFAFGYADEAIVSFTGEADLFQSTATVDMLSVGKDIAVKATITPDVTRVDVKTLPLYLKLDLQRLDETFSWFGGLSGFLNMGASEDSVAKAVQIPAKPPQKTRGVRFETPIDPMEKRSGSKIDVRINGVHVDVIGKDCRAVLNTSALKLVHREEAIAAVLKTIRLSGPYVRNSHARAPVVLELDSTRLDYILTPRTRDLERLLELITPSKVKFDEDEDEIMVDTLLRQRRKGGVLGLEVKNFKVRAGNLALLDCIPSLVDDLAKLGTVAKYLPEDDRPGLLTLGQVTNVDCEVDVGGRFGVVNARLTNLELAQITVPSLVAVAVGVVTVNRNENSPIEEELVSTSTAHAPGSSKAPVLMMRMIDDIEPVLKIKLFGLNVDYRVPTIMDVLGLIQEETTPEEFEANLAASVANLGGQATAALRRQDTPESPVVDKEFKPIKLDVAFRDCVVGLNPLGQDSKLAIVLADSHLEAIPGKDSTLDATATLKKACILLIDDVKTLQDVQINARGRAPAMSTPQALELCSKGFVSICEMSSAKAVVKVGKDENGESHVEVSVRDDLLVLETCADSTQTLISLANALTPPTPPSKEIKYRTSVLPVEDLFASITPDAFGRAEGEYDFDDDFAGAQGIECGNEDDDDYYGIGSTEHLEIQSEGYGVAEELFDATNSSLLGDIEVENTNDGMLVSTANLDVPPVSSQSESDLDIQENYFSSEPVKNTTLRWNSRKNLYDQSSDAQVFKSPLVICVRDVHVIWNLYDGYDWVRTREIITKAVQDVEAKAYERKARADRHTYEDEGDEESVVDDCLFNSIYIAVGPNGDPSNLRRAINQELQYQDTTTETESVATTAFTTSTVRASGHRQSRPRGKTLKLSRSKNHKITFELKGVNIDVVTFPPGNETINTIDVRIHDLDVFDHIRTSTWKKFAMYDIDAGERELSKHMVHLEVLNVKPVPDLPATELVVKVNILPLRLHVDQDALDFITRFFEFKDETQPIHQSSSDVPFIQRCEVGDVPVRLDFKPKRVDYAGLRSGHTTEFMNFVILEDSRLVLRHVILYGVSGFDKLGKKLNDIWTADVKSTQLPGVLAGVAPVRSLVNAGSGFKDLIEIPIREYKKDGRIFRSIGKGATAFAKTTGTEVVKLGAKLAIGTQYALQGAEGMLAKNPPNYNHAGPSSSSAGVPAGVDYEVWDEEDFGDHHTPKAISLYADQPLGIMQGMRGAYASLSRDIAIARDAIIAVPTEVMESSSAQGAAKAVLMQAPTILFRPAIGVSKAIGQTLLGATNALDPNHRKRIEAKYKKH
The following text describes a protein:
Function:
Transcriptional regulator that may act as an activator (By similarity). Plays a role for mesoderm patterning in early embryogenesis.
Subcellular Localization:
Nucleus.
Sequence:
MHSENKLSNHGKQVTSGAQSQLPNVNQAQQQAPAGIQGSKGSVSGNHGVKANQISPGNPGLKSLNQTGGGGGMMKTKAKRERSVSIDTGDQRESLTPVLEPDAKVEGVMRSKRRCVLERKQPYSGDEWCSGAETEEEDEKPLSATHREHVMCPSQGHSGSSTTGHVSDPGGPGLGSGHGPGIRTDLHSRPPQQVVYVFTTSLANSAAEAVMHGHTDSILLYHQQNVPRTKLDQSTGVGKVSNLAEHISSSHSPPIGTPKSQSGTPRPASVGGVGHLPGTSTPSSTGHPDSEPAQTHRGGGTSSNNGRSAVHTLGLGNSGPQSVGVSGTEGVDRPGAIPHHGAGVSPSTSPSVLSALRQSELGQRVGPGNTDGLSKEQLEHRERSLQTLRDIERLLLRSGTGVAQEDPRGPNGNPNGTNVNNNNSNDGGRGLEDGEIGGGIPGNCHINNAGMPGMPPVGGMKKYEEPLQSIISQTQNLGGPGLDDSLMGPHHGMPPHSHHLSSPSGLDMGPLLGPEGVTPEQLAWRKLQEEYYQEKRRQHDMNPHQHPQHFRIMPEMGMPGGPPMLMRGPPPPYHSKPGDQQWGPGPMVGGGMGGNARMMDMNQEGPRGPRFLGQMRGPSGGGGYPESPGGVLGVEGLGPQRPPRPGMGWLEEIPPNMGGGGPFHGCCPPGGPGGPPQHFQGDLDRPMTREEIYRRIHRLDLQQMSRQQQQAGLGGPRMMDNPGGPGFPNPGMAGGPPSRGDPMDFPVSRTIMGSPIGGVGGDGGPTMRDIVDSPLGGNLNMNMGMNINQQQQLLAQKLRGGPGVLGEMLNAEDISRIRASQNGRGGANKAMIPGPEGPLQFPNQSSFPGGQVDGPYLQQPGPDMYGPDQPGPPHLSSTSRLSHIPMNTGSRVTDLGARHPPDLPISVNPMGSPAIPPSHQLKSPSLSQEPSPLMPSPSAAGLKSPSQLPQSGPTHPPLPAASGAGTPSSTSIKSPQVMGPSLGLRSPSGSPGHLKSPSMPVASPGWTASPKAAMPSPGGPPSVKVTGNGGSSSTDTGMSLPPRSSNSTPISQPSNSINPSMPFTSSPDAPPSQNPLSLIMSQMSKYAMPSSTPLYHDAIKTIATSDDEMLPDRPLQPGTNMSVGGMGNHQSAQMLLSSQGAMGPHSGPQSPMGMVLQGGPPLSHDHPGPMLPSPNPMGIPGMPSEIMGGGGGPPDGIGPCNVSPMHTQNQMGGFPRIQGPLHSPIGGMGQQFPPRPDDVLPPQQMHLLSKGMSHQRPPHQPDSFPPMPMGDGPDLSEVIRPTHRGIPEFDLSRIIPADKPSSTLQYFPKSETMSQPQQNPHQGQPPPQVSSAQLLKQLSSSGPPHSNIPSSNPHIANLQNMMAEQQLPLHPSHCGMRPGMGMPQIGSRGMGSGGGMGPMCHPGHMMGRTGMSPQQQLQQQHHHQQQQAMMANNLLQHPSHPPRGMLSPQQHPHNLIAQQNLMMMQAKQRGMALPGEHFGQQGALMSPQGPMMGPPHSQTGMMGPQSLRQRSMSLDSPLGYGPGSMANMPF
The following text describes a protein:
Function:
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
Subcellular Localization:
Nucleus.
Sequence:
MTSKKRGLSLEEKRKGMMEIFYEKKDFFQLKELEKIAPKEKGIVQGTVKDVIQSLVDDGMVDTDKIGTSIYFWAFPSKAINAKKQKLVQLENSSQQLKKLRVDVEAKLAEKKVGQQDDDTKDELLKKLKEAQVQNAELKRSLKEYQELDPDELEKLKAESQVSLEAVNRWTDNIFAVKSWCKSKFYMEDNQLNKAFGIPEELDYL
The following text describes a protein:
Function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Sequence:
MTFSEPQNTTEYNQIFASADVAIVYLTATWCGPCRAIAPIFSRLANENPEIAFIKVDVDKCHDLPLASSVTGVPTFVAFRTKVEVDRKAGASPAAIEGLIKLLK
The following text describes a protein:
Function:
Catalyzes the oxidative cleavage of several carotenoids and apocarotenoids in vitro. In contrast to other carotenoid oxygenases, cleaves substrates at two different sites, namely the central C15-C15' and an excentric double bond at the C13-C14 position, leading to retinal (C20), beta-apo-14'-carotenal (C22) and beta-apo-13-carotenone (C18) from beta-carotene (C40), as well as the corresponding hydroxylated products from zeaxanthin and lutein. Converts beta-apo-10'-carotenal (C27) into beta-apo-13-carotenone (C18) and to minor amounts of beta-apo-15-carotenal (retinal; C20) from the cleavage at the C13-C14 and the C15-C15' double bonds, respectively. Can also cleave beta-apo-8'-carotenal, 3-OH-beta-apo-8'-carotenal and 3-OH-beta-apo-10'-carotenal. Does not use as substrates beta-apocarotenoids that have a chain length shorter than C25. Also cleaves lycopene into apo-13-lycopenone (C18) and apo-15'-lycopenal (acycloretinal, C20). Moreover, is able to cleave 3,3'-dihydroxy-isorenieratene representing aromatic carotenoids synthesized by other mycobacteria. Might be involved in the utilization of carotenoids from host cells to produce compounds required for normal growth.
Miscellaneous:
MISCELLANEOUS: M.tuberculosis is assumed to be unable to synthesize conventional colored carotenoids, but the data obtained in PubMed:20929460 reveal that M.tuberculosis may utilize carotenoids from host cells and interfere with their retinoid metabolism. The occurrence of suitable carotenoid-substrates (i.e. beta-carotene, lutein, zeaxanthin and lycopene) have been shown in human plasma and tissues, and the apocarotenoid substrate beta-apo-10'-carotenal may also be present in lungs.
Sequence:
MTTAQAAESQNPYLEGFLAPVSTEVTATDLPVTGRIPEHLDGRYLRNGPNPVAEVDPATYHWFTGDAMVHGVALRDGKARWYRNRWVRTPAVCAALGEPISARPHPRTGIIEGGPNTNVLTHAGRTLALVEAGVVNYELTDELDTVGPCDFDGTLHGGYTAHPQRDPHTGELHAVSYSFARGHRVQYSVIGTDGHARRTVDIEVAGSPMMHSFSLTDNYVVIYDLPVTFDPMQVVPASVPRWLQRPARLVIQSVLGRVRIPDPIAALGNRMQGHSDRLPYAWNPSYPARVGVMPREGGNEDVRWFDIEPCYVYHPLNAYSECRNGAEVLVLDVVRYSRMFDRDRRGPGGDSRPSLDRWTINLATGAVTAECRDDRAQEFPRINETLVGGPHRFAYTVGIEGGFLVGAGAALSTPLYKQDCVTGSSTVASLDPDLLIGEMVFVPNPSARAEDDGILMGYGWHRGRDEGQLLLLDAQTLESIATVHLPQRVPMGFHGNWAPTT
The following text describes a protein:
Function:
Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions.
Subcellular Localization:
Nucleus.
Domain:
The DNA-binding JBP1 domain (DB-JBP1) is necessary and sufficient for binding to J-DNA.
Sequence:
MRRQVKKVLREKADDSMKPGWDVYQPSNDVVYAFNHYMQGSQIDAEAREKAEKAFQEAVKKHPFHNNADHTVDFHGTTVFRNAKGKVCGVLIPKALPSFATSMAADVLECAVARTSLRSALFGGVSPNSGIAGYFDYRGTPVELKCRKTSFTYEHTKEWRSVFPMIDYTSAIYKAALPDHWKAQDAAVPDVVRIHGSPFSTLTVNERFRTASHTDNGDFDNGYGVLAVLKGEYSGLSLALDDYGVCFNMQPTDVLLFDTHLFHSNTELEAKEANATWNRLSCVFYYRAALGEQPCVEEYRRRLKKAKEEKSTSLSFNHIEQKDNGENTNKPAPVYPVSLTPFSCAASAWALRGCAAAMLTRLHGLVRENASLMTELFGEPVEVADGLPRRAPEEIIPVHKHTNVQMHYLGGFSEKGDILNEAMNKRHYLDKENLQKMFGEEFVNIWTQSRTHWLQLVKKEWEHQKETNPTRTRFSWNNTSAMNFAFFDLCDVAKQLMCGAFGDREVNKKEEQSFWGMFAAHLDNACINEIGMLQGSMGMHKLNVKLKDYNFGGTRYLKDMPPEEQERRRRRRLEIEQARRRAPICDSESGDWLRNEAFDYQTEDVAVNYEREQWITPENNAKRFGFPERGVYGAEGAATGTISVLIVLPKPTNHRQKTCELPTSREADRIMKNPAAQRLLCAKPCNIGLSTSSNKSRTVLCGNIRIDKVFDGGSVGGKMYDFVIMRHLLAATTGEREPLECLVRWTSLARYCTFVVEVDLLDRHHYILKSEIGEEYSAVSEICFSALYSATYARDKVNLRTTPCLLSFIDKSGNMLESRFKFNGSPLNTVAFVVRRREK
The following text describes a protein:
Function:
Oxidoreductase that catalyzes the last step in proline biosynthesis, which corresponds to the reduction of pyrroline-5-carboxylate (P5C) to L-proline using NAD(P)H. Proline is synthesized from either glutamate or ornithine; both are converted to P5C, and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCR3 is exclusively linked to the biosynthesis of proline from ornithine.
Subcellular Localization:
Cytoplasm.
Sequence:
MPFSQQPVQQPAEEKPDASPTLMGDYTVKKDISEMSLAFVGAGKMAQAMAKGFLAAGVVKADHITATAPSCRSQPTLEDIGCQFTHNNKEAVENSDIIFLSVKPHILPGVLQEIAPVVTKRHLMVSVAAGVPLQFLEEKLPPKSRVMRVMPNTPCVVRQGASVYVPGSHVEKEDSEIIKSLLSSLGYCSESNEGMISAVTGLAGSGPAYMIQKRGFCSDTYKDPVYVAIGLGGMGQAYAFTAIDALADGGVKMGLPRELSIKLAAQTLLGASKMVLETGKHPMQLKDDVCSPGGTTIYAIHKLESGGFRNLLIDAVEGACLRAEAIAKKAK
The following text describes a protein:
Function:
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Sequence:
MFKIVFFGTSTLSKKCLEQLFYDNDFEICAVVTQPDKINHRNNKIVPSDVKSFCLEKNITFFQPKQSISIKADLEKLKADIGICVSFGQYLHQDIIDLFPNKVINLHPSKLPLLRGGAPLHWTIINGFKKSALSVIQLVKKMDAGPIWKQQDFLVNNDWNTGDLSIYVEEHSPSFLIECTKEILNKKGKWFEQIGEPTFGLNIRKEQEHLDLNQIYKSFLNWVKGLAPKPGGWLSFEGKNIKIFKAKYVSKSNYKHQLGEIVNISRKGINIALKSNEIISIEKIQIPGKRVMEVSEIINGKHPFVVGKCFK
The following text describes a protein:
Function:
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MDTVNEKVDHGTFSPSNESIASSPERSYVQQKRTKLSAFFKGYSFPISIFSIVFLFLVFRSFVDHQPVNSCETSTVWPSYARIHDFDERYTRFSEKYSLYLYREKSVIENAEPSGIPIIFIPGNAGSYKQVRAFAADVAHQFADLLSASYDEAIASGKRNLDFFTLDFNEDFSAFHGQTLIDQAEYVNDAIAYILSLYPDTRTRSSFPDDDLPYPTSVILLGHSMGGMVAQSVFSLYNYVKGSVNTIITLSAPHTMAPFPIDRHLVEFYDSVKEYWTNSFLQPPENNALADVFVLSIGGGGLDTTVVPEYSAISSFVPPTNGLVIFTSGIPFVWAEVDHEAMAWCERFRQVVSRGLLAVTDARFPGGTKPLDERRALFWRTYVYGASIGNDLFLNKKDPLKEMLLYSEDTEYLGEVAHVTFDHFGDSNKKKTVVPLPHGKFQSFQLLTDQSLDIGSHVRVQFCKLDPSSSFPGSDDTEFGINALCHEKNEFLRLYPASTFETKHPHDGGVFYYLSAESKDLVDYDFILIDDRNFERREGFLEGFLSPLSLKPTLIDSSVLKLLTVGERLEFSPNNTLLSAFHFTGLQSSLFSYKLTLEYEIDDGVPALFAPFMKQKLQNPVESRYFPNIKSADIIMHGVSPFIDNVDTIFNKSLVLEFYMNPLKYQHVFLRIQPDYYGSMGRLLMRYRTLLASFPFVILAYVLRNQITRFNKGGSFSDVLEALELFARRGLIKLLAVVSLLTVFLSMSYRATTASAEHADNAVAAWRASAINSRSAFWKQNYLVFGLQEPMVWMLAPVLTIVFIGFSVSLNFLLTVILKCVSFLIRIFVKLRRSFKNIFFSPAKENIQQLTQETDLGDNVFKCNKRTIQFRIIANIILLTVSLTVVPFQFAYLFTCLTQICTTAKALYAAECCEYGPSVRRRWSFFNFSLSLLVIMLHLVPFDMPIILVWIRNVSMHWYIPFPTHHNFFSIIPFILVTEIQRTGRMLPRMSDLELCLNNFLLYFLSFYSLIYGAEKPYLIHNVVGLYFMWITYLYAKDFRRRDKLTKSYNPSFSCFINTPRSAHNVNSC
The following text describes a protein:
Function:
The glycine cleavage system catalyzes the degradation of glycine.
Subcellular Localization:
Mitochondrion.
Sequence:
MLKSTATALLRRAKRTSILPSTSSRSLASSTNEEPLVKTSLYNLHKELGGDMVPFAGYELPVLYKGDNGGVMKEHLWCRSDGKASLFDVSHMGQIRWRGRDRAAFLEKIVVGDIAGLSEGSGCLSLVTNVNGGIIDDTVITNAGDYIYMVVNGATKFGDMKHFKEQMESFDGDVNMEYLEDSMQLLAIQGPGAAEAVSKLLPGAFDLTKMAFMTGVDTTLDGVDGCRITRCGYTGEDGFEIAMPAEHAVSIASKLLSDPSVNPTGLGARDSLRLEAGLCLYGHDLDENTNPIEATLGWTMGGPKSRRRTEGGFLGAEHILKPDGKFQKVARKRVGIKGMKAPAREHAEIFDANGETKIGEVTSGTFSPCLKAPIAMGYVETELAKAGTEVNVQIRGKMQKAEIVRMPFVESRYYRIPE
The following text describes a protein:
Function:
Putative Lysin motif (LysM) receptor kinase that may recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MNLTFYIFFLSLLPSFSSSKPMNCSDTTRLCSSFLAFKPNQNQSFSVIQSMFDVLPQDITADISGGYFFIKKNCSCLTTTHQYTTNTTFTIRQNVGYVYNVTVSAYSGLAFPPNTTRAARAGAVVSVQLLCGCSSGLWNYLMSYVAMAGDSVQSLSSRFGVSMDRIEDVNGILNLDNITAGDLLYIPLDSVPGEPYETSKINPPAPSPAPASSLANGNISDDQVNHTAKSGSHVPYIWIVGGLGVVLALLVLCILVCICLRSSSCSSSEEDGNGHNFQILRKSGFFCGSGRYNCCRSGDFRQTNGETQVVAIPKALGDGMFEIEKPMVFTYEEIRAATDEFSDSNLLGHGNYGSVYFGLLREQEVAVKRMTATKTKEFAAEMKVLCKVHHSNLVELIGYAATVDELFVVYEYVRKGMLKSHLHDPQSKGNTPLSWIMRNQIALDAARGLEYIHEHTKTHYVHRDIKTSNILLDEAFRAKISDFGLAKLVEKTGEGEISVTKVVGTYGYLAPEYLSDGLATSKSDIYAFGVVLFEIISGREAVIRTEAIGTKNPERRPLASIMLAVLKNSPDSMNMSSLKEFVDPNMMDLYPHDCLFKIATLAKQCVDDDPILRPNMKQVVISLSQILLSSIEWEATLAGNSQVFSGLVQGR
The following text describes a protein:
Function:
Repressor for the trePA operon. It is able to bind trehalose-6-phosphate.
Sequence:
MKVNKFITIYKDIAQQIEGGRWKAEEILPSEHELTAQYGTSRETVRKALHMLAQNGYIQKIRGKGSVVLNREKMQFPVSGLVSFKELAQTLGKETKTTVHKFGLEPPSELIQKQLRANLDDDIWEVIRSRKIDGEHVILDKDYFFRKHVPHLTKEICENSIYEYIEGELGLSISYAQKEIVAEPCTDEDRELLDLRGYDHMVVVRNYVFLEDTSLFQYTESRHRLDKFRFVDFARRGK
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that acts as a negative regulator of mTORC1 signaling by mediating ubiquitination of RagA/RRAGA and RHEB. Catalyzes 'Lys-63'-linked polyubiquitination of RagA/RRAGA in response to amino acid starvation, thereby regulating mTORC1 signaling. Also mediates monoubiquitination of RHEB, promoting its association with the TSC-TBC complex and subsequent inhibition. Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed.
Subcellular Localization:
Lysosome membrane; Single-pass membrane protein.
Sequence:
METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGITKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERTLLPGDMGCRLLPGSQQKSLTVVTIPAEQQPLQGGAPQEAVEEEPDRRGVAKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG
The following text describes a protein:
Function:
Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines.
Subcellular Localization:
Secreted.
Sequence:
MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR
The following text describes a protein:
Function:
Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (By similarity). Preferentially cleaves the N-terminal side of paired basic amino acid residues (By similarity). Also degrades other unstructured peptides (By similarity). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (By similarity).
Subcellular Localization:
Mitochondrion intermembrane space. Mitochondrion matrix.
Sequence:
MNYAKLSIAFSKKTIKTHNCRLFQRWLHVGDKVHDFRVVDTKKVPELQLNYTRLKHEPTNADMIHLDREDPNSVFSIGFQTPAENDEGIPHILEHTTLCGSNKYPVRDPFFKMLNRSLATFMNAFTASDFTFYPFATVNTTDYKNLRDVYLDATLFPKLRKLDFLQEGWRFEHADVNDKKSPIIFNGVVYNEMKGQVSDSSYIFYMLFQQHLFQGTAYGFNSGGDPLAIPDLKYEELVKFHRSHYHPSNAKILSYGSFPLEDNLSALSETFRPFSKRELNLPNTFLKEFDQEKRVVEYGPLDPVMAPGRQVKTSISFLANDTSNVYETFALKVLSKLCFDGFSSPFYKALIESGLGTDFAPNSGYDSTTKRGIFSVGLEGASEESLAKIENLVYSIFNDLALKGFENEKLEAILHQMEISLKHKSAHFGIGLAQSLPFNWFNGADPADWLSFNKQIEWLKQKNSDGKLFQKLIKKYILENKSRFVFTMLPSSTFPQRLQEAEAKKLQERTSKLTDEDIAEIEKTSVKLLEAQSTPADTSCLPTLSVSDIPETIDETKLKFLDIAGMKAQWYDLAAGLTYIRLLLPLKNFPESLIPYLPVYCDACLNLGTHSESIGDLEHQIRRYTGGISISPSAVTNNSDVSKYELGIAISGYALDKNVGKLVELINKAFWNTNLSNTDKLAIMLKTSVSGITDGIAEKGHSFAKVSSASGLTEKTSITEQLGGLTQVKLLSQLSREESFGPLVEKLTAIREILRGTSGFKAAINASPTQHEVVEKALQKFMKSRGVNQQTQTKSTSKERNGINSIKTYHELPFQTYFAAKSCLGVPYTHPDGAPLQILSSLLTHKYLHGEIREKGGAYGAGLSYSGIDGVLSFFTYRDSDPIRSLSVFDEASEWATTHEFSQRDIDEAKLAVFQGIDSPVSESQKGMLYFVDGVTDEMLQNRRKQLLNVSANDLKAVAKKYLVNPKKSYTAVLGPKSEKQLPTWVIDKFES
The following text describes a protein:
Function:
Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.
Subcellular Localization:
Cytoplasm. Endoplasmic reticulum.
Sequence:
MVTAEAVMAVVRAARPVFCCAHDGVAFAANAAFLADGYSLCAVGPAALINPRPAEEEEVGIDGWNSMDNIYAFLYYKEDDGKKKFILMKCVVIADFLAIDALDLEAQHEGRFIVQINVKDFYSEEQHKNYKDMYKNFVCLINILNTTLLVELGRKDTTAVQIPDVENSSSMSSSGNFTWENPSTRTTEPAGSQYILWESRSTRMIEPAGLIYPPVVLVGDDDTFPVPGVGLYPHSGETGGSMHVGPNDPRFFPTNPSTPFGDLGSVPPGGRYDPIGPPDASGFEPSRFVSPSRHSGGSTHPDLEFFQQGPDFF
The following text describes a protein:
Function:
Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
Sequence:
MEPSCVQFLENKTVLVTGASGFLAKVFVERVLRLQPKVRRLYLLVRASDNKAAKQRLHSEVFEKDLFRVLRKNVGDERLNALISEKVVPIPGDISLNIMGVIRDSNFLQDMMQEIDIIVNSAATTRFDERYDVALGINTFGPLNILNFAKKCAKPQLLLHVSTAYVCGERSGLILEKPFAMGETLNGKNKVDIDAEMLLVEQKLKQLKKLGYSEEETKQAMKDLGLKRAKLYGWPNTYVFTKAMGEMLLGYCRESMPIVIIRPTIITSTFSDPFPGWIEGIKTIDSVIVSFRKGLLKCFLVDDMAVCDLIPVDMVANAMIVTAAEHSRESGSHTIYHVGSSYQNPVMYKQIYEILNRFFLASPLLGRNGLPIVPNVKIFPTMARFRVYTSLRYKLPLQILRLLRLIFPSQLGEKYEVHNRRFNIAMRMVKLYRPYVILKGIFDDRNLERLRIKNEGTGIDKLIDSIKCIDWEDYFMNIHIRGLITHVLEK
The following text describes a protein:
Function:
Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a voltage-gated highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate) that senses pH changes and confers electrical excitability to organelles. Localizes to the early and recycling endosomes membranes where it plays a role in the uptake and processing of proteins and regulates organellar membrane excitability, membrane trafficking and pH homeostasis. Ion selectivity is not fixed but rather agonist-dependent and under defined ionic conditions, can be readily activated by both NAADP and PI(3,5)P2. Required for mTOR-dependent nutrient sensing.
Subcellular Localization:
Early endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein.
Sequence:
MDISSTFDNMDTGLTQDRPVQMSSFYKEIEPVDGAGNHDVVNNVTIPASGASDPRAQNSLQQSWEMNFQEAAIYLQEGENNDKFFTHPRSAHALSAYLFAHSHLFYVVELLTAVLLMLLSLSEAPAVPFLRLDVYVHATLELLALVMVAFELCMKLRWLGFHTFIRHKRTMVKTSVLFIQFIEAIVVLVRQTSHLRVTRALRPIFLVDCRYCGAVRRNLRQIFQSLPPFIDILLLLLFFMVIFAILGFCLFSANTADHYFSTLENSIVSLFVLLTTANFPDVMMPAYSKNRWSCIFFIVYLSIELYFIMNLLLAVVFDTFNGVEKMKFKSLLLHKRSAIEHAFQLLVSRQRPDGVSLKQFDGLMRFYHPRMTPRDRFLTFKALNHSGAPMLSLQDFYKFYEVIGLKWKARRSGEHWFDDLPRTALLIFKGINLLVKSKAFQYAMYLVVAVNGIWILVETNMLNDGISWTRVVPWSYIIFLTIYGIEVLLKITGLGPITYFSSGWNLFDFSVTVFAFLGLIALAFDMEPFYFIVVLRPLQLLRLFKIKQRYRNVLDTMFELFPRMASLGLTLIIFYYSFAIVGMEFFADVIYPNCCDNSTVAASYRQINVTTGNRTELQEGYYYLNNFNNILSSFVTLFELTVVNNWYITMEGVTSQTTHWSRLYFMTFYIVTMVVMTIIVAFILDAFVFRMNYSRKNREPLDDPEDEKGIVFETEVSQTEALQTLDFYKHTLGVTNLTSLQDMCVALERSGQTSLVFLGRRSRTKSDLSMKMYEEEIQEWYEEYSRTNLQTDGTFHRELDSPDAGATNSIN
The following text describes a protein:
Function:
Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity).
Miscellaneous:
MISCELLANEOUS: One of the histocompatibility antigen responsible for chronic graft rejection.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Cytoplasm.
Sequence:
MDRDEEPLSARPALETESLRFLHVTVGSLLASYGWYILFSCILLYIVIQRLSLRLRALRQRQLDQAETVLEPDVVVKRQEALAAARLRMQEDLNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGRSYKRNSGRPQEEDGPGPSTSSVIPKGKSDKKPLRGGGYNPLTGEGGGTCSWRPGRRGPSSGGUN
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MATKKSENRRPALLSRTRPPTVQKKNAALSAKATRTLIRSHHTLLKQRAQALKSGDQDLVRKLEADIRANGGLKSYQIASKLGQSLDRGGDSSRVLVNWISPSLNVLRSTSLKLRVLEIGALSTKNACSQHKHLDVTRIDLDSQEPGILKQDFMERPLPLSNDERFHIISLSLVLNYVPDPVDRGEMLKRCVTFLTKEPPQGSSITIVPRLFLVLPAPCVTNSRYLTQQRLHDILTSIGFSLAEDKQTTKLIYQLWEYDGICQPKQFKKELLNPGKTRNNFAIVIKSGSQ