lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
O-methyltransferase required for two non-consecutive steps during ubiquinone biosynthesis. Catalyzes the 2 O-methylation of 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoic acid into 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoic acid. Also catalyzes the last step of ubiquinone biosynthesis by mediating methylation of 3-demethylubiquinone into ubiquinone. Also able to mediate the methylation of 3-demethylubiquinol into ubiquinol.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MMRNALLVSGKLRHLLSCSIGRNSTRSSSTAKSLDAGTQKEVRHHENHASEWWNQNGTMGALHALNEIRVPFIRDGIVSRGTVKPGYVNTTKVLLGQNILEVGCGGGLLTEHLARLGAQVAGIDLGEKLIEAAREHLKCSSPELASNVVYKIEPVDQHAKANCECYDAVIVSEVLEHVKDKVSLLEASVRSLKPGGSIFITTLNKTIPSWFGGVLLSEYVLNLVPRGTHHWDKMISPLDVQRILDTMNCQTVLVNGSTYDFWSNTWRWINNNQMCYALQAVKQAQREYN
The following text describes a protein:
Function:
Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres.
Miscellaneous:
MISCELLANEOUS: In BRCA1-deficient cells, function of the shieldin complex is necessary for sensitivity to the PARP inhibitor olaparib.
Subcellular Localization:
Chromosome.
Sequence:
MAARDATSGSLSEESSALDLPSACDIRDYVLQGPSQEANSEAFSSLEFHSFPYSSDVDPDTSNLNIEQNNSWTAENFWLDPAVKGQSEKEEDDGLRKSLDRFYEMFGHPQPGSANSLSASVCKCLSQKITQLRGQESQKYALRSFQMARVIFNRDGCSVLQRHSRDTHFYPLEEGSTSLDDEKPNPGLSKDITHFLLQQNVMKDL
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MASSAAVPFWRAAGMTYITYSNICANLVRKCLREPFKAESMNREKVHFSLSKWADGKPEKPVLRSDAPEV
The following text describes a protein:
Function:
Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides.
Subcellular Localization:
Secreted.
Sequence:
MYFSSFLALGALVQAAAATYFAPNSTGLRIQHGFETILIQPFGYDGFRVRAWPFRPPSGNEISFIYDPPIEGYEDTAHGMSYDTATTGTEPRTLRNGNIILRTTGWGGTTAGYRLSFYRVNDDGSETLLTNEYAPLKSLNPRYYYWPGPGAEFSAEFSFSATPDEQIYGTGTQQDHMINKKGSVIDMVNFNSYIPTPVFMSNKGYAFIWNMPAEGRMEFGTLRTRFTAASTTLVDYVIVAAQPGDYDTLQQRISALTGRAPAPPDFSLGYIQSKLRYENQTEVELLAQNFHDRNIPVSMIVIDYQSWAHQGDWALDPRLWPNVAQMSARVKNLTGAEMMASLWPSVADDSVNYAALQANGLLSATRDGPGTTDSWNGSYIRNYDSTNPSARKFLWSMLKKNYYDKGIKNFWIDQADGGALGEAYENNGQSTYIESIPFTLPNVNYAAGTQLSVGKLYPWAHQQAIEEGFRNATDTKEGSACDHVSLSRSGYIGSQRFCSMIWSGDTTSVWDTLAVQVASGLSAAATGWGWWTVDAGGFEVDSTVWWSGNIDTPEYRELYVRWLAWTTFLPFMRTHGSRTCYFQDAYTCANEPWSYGASNTPIIVSYIHLRYQLGAYLKSIFNQFHLTGRSIMRPLYMDFEKTDPKISQLVSSNSNYTTQQYMFGPRLLVSPVTLPNVTEWPVYLPQTGQNNTKPWTYWWTNETYAGGQVVKVPAPLQHIPVFHLGSREELLSGNVF
The following text describes a protein:
Function:
Required for disulfide bond formation in some proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MTPAKIRNALLAVVAIALSAAVYLGFQTQTQGISLEAQAQRAIPLATALDNGRPTLVEFYADWCTSCQAMAPDLAELKKNYGGSVNFAMLNVDNNKWLPEVLRYRVDGIPHFVYLDDTGTAIAESIGEQPLRVLEQNITALVAHEPIPYANVTGQTSVVENRTIEADPTSPRSHGNPRPS
The following text describes a protein:
Function:
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production; Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MNVDSRFFAERKWAYKGEGNAHVVLASHDGFVVRLLKNRRDGQISRRSQDAVKYYNIVGPQFIDPSYLPEMRLVTVPKDFFGVVEDVCRKQRPDYRLDTNIAMNATATVMPDVCFVRERSRISEVKKLGNVAQMKDKTIPTFCVEIKDGILIYEDNSAYESLDTILHEWFSNSKNSCKNLGATTENFREIIARILVSDQACGTIDINGKQSVNSNCILNQILCAQRLGETDIEDIYPLFLKLEHEMTKSKTVAEAMQQLECFDSASWKYLNVFIDELVECNRSKSLYDILGIRRDASDKEVKRAFRKLAIKYHPDKNKDKDSEKKFIEISKAYQILSDKGRRRYYDRYGTADAPVPGEGSYPSQDEPSFQNSAEFPDVDGFSGSKYTFFGDQDKYFDDDQLHTKDNYNYNRRGWKRKQFFSFDDLLNDDLFEDKLFHGDESIGDSFFTNFKSRFSGGRHFFNIHGPFQDDFFGNSEADAKKIHPDRRQDRFTEEFSNDESTCKTVTKRIGNIVTTETSCS
The following text describes a protein:
Function:
Negatively regulates a plant defense signaling pathway which is independent of salicylic acid (SA) and systemic acquired resistance (SAR). Confers sensitivity to P.syringae and P.parasitica.
Sequence:
MALPWELEEDILSRLPPISLVRFRTVSKHWNSLFNDKTFINNHLSRSRPEFIILTNSKIYSVDIIDHNNIDPTIRLHEIPTYDIHSRGTDLNRTIINTCDEFLFYNYRYWDNMTALWNPWLRQVRWIEYANQEFCVFGLGYDNSRPEKVYKILGHLFCHGKVLRDQKVVIYECASDSLRFIDRPEDDDWPITETAKRSNVSLNGNLYWFGCSNYENDEYYIRIFDFSTEDFKPFCLLPCQMSHSTDELVLAVYKGDRFSLLKQCSVTREIGVWVTKERISNDNGNGGEGVEWLKLMTLSKPNLPKLFGTVSYFIYGKTLYMCNGDDETALACIYIVREDVCKKFQIGSGNINCRHCVYTPNLLSLPLFIG
The following text describes a protein:
Function:
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower efficiency.
Sequence:
MSEAQPLVTPKPKKSVALSGVTAGNTALCTVGRTGNDLHYRGYDILDIAETCEFEEIAHLLVHGKLPTKSELAAYKAKLKSLRGLPANVKAALEWVPASAHPMDVMRTGVSVLGTVLPEKEDHNTPGARDIADRLMASLGSMLLYWYHYSHNGRRIEVETDDDSIGGHFLHLLHGEKPSALWERAMNTSLNLYAEHEFNASTFTARVIAGTGSDMYSSISGAIGALRGPKHGGANEVAFEIQKRYDNPDEAQADITRRVENKEVVIGFGHPVYTTGDPRNQVIKEVAKKLSKDAGSMKMFDIAEALETVMWDIKKMFPNLDWFSAVSYHMMGVPTAMFTALFVIARTSGWAAHIIEQRIDNKIIRQSANYTGPENLKFVPLKDRK
The following text describes a protein:
Function:
Common component of the spliceosome and rRNA processing machinery; Required for ribosome biogenesis. Part of a complex which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVKQGPNGTEEPDSQRHHAAPPRPGNTGLRDQGTSVQQSNMAKTPKKQKTEEKEEHEESGGNKEDRERAYEVLATRVNPIASPLAARKLTKKLYKTVKKASKDKNIRKGIRDVQKFIKKGERGIVLIAGDTTPIEVYCHLPVVCEDAKIPYCYVPAKQDLGEAAGSKRPTCCVLLKPNESYQTSYDECLTDVSTLPRPI
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MKLFPYLNKICLLNLYFIKMEKPSIYFMNNKIKKIQIQYEERENNAPMKNFMLDEKKENYDITYKINIKNEQTSYPSNDDIKSHCQDKPDEGNVYKNINLTKKGNKKEHMNDSLLNKRKVKTEYVIKQKQMKREKEQTVLEEGIKHVHELKKRKNKNVKSDKIKIDEKGVDKKFIDEKGVDKKFIDEKGVDKKIIDEKNVEFKRAHFLLTYNKLKEMRKDIIAPVDKYGCDKLSEKTNDMKVFRFQTLISCMLSSRTKDEVTAMVMDKLKKHGLTVHNILNTTEEQLKKLIYGIGFYNVKAKQILQICHILKNKYNSDIPHTYEELKKLPGIGEKIAQLILQTALNKHEGIAVDIHVHRIANRLNWVNSKNELDTQMKLKSYVQKELWSEINHVLVGFGQVICKGKKPLCEKCTLTNKCQYYQDTSTKQENKSNEYI
The following text describes a protein:
Function:
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and small amounts of phosphatidylethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and ensures the maintenance of asymmetric distribution of phospholipids. May be involved in transport from early endosomes to the trans-Golgi network (TGN) (Probable).
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein.
Sequence:
MGIADGQRRRSSSLRTQMFNKHLYDKYRGRTDDEIELEDINESKTFSGSDNNDKDDRDETSGNYAAEEDYEMEEYGSPDVSYSIITKILDTILDRRRTFHSKDGRHIPIILDHNAIEYKQAATKRDGHLIDERFNKPYCDNRITSSRYTFYSFLPRQLYAQFSKLANTYFFIVAVLQMIPGWSTTGTYTTIIPLCVFMGISMTREAWDDFRRHRLDKEENNKPVGVLVKDGNNDAQEVYTLPSSVVSSTAYLTKSAAAENNPPLNDDRNSSQGHFLDTHFNNFELLKNKYNVHIHQKKWEKLRVGDFVLLTQDDWVPADLLLLTCDGENSECFVETMALDGETNLKSKQPHPELNKLTKAASGLANINAQVTVEDPNIDLYNFEGNLELKNHRNDTIMKYPLGPDNVIYRGSILRNTQNVVGMVIFSGEETKIRMNALKNPRTKAPKLQRKINMIIVFMVFVVATISLFSYLGHVLHKKKYIDQNKAWYLFQADAGVAPTIMSFIIMYNTVIPLSLYVTMEIIKVVQSKMMEWDIDMYHAETNTPCESRTATILEELGQVSYIFSDKTGTLTDNKMIFRKFSLCGSSWLHNVDLGNSEDNFEDNRDNTNSLRLPPKAHNGSSIDVVSIGDQNVLDRLGFSDAPIEKGHRPSLDNFPKSRNSIEYKGNSSAIYTGRPSMRSLFGKDNSHLSKQASVISPSETFSENIKSSFDLIQFIQRYPTALFSQKAKFFFLSLALCHSCLPKKTHNESIGEDSIEYQSSSPDELALVTAARDLGYIVLNRNAQILTIKTFPDGFDGEAKLENYEILNYIDFNSQRKRMSVLVRMPNQPNQVLLICKGADNVIMERLHDRELAAKKMADICTSTKERKDAEAELVLQQRKSLERMVDEEAMARTSLRNSLSSVPRASLSLQAVRKSLSMKNSRTRDPEKQIDSIDQFLETVKKSDQEIGSVVNKSRKSLHKQQIEKYGPRISIDGTHFPNNNVPIDTRKEGLQHDYDTEILEHIGSDELILNEEYVIERTLQAIDEFSTEGLRTLVYAYKWIDIGQYENWNKRYHQAKTSLTDRKIKVDEAGAEIEDGLNLLGVTAIEDKLQDGVSEAIEKIRRAGIKMWMLTGDKRETAINIGYSCMLIKDYSTVVILTTTDENIISKMNAVSQEVDSGNIAHCVVVIDGATMAMFEGNPTYMSVFVELCTKTDSVICCRASPSQKALMVSNIRNTDPNLVTLAIGDGANDIAMIQSADIGVGIAGKEGLQASRVSDYSIGQFRFLLKLLFVHGRYNYIRTSKFMLCTFYKEITFYFTQLIYQRYTMFSGSSLYEPWSLSMFNTLFTSLPVLCIGMFEKDLKPMTLLTVPELYSYGRLSQGFNWLIFMEWVILATTNSLIITFLNVVMWGMSSLSDNTMYPLGLINFTAIVALINVKSQFVEMHNRNWLAFTSVVLSCGGWLVWCCALPILNNTDQIYDVAYGFYNHFGKDITFWCTSLVLALLPITLDIVYKTFKVMIWPSDSDIFAELEQKSDIRKKLELGAYSEMRQGWTWDKDPSTFTRYTDKVLSRPRTNSRASAKTHNSSIYSMSNGNVDHSSKKNFFGNSSKKSSERYEVLPSGKLIKRPSLKTQSSKDSIGGNITTKLTKKLKLPSRNVEDEDVNQIIQARLKDLE
The following text describes a protein:
Function:
Component of the gamma-tubulin ring complex (gTuRC) which mediates microtubule nucleation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center.
Sequence:
MVLPQRTTRLVDGDDAQSFVQKLQLSISKGLPHAVPVPALRTDEHGLVKAVFQVLQGFETSLLYWDCNVPGYREKAGIYVAHLSLTGLRSVLSPLLFAATCLKEVELFVGKVRMRSHGIPTLDAFGSSVDSWLKRLREAALKEEEQQFISLNRTITLLGLTDSMSSLSSGAEHLYQVVHGAVPDGFWDSGAQMASSEVSVHILNHLFKKLNEVCLVEDGEGEPYHMLLVLFVGSLLPYLQCLDSWLYDGILDDPYEEMFFYANSAVTIDQPAFWEMSYMLRIRGSRADSSTASADNESIRKKESSNQESTTAGTCLKVNNQGCLDILCPVFLKDIARAIVSAGKSFQLVQHVQDVHQIQTHKVTYGSNVCQNTDCSSQQKFWPDTSSLRIQDGHPKSEDALEESTSQFGNDSREMGLLTLSEIFLICLSGLLENGDHVYEYLRRPHADNVPNNKTSVESESNVHEAKDICAENSTEKNWVKLLKHATSGRKYDGMENNISRNTVMDKPIFVPGDPQDASSNAIEGCSTLSCYENPAITACREVLLSNPNSWSELNISESFHLPPLNDGDMRRAIFADGHSVGTSTSGDTQPTTSFPRLDGTDYKFGFHFDDLEYVRQEDDRRTLEDLYAFPTLLPCAKENVPLSEILPMQKDSTLASRVLKFIQNMSLKDPLQPVSIIQECLSQCIKRQVDHIGKQILFKLMGEWRLMDELFVLRAIYLLGSGDLLQQFLITIFDKLDRGSSWDDDFELNNLLQESLRNSADKMLLTAPDSLVVSLATHNGEEGASTSKKGRALGFGIDALDMLNFTYKVSWPLDLIVNTEALKKYNQVMGFLLKVKRAKFVLDETRKWMWKARGRTAHNFKQHLIVAQKLLHFVEAFHQYVMDRVYHSAWTELCDGMASATTLDEVMEVHEAYLSSIQRQCFVASDKLWALIASRVKTILGLALDFHNVEQTLSTGGTAPAVRTRCEMEIDRIEKQFDECVVFLLRILSFKLNVGHFPHLADLVTRINYNHYFMSDNGSFSAIPGSRPR
The following text describes a protein:
Function:
Serine/threonine kinase that plays a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
Sequence:
MAHQQQQQLAPSVNCSLDDIDLTALKDPAGIFELIEVVGNGTYGQVYKGRHTKTGQLAAIKVMDVTEDEEEEIKLEINVLKKYSNHRNIATYYGAFIKKSPPGKDDQLWLVMEYCGAGSVTDLVKSTKGQSLKEEWIAYICREILRGLSYLHSNKVIHRDIKGQNVLLTDNAEVKLVDFGVSAQLDRTIGRRNTFIGTPYWMAPEVIACDENPDATYDNRSDLWSLGITALEMAESQPPLCDLHPMRALFLIPRNSPPRLKSKKWSKKFHGFIDTVLVKDYHQRPYTENLLKHGFIKDQPTDRQVRIQLKDHIDRCKKRKQEKEREDYRYSGSDNDDDEPQLAGEHSSIVQAPGGDTLRRNFQQIQEGRLAAEQQQQHHLMAQAQAQAAAAHAAAQAQAQLQQQQQQAAAAAAAAAHAAQQAQQAAQQAQAQQPQANRQPKPPSRQQVEEPGPPARPPQRLIVVPDPPHANRPLPPTPKCGEPAGQTPQQQQRNSQNNFKPSLPPRRPEDHLDVLAAQLSELGVVFSQQPQPQTAAGGQGSQQQAQPEAPPRNNRQSSGLSSSGGSASGGGGSSKPAAALPQQSNNHLGQPVNPLDPLDSSDSDSEPDEPNDRARNDGTLLASDPPKPLPGLGPVSEDANTTTPLSHGSGGPPNRPLPPTPDDDDQAGDRTLIMKRNRGGGGGGGGGGGGGGSSGVGADGTGLGTPGTRTSSVLPDLLSQASPATPPRHDKSSSEEKQRSFLTFGFGAGGSGPSRRESHVNVNVTPTSHEAANDTPEIRKYKKRFNSEILCAALWGVNLLIGTENGLMLLDRSGQGKVYQLISRRRFQQMEVLEGQNILVTISGKKNRVRVYYLSWLKSKILRTDGLSDQVERRNGWINVGDLQGAVHFKIVKYERIKFLVIALKDSIEIYAWAPKPYHKFMAFKNFGELEHRPLLVDLTIEDQSRLKVIYGSAEGFHAVDLDSAEVYDIYLPKHTQGAIIPHCIVALPNSNGMQLLLCYDNEGVYVNTVGRVSKNIVLQWGEMPTSVAYIGTGQIMGWGNKAIEIRSVESGHLDGVFMHKKAQRLKFLCERNDKVFFSSAKGASSCQIYFMTLNKPGMANW
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. Required for the de novo DNA methylation directed by the RdDM pathway.
Subcellular Localization:
Nucleus. Note=Detected as small foci dispersed throughout the nucleoplasm.
Sequence:
MSEKGGKGLKSSLKSKDGGKDGSSTKLKKGRKIHFDQRTPPANYKILNVSSDQQPFQSSAAKCGKSDKPTKSSKNSLHSFELKDLPENAECMMDCEAFQILDGIKGQLVGLSEDPSIKIPVSYDRALAYVESCVHYTNPQSVRKVLEPLKTYGISDGEMCVIANASSESVDEVLAFIPSLKTKKEVINQPLQDALEELSKLKKSE
The following text describes a protein:
Function:
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Sequence:
MAHATQSPDAYDALLDHYETITGLGGAAGILSWDQEVMMPEGGTPARSTQKSAVSTVRHDLLTDQQVADWLDDLADADLTDEQAAVVREIRREHERAARVPSDLIADLSEKTSEAHPKWKQAREEDDFSIFAPVLEDLIDLKREYANHIDPDADAYEVLFADYEPYLDLDTAERVLERLRDELVPLIADIRDSDVTLADPFAGSQFDVDTQEDLARDVLDTLGYDWEHGRIDTAPHPFSSGTPFDARVTTRFDPEKPVDALLSTIHEFGHARYTLGLPRAEYGTPLGESRDLTVHESQSRLWENHIGRSPAFWEAFLPEMKTQFPQVEDATPQAAFEAANEIFEDNLIRVEADELTYHMHIVVRFEIERELIEGDLDVADVPEAWNDKYEEYLGVRPETDAEGCLQDIHWSQGSIGYFPTYSLGSVLAAQIFAALEADIGPVDERVREGDFDVVGDWLESNVHQHGARYTTPDLVREATGEAFTADYFLDHVHEKYGELYDL
The following text describes a protein:
Function:
Tjp1, Tjp2, and Tjp3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PatJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (By similarity). Promotes cell-cycle progression through the sequestration of cyclin D1 (Ccnd1) at tight junctions during mitosis which prevents Ccnd1 degradation during M-phase and enables S-phase transition. With Tjp1 and Tjp2, participates in the junctional retention and stability of the transcription factor DbpA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to Tjp2, Tjp3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, tight junction. Nucleus. Note=Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (By similarity). Shows an epithelial-specific tight junction localization in a Tjp1/Tjp2-dependent fashion.
Sequence:
MEELTIWEQHTATLYKDPRRGFGIAVSGGHDRASGSVVVSDVVPGSPAEGRLRTGDHIVMVNGVSVENVTSAFAIQILKTCTKTANVTVKRPRRVQLPATKASPASGHQLSDQEEADHGRGYEGDSSSGSGRSWGERSRRSRAGRRGRVGSHGRRSSGGGSEANGLDLVSGYKRLPKQDVLMRPLKSVLVKRRNSEEFGVKLGSQIFIKHITESGLAARNHGLQEGDLILQINGVSSANLSLSDTRRLIEKSEGELTLLVLRDSGQFLVNIPPAVSDSDSSLMEDISDLTSELSQAPPSHVPPPPLKGQRSPEDSQTDSPVETPQPRRRERSVNSRAIAEPESPGESRYDIYRVPSRQSLEDRGYSPDTRVVSFPKGASIGLRLAGGNDVGIFVSGVQAGSPADGQGIQEGDEILQVNGMPFRNLTREEAVQFLLGLPPGEDMELVTQSKTGHSLRRWSQSRVGDSFYIRTHFELEPSPPYGLGFTRGDVFHVVDTLYPGSGPGHGHSSHGGLWLAARMGRDLREQERGVIPNQSRAEQLASLEAAQRAAGVGPGASVGSNPRAEFWRLRSLRRGTKKASTQRSREDLSALTRQGHYPPYERVVLREASFKRPVVILGPVADIAMKKLTTEMPEEFEIAESMSRTDSPSKIIKLDTVRVIAERDKHALLDVTPSAIERLNYVQYYPIVIFCAPESRPALKALREWLAPASRRSSRRLYAQAQKLQKHSGHLFTATIPLHGTSDSWYQEVKAVIQQQQARPIWTAEDQLNSSSEDLDLTGHGLAASSGDLSCDSRTNSDYEDTDGEGAYTDREGGPQDVDEEVAPTALARSSEPVWVDDHQGLMGHGTTITDKWETQADSHYTQDQRRQDSMRTYKHEALRKKFTRARDVESSDDEGYDWGPATDL
The following text describes a protein:
Function:
Might be involved in RNA metabolism; it is missing helicase motif III and may not have helicase activity.
Subcellular Localization:
Nucleus.
Sequence:
MGLELAAVLTRPRAASRSCQRATMASQPLRLAEEYGPSPGESELAVNPFDGLPYSSRYYELLEQRHTLPIWAARFTFLEQLESNPTGVVLVSGEPGSGKSTQIPQWCAEFVLARGFQKGQVTVTQPYPLAARSLALRVADEMDLTLGHEVGYSIPQEDCTGPNTLLRFCWDRLLLQEVASTRGTGVWGVLVLDEAQERSVASDSLQGLLQDARLENLPGDLRVVVVTDPALEPKLQAFWGNPPIVHIPREAGERPSPIYRDTIPPDRVEAACQAVLELCRKEAPGDVLVYLPSEEEISLCCESLSREVESLPLQRLPPRVLPLHPDCGQAVQAVYEDMDARKVVVTHWLADFSFSLPSIQHVIDSGLELRSVYNPRIRAEFQVLRPISKCQAEARRLRARGFPPGSCLCLYPKSFLELEAPPLPQPRVCEENLSSLVLLLKRRQIAEPGECHFLDQPAPEALMQALEDLDYLAALDDDGDLSDLGVILSEFPLAPELAKALLASCEFDCVDEMLTLAAMLTAAPGFTRPPLSAEEAALRRALEHTDGDHSSLIQVYEAFIQSGADEAWCQARGLNWAALCQAHKLRRELLELMQRIELPLSLPAFGSEQNRRDLQKALVSGYFLKVARDTDGTGNYLLLTHKHVAQLSSYCCYRSRRAPARPPPWVLYHNFTISKDNCLSIVSEIEPQMLVELAPPYFLSNLPPSESRDLLNQLREGMADSSAGSESSSVQEFRDPCVLQ
The following text describes a protein:
Function:
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSRQPLEHTRRYGSRESGSSCQLTVSGSTEDGSSTEVSNPTDYTEYDVSSSVPDCDLSKVEDYGDDRRFSMYSMRSNLRSSRPVSAAPSYRPFEYDLNGNIIESNFEEPIYEKGDWTEAPSYISNYEVERELPKLPVITETNTLRRDVPQYSVKEVPLVDGNLIVDYSVSKQLLALQGTFADQPEAQTLRYSAVTCEPEETQDKGYKLRQQIYGRETEIAVCLTLEKESVHQFINTLQCVMENIADLCSRESSRFWNTDSWQKVVVCIIADGDGDLDCSFVDVLSSLGVYQHRSGSKMVSGSPVLAHIYEYTSCLRIDQQFYITSMESVPINLIYCKKAQSCGKVNSHRWFLNGIAKLLQPKVCFFIKAGTAINETAIYHIWKQFTTDNKVGGVCGNTNIELPNWYSTLCNPLLAVRNFELQTYKCMQYPFDSCMGYVIDIPGKFYAYRYAVLVEDAFCSEPLKDYFQKDISGSNSRKIFGTNACLAEESLLSWSVMLRPKTDWVMKYVDTVKATIRSQNSIASYLDNAKYEVNTSLGSTLYALSRFPSIWETNHSTLRQFSLSFKVLLNSLELQVNYFAMANLFSVFYFVCHATSTSDYDLFGHGWGNHIFVFFYYVFICLIFSQFVLALGNRPYATHSLYLGSMCISVIVCIYFLICLFYVACKNASNSSSNGDSILGNNSFTTLLFCPLMMFLFHLITALLQLNPWHILTGSIPYVLLLPFRVFTKNIFAFCHMHDTLQLGERKHYVDIEDGLLECVRSNNSQTIVLSIPTEEDVENQYHASRNNLHGDASDMTMNHIVSESQQSRMFADYTRSIRTRFVLLWALCNLVLAMILTQSLNDTSIDDNGYVKFIFWLLFSFSALKMMGAFSYATIQLFQKLRTKVYSPKHET
The following text describes a protein:
Function:
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrium between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
Subcellular Localization:
Cytoplasm.
Sequence:
MIQLAQNAKHPSKKEQKPLVNEQIAFNQFTLIDENSTNLGIVKMENALKLAQEKQLDLVLIAPNPTKPIVKLLDFGRYTYDLKRKKRQAKKNQTIIQTKEVVVKPTIAKHDLEFRAKQSKNWIEKGHHVKFIVRAFGRVSTRIELIEKVFDDFYQLVKDVVEIQKPLTASSKTMYAALLVPLKR
The following text describes a protein:
Function:
May cause the redistribution of PAPOLB from the cytosol to the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Colocalizes with PAPOLB in the endoplasmic reticulum.
Sequence:
MAKMELSKAFSGQRTLLSAILSMLSLSFSTTSLLSNYWFVGTQKVPKPLCEKGLAAKCFDMPVSLDGDTNTSTQEVVQYNWETGDDRFSFRSFRSGMWLSCEETVEEPALLHPQSWKQFRALRSSGTAAAKGERCRSFIELTPPAKREILWLSLGTQITYIGLQFISFLLLLTDLLLTGNPACGLKLSAFAAVSSVLSGLLGMVAHMMYSQVFQATVNLGPEDWRPHVWNYGWAFYMAWLSFTCCMASAVTTFNTYTRMVLEFKCKHSKSFKENPNCLPHHHQCFPRRLSSAAPTVGPLTSYHQYHNQPIHSVSEGVDFYSELRNKGFQRGASQELKEAVRSSVEEEQC
The following text describes a protein:
Function:
Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Sequence:
MTMGDDLWGWQNINGSPYLTCALLAPWPHAFFTRAFYPQLPEQLITYLDPQGKAFRVKQVHGDVTLTATEIGQTPLAPDSTHPPADGIISDAPHQGVWVASADCTPVLIGDLIGKRVAAIHAGWRGTKARIVPKTIDKFLALGSELKDLRVALGPAIAGEVYQVDPWVALEVGQSVQAVQKLATEEQQWDHLSTMVNPPVLPDAEPEKYRLDVRRINQLQLLELGFAQEQIAVAPHCTFQMEELFFSYRRTHTKEVQWSGIVSY
The following text describes a protein:
Function:
Inhibits sodium channel Nav1.7/SCN9A with high potency (IC(50)=117 nM) and Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.6/SCN8A and Nav1.5/SCN5 with weaker potency. Also inhibits voltage-gated calcium channel Cav3.1/CACNA1G, Cav3.2/CACNA1H and Cav3.3/CACNA1I.
Miscellaneous:
MISCELLANEOUS: Negative results: does not show activity on voltage-gated potassium channels (Kv).
Subcellular Localization:
Secreted.
Domain:
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Sequence:
ECRWFLGGCSGGQTCCEHLVCHRKHQWCVWDWSF
The following text describes a protein:
Function:
Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor. Note=Shuttles between the plasma membrane and the Golgi apparatus.
Sequence:
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGLLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM
The following text describes a protein:
Function:
Catalyzes the phosphorylation of mevalonate (MVA) to yield mevalonate-3-phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Sequence:
MTYRSIGSTAYPTIGVVLLGGIANPVTRTPLHTSAGIAYSDSCGSIRSETRIYADEATHIYFNGTESTDDNRSVRRVLDRYSSVFEEAFGTKTVSYSSQNFGILSGSSDAGAASIGAAILGLKPDLDPHDVENDLRAVSESAGRSLFGGLTITWSDGFHAYTEKILDPEAFSGYSIVAFAFDYQRNPSDVIHQNIVRSDLYPARKKHADEHAHMIKEYAKTNDIKGIFDLAQEDTEEYHSILRGVGVNVIRENMQKLISYLKLIRKDYWNAYIVTGGSNVYVAVESENADRLFSIENTFGSKKKMLRIVGGAWHRRPE