lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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; This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MRKVRGAKAKKYAKQFLSLVNIDQVPEIVSKLETVVMLMQKEKQFRNMLTSPSFKDEERVGVIGYLCEKLGLPEETKKFLNFLSIEGVLIGLGEIVRYINALYLEAKKKVKGIVTSAVELPENIKQKIVESLKAITGRDVELQYEIDPSLIGGVRVKVGSTMYDLSIKGQLGLLRDKLIKG
The following text describes a protein:
Function:
Inhibits the secretion of pituitary hormones, including that of growth hormone/somatotropin (GH1), PRL, ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-stimulated secretion of GH1 and LH; the inhibition of ghrelin-stimulated secretion of GH1 can be further increased by neuronostatin; May enhance low-glucose-induced glucagon release by pancreatic alpha cells. This effect may be mediated by binding to GPR107 and PKA activation. May regulate cardiac contractile function. May compromise cardiomyocyte viability. In the central nervous system, may impair memory retention and may affect hippocampal excitability. May also have anxiolytic and anorexigenic effects. May play a role in arterial pressure regulation. May inhibit basal, but not ghrelin- or GnRH-stimulated secretion of GH1 or LH, but does not affect the release of other pituitary hormones, including PRL, ACTH, FSH or TSH. Potentiates inhibitory action of somatostatin on ghrelin-stimulated secretion of GH1, but not that on GnRH-stimulated secretion of LH.
Subcellular Localization:
Secreted.
Sequence:
MLSCRLQCALAALSIVLALGGVTGAPSDPRLRQFLQKSLAAAAGKQELAKYFLAELLSEPNQTENDALEPEDLSQAAEQDEMRLELQRSTNSNPAMAPRERKAGCKNFFWKTFTSC
The following text describes a protein:
Function:
Part of the ESX-5 specialized secretion system, which is responsible for the secretion of EsxN and a number of PE_PGRS and PPE proteins, including PPE41.
Miscellaneous:
MISCELLANEOUS: Part of the eccB5-eccC5 operon, which is essential for in vitro growth.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MKRGFARPTPEKPPVIKPENIVLSTPLSIPPPEGKPWWLIVVGVVVVGLLGGMVAMVFASGSHVFGGIGSIFPLFMMVGIMMMMFRGMGGGQQQMSRPKLDAMRAQFMLMLDMLRETAQESADSMDANYRWFHPAPNTLAAAVGSPRMWERKPDGKDLNFGVVRVGVGMTRPEVTWGEPQNMPTDIELEPVTGKALQEFGRYQSVVYNLPKMVSLLVEPWYALVGEREQVLGLMRAIICQLAFSHGPDHVQMIVVSSDLDQWDWVKWLPHFGDSRRHDAAGNARMVYTSVREFAAEQAELFAGRGSFTPRHASSSAQTPTPHTVIIADVDDPQWEYVISAEGVDGVTFFDLTGSSMWTDIPERKLQFDKTGVIEALPRDRDTWMVIDDKAWFFALTDQVSIAEAEEFAQKLAQWRLAEAYEEIGQRVAHIGARDILSYYGIDDPGNIDFDSLWASRTDTMGRSRLRAPFGNRSDNGELLFLDMKSLDEGGDGPHGVMSGTTGSGKSTLVRTVIESLMLSHPPEELQFVLADLKGGSAVKPFAGVPHVSRIITDLEEDQALMERFLDALWGEIARRKAICDSAGVDDAKEYNSVRARMRARGQDMAPLPMLVVVIDEFYEWFRIMPTAVDVLDSIGRQGRAYWIHLMMASQTIESRAEKLMENMGYRLVLKARTAGAAQAAGVPNAVNLPAQAGLGYFRKSLEDIIRFQAEFLWRDYFQPGVSIDGEEAPALVHSIDYIRPQLFTNSFTPLEVSVGGPDIEPVVAQPNGEVLESDDIEGGEDEDEEGVRTPKVGTVIIDQLRKIKFEPYRLWQPPLTQPVAIDDLVNRFLGRPWHKEYGSACNLVFPIGIIDRPYKHDQPPWTVDTSGPGANVLILGAGGSGKTTALQTLICSAALTHTPQQVQFYCLAYSSTALTTVSRIPHVGEVAGPTDPYGVRRTVAELLALVRERKRSFLECGIASMEMFRRRKFGGEAGPVPDDGFGDVYLVIDNYRALAEENEVLIEQVNVIINQGPSFGVHVVVTADRESELRPPVRSGFGSRIELRLAAVEDAKLVRSRFAKDVPVKPGRGMVAVNYVRLDSDPQAGLHTLVARPALGSTPDNVFECDSVVAAVSRLTSAQAPPVRRLPARFGVEQVRELASRDTRQGVGAGGIAWAISELDLAPVYLNFAENSHLMVTGRRECGRTTTLATIMSEIGRLYAPGASSAPPPAPGRPSAQVWLVDPRRQLLTALGSDYVERFAYNLDGVVAMMGELAAALAGREPPPGLSAEELLSRSWWSGPEIFLIVDDIQQLPPGFDSPLHKAVPFVNRAADVGLHVIVTRTFGGWSSAGSDPMLRALHQANAPLLVMDADPDEGFIRGKMKGGPLPRGRGLLMAEDTGVFVQVAATEVRR
The following text describes a protein:
Function:
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MIHWDQSRTLLSFPRVGLHLSWYGILFSLGIFLSSFSGIKLATALCKDREEKKELRTSLENFALGALLAIIIGARLAYVLFYGGSFYFENPSEIIKIWKGGLSSHGAVISVVIWAAVFSRLHIRKLPMLSVTYICDLCGAVFGCAALLIRVGNFMNQEILGTPTSMPWGVIFPNGGGQIPRHPVQLYEGLGYLVLSCILYRLCYRGVIRLGSGYSAAGALIGVAVIRFCAEFFKTHQGAWLGEENILTIGQWLSIPMIFLGVGIIWIASKKK
The following text describes a protein:
Function:
Receptor for basic fibroblast growth factor.
Subcellular Localization:
Endomembrane system. Membrane; Single-pass membrane protein.
Sequence:
EKETAADPRWEFPRCRLKLQSQLDVGCFGRILKAEAKGIVPNEPVTTVAVKTVHSNDDFKAKHGLLEEFKILSQLGRHLNIVHLLGACTKYTNKEPLLIVFEYCPFSNLRAHLITFRHRFFGELNESRNLMPRDHFHGQNNTGNRTFSTRDLIYWAYQISRAMAYLVVKKVLHRDLALRNILLTANNIVKVSDFGMSLQTHSGTESRNNEELLPIKWMAIEALKDGLFSHQSDVWSFGVVLWELFTLGETPYTVYAKANKDFLVRILLMGRRLKKPTNAPEFVSAIMYSCWRSEPLQRPIFHELEKMFYAQLEPHAVLELMKLDENYIKMSRERDMETDTPCCINVAKHDSNCFD
The following text describes a protein:
Function:
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSFDEMTPKEIVQELDKYIVGQYEAKKAVAIAVRNRIRRQKLPEEWRKEVLPKNILMIGPTGVGKTEIARRLAQLSGSPFLKVEATRFTEVGYVGKNVDSMIRDLVEISVNMVKQEKIKEVERQAEELVEERILDALVPESKAMPVVTNPFINLITGGQQQQYTPEDRRRFRAKREEMREKLRKGELEDEEIEIELEETVSPFMGIFGPGMEDLGIEITNMFSGMLPKRKKKRKMKVSEARKVLLPLEAEKLIDMDKVVQEALDRAQNRGIIFIDEIDKIAGKESAVGPDVSRQGVQRDLLPIVEGTTIMTKYGPVRTDFILFIAAGAFHVSRPSDLIPELQGRFPIRVELSPLTEEDFVRILKEPENAIIKQYQALLSTEGVELVFTEDGIREMARIAYQLNQRLENIGARRLYTVAEKVLEEISFEAPDIPEKRVVVDAEYVRRRLEKIVQDEDLSAYIL
The following text describes a protein:
Function:
Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators; Bifunctional enzyme. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid. Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates.
Subcellular Localization:
Cytoplasm. Peroxisome.
Sequence:
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM
The following text describes a protein:
Function:
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Subcellular Localization:
Secreted.
Sequence:
GVSVSHASKKITRATTIFSNTEYENFTEAETIRGNVTQRSQSSDDFTRIVGGENAKPGQFPWQVLLNGKVEAFCGGSIINEKWVVTAAHCIKPDDNITVVAGEYNIQETENTEQKRNVIRIIPYHKYNATINKYNHDIALLELDKPLTLNSYVTPICIANREYTNIFLNFGSGYVSGWGRVFNRGRQASILQYLRVPFVDRATCLRSTKFTIYNNMFCAGFDVGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAIKGKYGVYTRVSWYVNW
The following text describes a protein:
Function:
Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity).
Subcellular Localization:
Secreted.
Sequence:
EDHPVHNLGEHSVCDSVSAWVTKTTATDIKGNTVTVMENVNLDNKVYKEYFFETKCKNPNPEPSGCRGIDSSHWNSYCTETDTFIKALTMEGNQASWRFIRIDTACVCVITKKTGN
The following text describes a protein:
Function:
Alpha-ketoglutarate-dependent sulfate ester dioxygenase, which oxidizes medium-chain alkyl-sulfate esters. Shows preference for 2-ethylhexyl sulfate (2-EHS) in vitro, leading to the formation of succinate and 2-ethylhexanal. Has likely a role in sulfate scavenging in vivo; Also causes the inactivation of the 2-carboxyquinoxaline Ty38c (an antitubercular compound that inhibits DprE1) via oxidative decarboxylation, using Ty38c instead of alpha-ketoglutarate as a substrate. Is thus responsible for primary resistance of M.tuberculosis to Ty38c in vitro. Overexpression of Rv3406 causes resistance to Ty38c.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Sequence:
MTDLITVKKLGSRIGAQIDGVRLGGDLDPAAVNEIRAALLAHKVVFFRGQHQLDDAEQLAFAGLLGTPIGHPAAIALADDAPIITPINSEFGKANRWHTDVTFAANYPAASVLRAVSLPSYGGSTLWANTAAAYAELPEPLKCLTENLWALHTNRYDYVTTKPLTAAQRAFRQVFEKPDFRTEHPVVRVHPETGERTLLAGDFVRSFVGLDSHESRVLFEVLQRRITMPENTIRWNWAPGDVAIWDNRATQHRAIDDYDDQHRLMHRVTLMGDVPVDVYGQASRVISGAPMEIAG
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPIKLAQTNKEIKTTFNPFWSAAVVNEKNNWKNFKKFSAIFIKVIKVFIFIFLTIVGLWGCTQTLAQPWTGTNQVLGSGLEIGYKFGTTGDYRYDLISNNFGPYFTFSDYTLAYGPFYGWFVWPAAQIVLPIMYATRVPLGSGVELGFNMILSLIVLLLLVRLITIVITLNSTLALEKMNEVQGKLAEINAKYKGAIDLQSKRNRQLEIMSLYKKHNIKSSAAFVQVFVTLPIFLIIYRIVTTLRPIKAIILFNFWDLSKVPLTEIFSNFTTTGWPFIIFLVIVLPVQFLSQKLPQVWASKRNENAKAHSQKSIEQLNKTKKMQLIFYFVFAAITAFSAAGVGVYWFLNALFTLLQSYLTHVFIVKRREKRKQNYSKLDLILERE
The following text describes a protein:
Function:
May be involved in maturation of the 30S ribosomal subunit.
Sequence:
MHLAALLEGKMPTAREVRADLLIERLKEELKKFDGIKPPDWAYYTKTGSHKERPPIQEDWWYIRAASLLRTLYLRGEPVGVERLRTKYGGRKKRGVRPERFAKGSGHVIRLILQQLESLGLVEKVEGRGRRISPAGISLLDKLAGEIIKELNITPGKVVPP
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Sequence:
AEKSDTVVTWEDQQNINKFSKLNNRFHELEDEIKFAKETNDNLEDAGNELILTDEDIVRFQIGEVFAHVPREEVEIRIEEMKEVNSKTLEKLEKEKETVLAQMNELKKILYGKFRDSINLEED
The following text describes a protein:
Function:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTFLALFLLIGLASIFCGSVLSSLTLRLILELAPKLEKAGLSGRDLNKAVSEKIPEDAGLGPSAMFLLTISLWSLVMPRSSTLLSAGFSIMASSFLGFVDDVVNLRWRYKLIVPSITLLPLVGAYSGSGLSLGPLRLTSSMTKLYCLLFAIFSQNAVNIYAGINGLEVGQSIVACTFLLPIVLYKLYVALDTTRYAEHLAPWQRLLSHPSLLSSLVIIVCFLAVSHPVYLLNRYPSRVFVGDIYAYFAGSVFASACILSDTLIAGPLLFLPQILNFVLSVPQLFGIVPCPRHRLPRFSQDHGTLTGVATHLNLINQYLRIRGPLSEKRLCRELLSIQAIISAFVVLFFVLARGKVENSFVGVHRKL
The following text describes a protein:
Function:
Plays a regulatory role in abscisic acid (ABA) signaling and tolerance to abiotic stress during germination. May be involved in the regulation of the ABI transcriptional factors.
Sequence:
MDKEKDHEVEWLEAQKIEISVDLLAAAKQHLLFLETVDRNRWLYDGPALEKAIYRYNACWLPLLVKYSESSSVSEGSLVPPLDCEWIWHCHRLNPVRYNSDCEQFYGRVLDNSGVLSSVDGNCKLKTEDLWKRLYPDEPYELDLDNIDLEDISEKSSALEKCTKYDLVSAVKRQSPFYYQVSRSHVNSDIFLQEAVARYKGFLYLIKMNRERSLKRFCVPTYDVDLIWHTHQLHPVSYCDDMVKLIGKVLEHDDTDSDRGKGKKLDTGFSKTTAQWEETFGTRYWKAGAMHRGKTPVPVTNSPYASDVLVKDPTAKDDFQNLIQFPEVEVVEVLLEIIGVRNLPDGHKGKVSVMFSKTQPDSLFNAERRLTILSEVGEKQVATFQCEPTGELVFKLISCSPSKIPVSREPKNLGFASLSLKEFLFPVITQLSVEKWLELTPSKGSQTDTKPISLRVAVSFTPPVRSPSVLHMVQSRPSCKGSCFFPIIGKSRLAKSSTHIVDETQTEVITLQIRNSADGGILKDDQRQVMGVTDSGETRVLAVYTGSFWSLLDSKWSLKQINASTADNPLFEILGPRVVKIFSGRKLDYEPKHCANLRSDLDFMTLVEFSKQHPYGKTVGLVDMRFGSIEAKENWLLLPGIVSAFILHTVLKKGGSEGFNVTTKDIKEESKQTKLVAATENNVNANSTNVETQTAITAPKKGSGCGGGCSGECGNMVKAANASGCGSSCSGECGDMVKSAANASGCGSGCSGECGNMVKAANASGGGYGARCKAAKASGCGGGCGGGCGGGCGDMVKSVNASGCGGGCNGECGNMVKAA
The following text describes a protein:
Function:
UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens). Displays glucuronidation activity toward several classes of xenoblotic substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4-hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins). Catalyzes the glucuronidation of monoterpenoid alcohols such as borneol, menthol and isomenthol, a class of natural compounds used in essential oils.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MSGKWISALLLLQISFCFKSGNCGKVLVWPMEYSHWMNIKIILEELVQKGHEVTVLRPSAFVFLDPKETSDLKFVTFPTSFSSHDLENFFTRFVNVWTYELPRDTCLSYFLYLQDTIDEYSDYCLTVCKEAVSNKQFMTKLQESKFDVVFSDAIGPCGELIAELLQIPFLYSLRFSPGYTIEQYIGGVLFPPSYVPMIFSGLAGQMTFIERVHNMICMLYFDFWFQTFREKKWDPFYSKTLGRPTTLAEIMGKAEMWLIRSYWDLEFPHPISPNVDYIGGLHCKPAKPLPKDIEDFVQSSGEHGVVVFSLGSMVRNMTEEKANIIAWALAQIPQKVLWRFDGKKPPTLGPNTRLYKWLPQNDLLGHPKTKAFVTHGGANGIYEAIHHGIPMIGIPLFAEQHDNIAHMVAKGAAVEVNFRTMSKSDLLNALEEVIDNPFYKKNAMWLSTIHHDQPTKPLDRAVFWIEFVMRHKGAKHLRSLGHNLPWYQYHSLDVIGFLLSCVAVTVVLALKCFLFVYRFFVKKEKKTKNE
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MDCAEEKAKSLRRQIADTEAELAQLKLQLLSLEEKDTNSKNLEAKTSASEKDDPVTHIENKWPMSLEEYKRYGRQMIVPDIGIKGQLRLKSASILLVGAGGLGCPAAAYIAGAGVGTIGIVDGDIVEESNLHRQILHSTDRVGVNKAGIVKDYDIVLDCTDHPTSRYLISDICVLLQKPLVSASALRTDGQLIVLNNPALPPGDLSGGSCYRCVFPKPPPPEAVTSCGDGGIIGPVVGVMGVLQALEAIKLIASGKLAAVGENDNTSPTPKMNPTTMLLFSTNGSTPFRNVRLKGRRSNCFACGEEAQLALEQMSSGSMDYVLFCGMTHPVKLLSDEERIEARDYDSIRKEKEHLLIDVREKVQFDICNIEGSYNIPFSSFQGSKGSSDHPLSTLTENLNPKTPIYVVCRLGNDSQIVTKKMKDLGLDQKGDRYIGDIKGGLRSWKEQVDGSWPEY
The following text describes a protein:
Function:
May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells.
Sequence:
MAQVLNLNNEVVKMRRDVKKARVFIIRKLTRHVAKLKTKKGKAEDIERNLRRVERLIEEIHAMKALKPDEVTKAALQRNLIFEKVCKNPNSTTAERATARIASHPLISKKIIDIKAAIKAFKEERIQKSSESKKAPEKPNSGKNTKKPINKTSDHSTTEEEDSTAELAEMNNEEIKKEKEVQKSENDQDKFKPERTSEPLVQQTIPTKSLTPDVLQTTSAVKKGQQTSTSKEAISPANTEGKIRIQGSQSVSEESELDDSDAEEKEYFDDSTEERFYKQSSHSEDSGSEDGDGFFIGKVNKVKKKSHHLGPRQEKKNLDVKKATEDVLKKASPATHMSVDEKKGLQNSKQMKLKSVFCSTLSGSKASRPQHGKRNPHENSQAYKSTAATVKNKPQFQKHKAHLSTGRFPSPAQQTQQSLHPSWEASRRRKEQQAQIMAFQGKKIKFDD
The following text describes a protein:
Function:
Serine protease that catalyzes the first step (site-1 cleavage) in the proteolytic activation of various factors, prior to site-2 cleavage. Part of a regulated intramembrane proteolysis (RIP) cascade. Cleaves BZIP17 and BZIP28 after the Arg-Arg-Ile-Leu (RRIL) motif. May cleave BZIP49 after the RRIL motif. Targets the membrane-associated BZIP17 factor, which functions as a stress sensor and transducer in a signaling pathway that resembles an ER stress response. Following salt stress, BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the C-terminus and the N-terminal bZIP component is translocated to the nucleus, where it activates the expression of salt stress response genes. Cleaves the pectinesterases PME1 after the Arg-Arg-Leu-Met (RRLM) and Arg-Arg-Leu-Leu (RRLL) motifs, and PME5 after the Arg-Arg-Leu-Leu (RRLL) and Arg-Lys-Leu-Met (RKLM) motifs. This processing and C-terminus release occurs in the Golgi apparatus and is required for cell wall targeting of pectinesterases. Thus, SBT6.1 mediates the regulated release of mature pectinesterases from the Golgi. Cleaves the peptide growth factor RALF23 after the Arg-Arg-Ile-Leu (RRIL) motif. This processing is required for RALF23 function in the negative regulation of brassinolide (BL)-mediated signaling pathway (e.g. BL-induced hypocotyl elongation and branching limitation).
Subcellular Localization:
Golgi apparatus membrane; Single-pass membrane protein.
Sequence:
MKVLGEASSYPYRSCIIVVFLSVSLFWLRPSTYHPQQQNLNPENVTRLESENETKTNYIIRFKQYKPAKDHRIYLESKVRSGGWGWIERINPATKYPTDFGVLWIEESGKEAVVGEIERLEMVKDVNVEFKYQRVLLGGSFPDGKKRPGKIFTSMSFEEGTESSPMADTSNTTLNWSRHLLAQKTQVTSMFGADHLWKKGYTGAKVKMAIFDTGIRADHPHFRKIKERTNWTNEDTLNDNLGHGTFVAGVIAGRNPECLGFASDTEIYAFRVFTDAQVSYTSWFLDAFNYAIATDMDVLNLSIGGPDYLDLPFVEKVWEITASNIIMVSAIGNDGPLYGTLNNPADQSDVIGVGGIDNDDHIASFSSRGMSTWELPHGYGRVKPDVVAYGRDIMGSKISTGCKSLSGTSVASPVVAGIVCLLVSVIPEARRKDLLNPASMKQALVEGAAKLSGPNMYEQGAGRVDLLESYEILKSYHPRASIFPSILDYNDCPYSWPFCRQPLYAGAMPIIFNTTILNGMGVIGYIESPPTWHPANEEGNLLSIHFKYPDVIWPWTGYLALHMQIKEEGAQFTGEIEGNVTVKVYSPPASGESGPRRSTCSLQLKLKVIPTPPRAKRILWDQFHSIKYPPGYIPRDSLDVRNDILDWHGDHLHTNFHIMYNMLRDAGYYIETLGSPLTCFDAQQYGTLLMVDLEDDYFPEEIEKLRDDVINTGLGLVVFAEWYNVDTMVKMRFFDDNTRSWWTPVTGGANIPALNNLLASFGIAFGDKILNGDFSIDGEQSRYASGTNIVRFPAGGFLHTFPLLDSSESGATQNLLLTEASKEDPAVLGLLEIGEGRVGVYGDSNCLDSSHMVTNCYWLLKKMLDFSSSNIKDPVLFSKFAKRYSPVIIDEKQLPSRRTDVNFSTYSSVIGKELICESDSRFEVWGTKGYNLHVRGRNRRLPGYHGIDLGRGLNFTVESKRPTRWRSAKEGGELSSSRSKSLGGLFNRDEIDMPFLVPTRWIVLAGVVASGVLVLLSIWRIRQKRGRRRRASGSNRLA
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Localization:
Nucleus.
Sequence:
MMSTNNNNHYRGWTTTSVGEENEELEDLLNHLSSAAGDRGLGEGSGLDDETMPAFDDILQPASSSTARDRAGLTALLPFDYPPDGHEHDDDDDDDEDDEDDEDDDEDVDEERKAAVQAAMRGLHTPFTHLSRSERAQTLIEEDGEEEDEQSDEEQVKGGKEEEEEGWEMARPIEEEGAEGLVKIESEDEEPSALPTISLDHREASPLGLPERPGEEEEEEVDPKEEEEEEEIPATLGGVDAVSSVPEDGPTGSSELVMRDKPGVAGLPIRGPNSTERPVFVNPKQYQRIIKRRLARARLEEMGRLSRERQPYLHESRHKHAVRRPRGPRGRFLTKEELARADHPNIDPTPDPIPTAT
The following text describes a protein:
Function:
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Localization:
Cell outer membrane; Lipid-anchor. Bacterial flagellum basal body.
Sequence:
MSTRRLPALLLPLALLAGCQNNQTLKEIGNAPAMSPIGSGLQFSQTPQMGMYPKQPKHMASGYSLWSDSQGALFKDLRALNIGDILTVNIQINDKADFDNETERNRTNASGLNWKAKAQILGWTPDADSSIKYGSDTDTQAKGKTKRSEKLTLLVAAVVTGILENGNLIISGSQEVRVNHEIRILNVGGIVRPQDVDAQNIISYERIAEARISYGGRGRLTEVQQPPVGQQVVDLFSPL
The following text describes a protein:
Function:
Vasodilator protein that inhibits vasoconstriction of isolated rat femoral artery induced by phenylephrine. Since platelet aggregation and vasoconstriction are key hemostatic responses, particularly in small wounds, this protein likely participates in the antihemostatic responses during blood feeding. Blocks L-type calcium channels (Cav1/CACNA1) in left ventricular myocytes isolated from rat hearts.
Subcellular Localization:
Secreted.
Sequence:
MKFALFSVLVVLLIATFVAADECPRICTADYRPVCGTPSGGRRSANRTFGNQCSLNAHNCLNKGDTYDKLHDGECK
The following text describes a protein:
Function:
Transcription factor. Determines the fate of epidermal cell differentiation. Represses trichome development by lateral inhibition. Together with GL3 or BHLH2, promotes the formation of hair developing cells (H position) in root epidermis, probably by inhibiting non-hair cell formation. Represses the expression of GL2 and WER in H cells. Positively regulates stomatal formation in the hypocotyl.
Subcellular Localization:
Nucleus. Note=Moves from developing non-hair cells (atrichoblasts) to developing hair cells (trichoblasts).
Sequence:
MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK
The following text describes a protein:
Function:
May play a role in insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
Sequence:
MSAAETGPIASGSAVSTGQRGVSRVLAKLSQSLAGGEFYEAHMMYRTLYFRYTAQKRYQDCLELLFDGAQQLIAKEQESSAADLCLLLVDTLEKRGPQAEDTDNFLWVPRLGALIRGLNSATVERETLIQRTIKWSTALHGQYGHPVLHKLIAHVFWTEGNIESARHHYLLCQDGSLCGRVLIEISQSRGFQGEMDLFLVQAVLQQLSLKDRKTAEDTFTEYTRYHAKLLKHEFPYKEPLVNFLYFLFRLIDAKRVAGFRALRKLYDPSLKRDTSFLKYVAKIGVLYFDEHPEAAHSGPPGLGGMFGDIFNRLMAGFEEDDADDHDTTLRRQNENNELE
The following text describes a protein:
Function:
Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MSANTHWQKLRHIADRLALCNILMLLQKSISHMRRCRNIATTLRNHREIAQKLPLSVPLPLKNPEGVKVIPKGSPPIGRNSRVTKLENGLRICTEDTYGDFVTVGVAVESGCRFENGFPLGISRVVEKLAFNSSENFEGRDDIFAQLESNSGIVDCQSTRDTMMYAASCHRDGTDSVMNVIADTIFRPTIDETGLEQAKMTAHYENIDLPTRIEAIEILLTDYIHQAAFQHNTIGYPKYGMGSMDRIRVSDVYGFMSRAHTPERMVVGGVGIDHDEFVSIVTRHFDQKNSIWNRKSTLLPPKIPEIDISRSQYTGGEVRMQKDLKPLTIGKPYPLLAHVVLGLEGCGYKDEDFVAFCVLQSLLGGGGAFSAGGPGKGMYARMYTELMNRHHWIYSAIAHNHSYSDGGVFTVTASAPPDNIHDALILLVHQILQLQQGIDPTELARARTQLRSHLMMNLEGTERGNSQRSMRRELVSILCASTEFKSLFALKRCLKRVFFAEKVTNEDILRVTERLLSSKPSLVGYGDIETLGNYRSLDQALAKRDLKYLFKN