lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Forms the apical lamina, a component of the extracellular matrix; Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Secreted, extracellular space.
Sequence:
MTPSMDPSSPIRRRAWLLDPKLSIVLLLSFLKISQVHCTATFSLKLVSYANAANRELDGDCCDTIWVCHIDKCDPRFNVCFHRISGSNSMTACDHGRIETRLIKDNGQSFSFPAVLPSNIANPIRRQIPTWTGGIRVKVEVWDVDPNADDKIDFYAVNINLPAARNEAAATARRYTLSSRRGYSTTIIEAKVFCDPHFYGSNCRTYCQPTNSDSGHYSCNPQGQKICHPGYAGYNCINEIDECESGPCQHGGTCSDIMNGYTCECIEGISGSNCEVDIDECSSSPCLNGGSCEHYVGNYSCSCSAGFVGRNCEMNANECSSNPCNNGGTCHDELNGFSCACASGFEGTTCETNTDECVSNPCKLDHTCIDGVDGYACECSPGYEGIQCEVEINECNSGPCLNNGSCIDAVNGYTCLCVNGYNGSACEIDVNECESIPCQNNGTCSDSINGYECICTPGFTSVNCEGNIDECSSNPCTLDHTCVDEVNGYTCQCSPGFTGTHCELDVDECESTPCNNNATCTNGINMFQCQCQSGFEGALCDVNINECMSNPCQNDHTCVDGDNGYTCHCAAGYTGTHCEINIDECTSGPCLNNGSCEDLVNSFICHCASGYEGELCAENINECQSNPCLNNGTCEDVIAGFTCHCSDGFDGEFCQFDIDECQSQPCLNQGSCVDGVSSYRCICKDGFTGNTCDGNIDDCLESSCLNNGTCIDGINSFTCRCPPGFEGSLCEINVNECESRPCLNNGSCMDGVNSFQCDCEPGYGGDLCQTNVNECSSNPCQNGAYCIDGIDGFICSCPDGYFGLTCEVDHDECASAPCLHGGSCIDIVNGFYCRCTQGFGGMVCEVNLDECSSTPCTNDGTCEDMVAGFTCHCPEGFDGDFCEMNIDECVSLPCLNNATCVDGILSYSCDCPAGYTGSLCSEQVTLPPVPLCAQEFCQNGATCIQRDSQERCICAPGFTGPRCQDVLSGPCFPSPCLNGICVLGDANTTESRRCICSDNFLGDLCDVDPTRDIYSITLADHVKPSADLQAHISELLTSTLDIRDPESLQIVFQKAQYGESQLTSLAYTTIDFFVRADEAVLTESQLTSAIHSRSNQKIDAILKPYRLFIETPQAHITSNGNKQWMSKNWFIFCIIGLLILIALVLFAYIYRKRRKQSEAYLHAELEREVTRFINPAFGSPPTNGQLRLEGAVPVKEDVPSWEANFSNSTMGTFKGPAESDSEL
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLTDKFLRLQSALFRLLGLELLHEQDVGHRYPWRSICCILSVASFMPLTIAFGLQNVQNVEQLTDSLCSVLVDLLALCKIGLFLWLYKDFKFLIGQFYCVLQTETHTAVAEMIVTRESRRDQFISAMYAYCFITAGLSACLMSPLSMLISYQRTGELQPKFPFPSVYPWDNMKLSNYIISYFWNVCAALGVALPTVCVDTLFCSLSHNLCALFQIARHKMMHFEGRNTKETHENLKHVFQLYALCLNLGHFLNEYFRPLICQFVAASLHLCVLCYQLSANILQPALLFYAAFTAAVVGQVSIYCFCGSSIHSECQLFGQAIYESSWPHLLQENLQLVSSLKIAMMRSSLGCPIDGYFFEANRETLITVSKAFIKVSKKTPQVND
The following text describes a protein:
Function:
Regulatory protein involved in rpiB gene repression. Also involved in als operon repression.
Sequence:
MSQSEFDSALPNGIGLAPYLRMKQEGMTENESRIVEWLLKPGNLSCAPAIKDVAEALAVSEAMIVKVSKLLGFSGFRNLRSALEDYFSQSEQVLPSELAFDEAPQDVVNKVFNITLRTIMEGQSIVNVDEIHRAARFFYQARQRDLYGAGGSNAICADVQHKFLRIGVRCQAYPDAHIMMMSASLLQEGDVVLVVTHSGRTSDVKAAVELAKKNGAKIICITHSYHSPIAKLADYIICSPAPETPLLGRNASARILQLTLLDAFFVSVAQLNIEQANINMQKTGAIVDFFSPGALK
The following text describes a protein:
Function:
May play a role in the conversion of interphase chromatin into condensed chromosomes.
Subcellular Localization:
Nucleus.
Domain:
The SMC hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with smc4 forming a V-shaped heterodimer.
Sequence:
MYIEEIILDGFKSYPTKTVIGPFHPQFNAITGLNGSGKSNVLDAICFVMGINNLNLIRVNRLDELIYKQGQAGITKGSVTIKFNNEEKPSPLQEPYRDMKNITITRQIVLGGRNRYLLNSHNAKPKDISDFFQSLKLNINNPHFLIMQGKITKVINMKPIELLGLIEESSGTKLYEVKRTNAIKLMVKKDQKLGEINKVLFEEIEPTLVKLKKEKEEYNKFVSNNEEIEKYEKVEIAYKYYVAKKMMTKCEEKIEDAKSEEKILEKGIKEIDKDIEKYKIEKEKIVKETNTASEPMKILISQKEELEKKISQLKSEAKMENKEKAKEKRRREDIKKEINNLQNKLDDYQKNNEKNNKNLKSYEDLKKKIEILKEELNEKQLTMNCLLSAGTNNNEYTGSFREQLKNYKTNLSKAETQINNFLQNNKHLEKEIMTLKEQRKKYEKEYNEISKEKDIEEKKKKLCEQELDKLNKEYNNFMELDTLKTDKNILYNDMEKLQQELQVLKNIINSVKIDYKIPSNMKSTDVLGQIYKLIKIKKEYINTALAVHLILGGKLTYLLVQNKEHSKRLFEYNNFSSGSKRVTLLPLEDCVISREVHEKHIEECRRNVGLNIKDKNDVIYFLDIMEYDKNLERIIQYLFNGTLICSNVDLCKKITYNPNKKLSYTTITLEGDKFDTSGSMSGGSNKNINLFLLNYEKYKHKKEQYHDNENKLKEVSEKLKSLEKAEEKKKIISKELQIYENNLNNIENRMETSKYGSVNKKIEEHKNEIDKGRNELSELYKEQKKLTEVIRKLEKDISEYEANKDKKEEDLKETIKKLKNKIKQLETEEHKKKEEIDDVLLQIENYKKQKEKETNDLSSTDEIINEIEKKIEDIEKNINITKENLKELENKITELQSSFSSYENEMKHVVKKIEDLEKKKSENILDLKKLENTLLDLQKDLKTSSDTVKYLYKTHVWIESYEPLFNKKYTPYDFENFRHDVIQKKIQALQNEQNKLSININRKAVQMYEQVQVDYKDLVTKKSQVEEDKKKIQEVIADLDVKKSESLLAMYQQINEYFQAIFSTLLNNAQAKLSIVDGDLANGIEMKIAFNNNWKESLTELSGGQRSLLALSLILALLKVRTVPMYILDEIDAALDLNHTQNIGDMIRTQFPHSQFIIVSLKEGMFSHADVLFKMRFIDGISTVNRHALDIRQNTNKKEVQEVKRRRVTIHDKEPDHD
The following text describes a protein:
Function:
Proton-selective channel that specifically transports protons into cells. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDSSPDLSLKLRRGSSDSRDNFYMDFAQGIDSDIEEVDNTANNQEAGEVPPPPLPTVSLAEEVLLLVAPPPPPPSLLGQPLPTLTETDDIPPTPTPPPQQKDDEGDDEDEREEPVPEQDQGAPAAPSPPGSPINSVLELELIPPPPLSPMDDAGLRTDDDGEGEETDDAEEVAAIPPPHEMLDIESNPDEEEEEEEQEQASQEDTPKEEDEEEDDDKSTPPPPLPPLPSNFSYVQGHNLGQVTPPLTKSPSNSPSPPVTPPPCPELNISRMVSPPAQHISQIPPLTPSDESEGEAESQPNSPPLRLDAEQPPPDMDQPEPEDQPPEPENEPEPEPEPEPEPEPVSGAREDYSRSLDNEDESTTITTPPSNGYSASSIIAPPPEHFAELDEDRGFIPPPPLEQEPEEEVEEEEEEEEEELTKETDEISVDRESLQDQGGDSISSPRPASILTGSISTSVGGGAGGSPKPESRGPSRSGSQRSQLRSGSQQGSIAESRGGSRIGSRTGSVASAQAAGVLSPQASLKSQTSIRSQGQAGVRSPAGSIKSGSQRMQSPQAGEGAPAMPSPPLMRSPPPELARQMHSPPRITTPPRVCSPPLVSSPPKLAESAAAAVGVAATVKEQIGSSSSTAEPLEPSKPEPLKPPIATVSYQDEQKPSPPPTAAAAPAVTTTAATTAVTSQPRSHFTSSHHHYHLPHQFQHPHHQNHHTHSVRVPTPTVPSSYAPPPPPDSGSSSSPVDRRRLFMAGVAPPIAAGAGSLMAMPAEPAVAISPGRVSARSGSQHHVTIDESSLPSHKGNIQETPGPSGLIIGGGDGDGDRDIGGGGGPDSSDPPSSPGGSSSQPALSGSQADGQLALMYHSHQLTNYPVLPAIKRTHRPSFVYPPMPRVKAGDALATLFSALYGKLLVVMGIAFPMAEVISTYIPPSFYEVYYLYLYIGSMIFLLFMYATLIWGRPKLPVPIASPSKSATKASGTDSMDESDTDSNSVHHRLPPPIPVRRPSLLSPLGRRDAHYGSFYLRMGAVAFGIGSMIYSGLEFGQYFELNPDTKCHNVLLALTPATRMAFIFIQMYFIFLNNEQIKVYRYKIIARFGLMHMIGTNLAVWLNVLIQETKHEILTFYNPENRTLRISHRIPGHSRGHAIIQHDPTAHLRVPRGLKGPYQIFECRRTNIIGTLVQDASPFLFPCTIEYSLICAAILYVMWRSISRPQTPTPQRPDMISSPMKRSPHHYSVDCARAHKGLFVGILILVLTIISLIIFFVLISRPEFVAMAVTEVTICELLIYGTATIATLVGMIQIRHLQYDAYRSFSLDDILLVGAQTGSFLYNIFTVIAGHFTLRSDDMLVPINALASIVQTACQTMFILDASRRQAVSPEHLRKKPGREIVTFMLVVNLAMWAISTLEKSRAESHPIQLNFYGLWAWTIITHVSMPLAIFYRFHSTVCLCEIWKRAYKLKPTYMXEFARSRIQSIAQQQQFCEDLKTNLSYCYCSTTLAGGELETVEEVDSGESNSAEDAGAGAGSGGSRGSGGGAGAAEAGEAGEEGQQGGDSSCGLKAPIRALSPQSLNTEKAFCPVYVINGE
The following text describes a protein:
Function:
Regulates the copper-dependent mineralization of copper sulfide complexes on the cell surface in cells cultured in medium containing copper salts.
Miscellaneous:
MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
Sequence:
MSSQNLNDNPKNTSSAAEDKKKQTSSLKLAPIPTTSPWKSSSPDSNTVIPVEELRDISKTAKPSKNGSGSIKLTSNTKWTPITPSVIISGSKDTNSKSGKNSKNSKTNKKMKKRGKYNNDINKKDFNGQTNSTSEISNVSNLESKPLDANAKVNIHSSSGATANGNIKRITNNNNSTNGRQSRNYQNRNGKTRYNNNSRHSQAANNAISFPNNYQARPEYIPNASHWLNNNSRNSYKQLSYFRQQQYYNNINYQQQLQTPYYYSMEPIFKSIESIKNQIEFYFSEENLKTDEFLRSKFKKANDGFIPMSLIGKFYRMVNLSLGGDPNLILASMREVLQHKETNHLEIALGSIEGAQKNMADDFNPLENYFIRRENWAEYAMESNFDENDDETEKYNIEKLLGPNDLDNYSYMGYPNFFPSNENGKKSQSYDQGEISRQFEQNLQIND
The following text describes a protein:
Function:
Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Sequence:
MVLRQVMDFAQAVEHLLHPAVVSFNPHPRSFFSGRTQPLLTPLPEKAAQLTAIGIEQLVLLPFTEKLANLSPKQFVQSILVEQLQAKFISVGQDFCFGHQRRGNVQDLQNLGQEFGITVAIAQLEQTDTERISSSRIRRALKEGKLAMANHLLGRPYALRGTVVQGQQLGRKLGFPTANLCLPADKLWPKYGVYAGWVNLNALDVPIPAVINLGDRPTVNGQEPSAEVHLLQWSGDLYGQGLEVALTHYLRPETKFAGLDQLKNQIAQDCQQAEKLLNLDGAIP
The following text describes a protein:
Function:
May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MYAFYSLLIYIFYSLFRRDGGAAAAAEPGDPAQRARKPRGRRRPDLPAPELWTELTGLAASSEPEDGSEGAAEGRAAAVSLEEALLRLAEFLSVQLGAEESCGSPADLGQSGEVPPLLSVTSQLLALLAWLRSPRGRQALLQGTQPAPRVRPPSPDGSTSQEESPSHFTAVPGEPLGDETQGQQPLQLEEDQRAWQRLEQLILGQLEELKQQLEQQEEELGRLRLGVGATDSEKRVQHLTLENEALKQSLSLMRDLLLHWGPGPPIRAPQEEAEALLELQGRLQEAQDTTEALRAQLGVQEVQLQGLQGALQQLQQETEQNCRRELQQMHGQLAGLRARMASLRQGCGDLRGLVSTFTQSCQGSLSEARGQVSWALGALSSGGPDTQLPEGQQGPPAGCPGRLPELKGNIRVLCRLRPGTSSSLVSVEPGPGGTVTTCYRGRHRRFRLDWVFPPDASQEEVFRELEPAVLSCLRGYSVCIFTYGQTGTGKTYSMEGPPEDPGIVPRALQSLFREMGAGRQHRVTLSMVEIYNEAVRDLLAPGPPERLAVRQGPEGQGGIQVAGLTHWDVPNLETLHQMLKLGRSNRATAATAMNQRSSRSHALVTLTLRAASPPRAPGTAGTLHLVDLAGSERARKAGAAGPPRGDPDGARRLREAQTINRSLLALGGVMAALRAHRPHVPFRDSQLTRLLQPALGPGTTAVLLLQVGAGAAQVCACRSPPTRARPPAPLARRSPRGRRISGRQSAHSSSPTEWVKWSWGQPGAAGSRAPPGRPLPSVPTLRSPGPPAPLRRPLAVLHAPVPTTARARPSRPQRACPCSPGSRPCPWGLRPGLCWQRR
The following text describes a protein:
Function:
G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. HTR1B is coupled to G(i)/G(o) G alpha proteins and mediates inhibitory neurotransmission by inhibiting adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Ligands are bound in a hydrophobic pocket formed by the transmembrane helices; A residue in the 7th transmembrane region ('Thr-355' in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists.
Sequence:
VEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRAPDLPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLAMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMFNEDFKQAFHK
The following text describes a protein:
Function:
Component of an histone acetyltransferase complex; Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MAHGQEDCASVLEQFVHDVANLPLEINHLMEEIQAKDKIIQECRAIINSRDASIQKFIKLNGSLTPNPKEEQYSKIVLQNLDKSSQLQDEKIQLSEKACILLDRQIKKLDIKIRDLQNDGVLSNDPPIPSLFNNKDQYRDPPKIFFPDSSNDSASYTSPLAASSGNANPTPRLSLSLNRPHSAAALSQTARSSAPATPAATAHFQQRQRESSAGAIDSKRRRLNATLGSLPAASSNLRQSSLGPGTPKAGTPASSRAGSAGPRSAGVTKKALTKKVAPHQQLKKLKSLNGKHTKRSSSTSRVKSHKKSPSGGDDDDDESMLSSAELSESENGDMHIDEEEEDEGNEDTKVYCTCRTVSHGDMVACDNDDCKFEWFHWKCVGLTREPVGKWYCPDCLAAKGGE
The following text describes a protein:
Function:
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex seems to bind preferentially to single-stranded DNA.
Subcellular Localization:
Nucleus.
Sequence:
MENGLGNHSNKLIHDSKRTLYLDYLPPYQTDAVADVVREIRAVDREASAVLSHLTENGTVTFQPEEHPSEAASLLMLHATNLHNKRCLMAYHNLRLGRIRQYCWDGGKKMEASLKTALSPTEREYLSRYSELLAAYKGPWTDVDLTGSTVPPKDLFIDVRVLEDVGEIETEYGTINLTKNSQLHVRTTDVERLIRQGYLVKL
The following text describes a protein:
Function:
Methyltransferase which catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). Does not seem to possess caffeate O-methyltransferase activity. Implicated in melatonin-dependent circadian dynamics of stomatal aperture to minimize night water loss and promote drought tolerance. Prevents seed germination by promoting melatonin biosynthesis. Promotes melatonin-triggered defense responses to the necrotrophic fungus Botrytis cinerea; (Microbial infection) Promotes melatonin-triggered defense responses to the necrotrophic fungus Botrytis cinerea.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSDQLSKFLDRNKMEDNKRKVLDEEAKASLDIWKYVFGFADIAAAKCAIDLKIPEAIENHPSSQPVTLAELSSAVSASPSHLRRIMRFLVHQGIFKEIPTKDGLATGYVNTPLSRRLMITRRDGKSLAPFVLFETTPEMLAPWLRLSSVVSSPVNGSTPPPFDAVHGKDVWSFAQDNPFLSDMINEAMACDARRVVPRVAGACHGLFDGVTTMVDVGGGTGETMGMLVKEFPWIKGFNFDLPHVIEVAEVLDGVENVEGDMFDSIPACDAIFIKWVLHDWGDKDCIKILKNCKEAVPPNIGKVLIVESVIGENKKTMIVDERDEKLEHVRLMLDMVMMAHTSTGKERTLKEWDFVLKEAGFARYEVRDIDDVQSLIIAYRS
The following text describes a protein:
Function:
Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MISPIRSFALVHALFTAIAQAVHPVEVRGQDFVDTVTNKRLMIVGVDYQPGGQAGYKPSEGKDVLSDADVCLRDAVLIQKLGVQVNTIRVYNIDPELDHSQCASIFNAAGIYMMLDVNSPLQGESINRAEPWTSYNTDYLTRVFGIVENFKNFPNTLGFFAANEVMNDLNTAKYNPQYIRAVQRDLKNYIKKHASRKIPVGYSAADVREILQDTWAYMQCDHNDDASSSDFFGLNSYSWCGGDATLQSSGYQDLANMFNQSAIPVFYSEYGCNKVQPRVFTEVPALYGTEMTALSGGLVYEYSQEEQDYGLVQVNSNGSVTLRTDYDNLQGQYNKLDTGLLESTNPSSTSIKAPACASGLISAEQFSKNFTIPAVCPNCQSLIDNGISNPKNGKLVDVSATKPKQQIYGSNGALIQGLSLNKISNDGVNAPGQQSTTPSSASGSGGPAQPTESKKGAAPKQAAGALACIAVLVSALLI
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Sequence:
MTKAYDFNWQRTIPDALLKGCIFDRWEEEKEQVVYEPGALFRVDEYGFFIYWNSEGRDGQVLELSQVNDIRAGGIPKDVRLLAELSSKNRYGLDEVSLTICSGTDMVNINYTHVVCPDPDTAKVWQAGLRSITNNIKANNVCPATCLEKHWIKLGFLVEPEGKLPVRRIAQTFASGKTEKLVYQCIADVGLPGGKNDVIEPKEFTLEKFQELYQRVCPRNDIEELFNTITEGKTDYITLKQFISFLNEKQRDPRLNEILHPFYDERRVREIVGAYETSPELVKEGRLSQGGLVRYLMSDENAPVFLDRLDMYMDMDQPLSHYYINSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDEEPIITHGKAMCTDILFKDVIYAIRDCAFVTSDYPVILSFENHCCKKQQYKLAKYCSEIFGDLLLTEPLPSYPLEPCVSLPTPNELKRKILIKNKRLKPEDEKRELELWKKGQLQNDDDEEEKEDASVTILAPTEEGEGEKKVSSPRDGRGWSTRYSTLTRSADGAVQVEAQLEEQLAMAHYQYTGATVHVHPFLSSLVNYAQPVKFQGFDVAEERSVHFNMSSFAETSALGYLKSQAIEFVNYNKRQLSRIYPKGTRADSSNFLPQIFWNAGCQMVALNFQTPDLPMQLNQGKFEYNGGCGYLLKPDFMRRADKTFDPFAESPVDGVIAAQCSVRVLSGQFLSDKKVGTYVEVDMYGLPTDTIRKEFRTRMVPANGLNPVYNEEPFVFRKVPPSSSSSDSQLLRKQTQICEQAFTLSVISGYRHVSLRTEGNFPMSLAMLFICIELKIYVPDGLGDLMDALSDPRAFLSAQEKRMVQMRAMGIEEADILVNRPDLGSQQKKDDDKREEWRMEAITVDALRTEKDYVKLRRKQIKELEGLRKRHHKDKQQVQKQQCLAVEKLVPKDSPGPVSESEDGGVRALVVQQMHQWSSLLGTHRAQEWDLLRLHLTNQGQLLRSLMLKAQAQQMKQLDAKFERENKEMKMKQAKVSVETAREVSSDKTLRNKAERERRLREKNSNNTKKFIEERKSAALKQSKERERLKKIHEKQLHDLQREIDNGLELYNAAETEYKLCAKLECFV
The following text describes a protein:
Function:
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Sequence:
NLTKKYNIMNKAILHTIIIYTLASCPYCIKAKALLDKKNVAYEEIEVSNFAQEEKEKFIKKSGGKKTVPQIFIDNMHVGGCDALFDLEKEGRLDKLLE
The following text describes a protein:
Function:
Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
Subcellular Localization:
Secreted, extracellular space.
Sequence:
MAGTSNYPPQTPAPMPVPNPVAIINPQFCAPYPVDLNVVRKLMTWSEGAFGVTDVNGNIVFKVKGKFFSLRDRRILLDAAGNSLVTFQQKMLSAHRRWQVYRGESTDSKDFLFSVKKSSLLQFKTKLDVFLAHNTSEDVCDFRIEGSWLERSCVIYAGNSSSIIAQMHRKHTAQSILLGKDNFGVTVYPNVDYAFIVALVVILEEINEDRSVILVSLCERNVDYAIVVALLVILEGFIRLTVSLDSMDVKVCLFLVLLGAVYCTARELAAPDLLIIETEDVSALWTSNLQAQKQLQPLKDVSNIKGLCTLCEEYTATALDYLSNKQTQAKILEVLLMTCSKMPIYKEECTAMVDQYAHLFFSEISTIKPDDICQKVDLCRKVVSISQKFSPNGCDLCHQVVEETVSKLKDPDTQLDILAILLKACGSAEKYSNKCKKMVFEYAPVILINAEHFLEKNDVCTIMHACQPAVDKEDALPEMQTSLHSAS
The following text describes a protein:
Function:
May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSSLTLNSVVDEFNRLAPLSLAESWDNVGLLVEPTSSKIIKKILLTNDLTNSVMQEAESSSVDLIYSYHPPIFAPLKRITASNWKENIIARCLENKIAVYSPHTALDALKGGVNDWLAEAFEGKKLVRSILELVASVPEARLEEHISTADGYEQMTIMAPEKALPSIIELVNQCSFANASRYVRIIRVEKPPIPGSGMGRLIRLSEPITINRVVELVKTHLKLQHVRLATAGNAENNMNVETIALCAGSGASLLKNVKADVFLTGEMSHHEVLDAVHRGTSVILCEHSNTERGFLSKWKEVLHSALGEDVQIDVSLNDHDPLQVV
The following text describes a protein:
Function:
Functions as a transcriptional activator playing a crucial role during development. Functions in gastrulation, regulating mesoderm differentiation. Activates wnt8, t/bra, chrd and mix-A/mix.1 expression.
Subcellular Localization:
Nucleus.
Sequence:
MVPGAWHSLLFTTSSASEKEENRSQRMQLGEQLLNSSTPNLPHTFYPLTGDPSSAVHSPSLEFSVGHKGQQHKKYSSGSSRGLQLDSPREAGSSSTMLSETGEGFSVAKTLPDNVRKGSPSAEEELNTAVPTSAPRYLDGSLQAASERYYLQPQGQQLQQTTTELGSPCSIFPYAPPQHSAVYPAGGAARYPPYGSMLPPAGFSPPVCPSRPQYSSGYQYSQAPGTMYSPYPPAGTGSGLSALGLPGGGAGVRAQVFLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNITGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKVYVHPESPNTGAHWMRQEISFGKLKLTNNKGANNNSTQMIVLQSLHKYQPRLHIVEVSEDGVEDLNDSAKNQTFTFPENQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSMYTASESDRLTPSPADSPRSHQIVPGTRYSVQPFFQDQFVNNLPPARYYSGERTVPQANGLLSPQTNEEVANVPPQRWFVTPVQQAAANKLDMGAYETDYSSGSLLTYGIKSLPIQTSHPMAYYPDAAFASMAGWGSRGSTYQRKMTTSLPWSSRSSPSGFSEDLLPKDKVKEEMSSSWVETPPSIKSLDSNDSGVYTGACKRRRLSPSTSSNENSPPIKCEDIGTEDYKDATKGLGYYSFYSSS
The following text describes a protein:
Function:
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
Subcellular Localization:
Cytoplasm.
Sequence:
MNTQVSTIITIDHPAGLHARPAARFVTLAARFPCSITVRKLNGSKPPVNAKSALGVLTLAVNQGDTVEIVAQGDQAQEAISALIALIRHNFEESTTSHS
The following text describes a protein:
Function:
Putative phospholipase.
Subcellular Localization:
Secreted.
Sequence:
MPDVSVNGWSYLSLKTNSLNGKYDDYVQALAAGYLEGYLTQEMIWDSKYNYYTNYFNSSTIPKVLNDWLTENYYNMHEFIVNNVDSWYWRQLNLTLTQMNGLLDGYTYALSLTNNRSKIHQQTIVLFDLFVLNMYGDLGDLGPALHMGNFPAAKRASDFNDIQDYFMKTQHCSALIKLTSDYSELYAAHTTWTGYNTMLRIFKSYNYGYSFEYSGTISRRNMFSSYPGVLISIDDFYQMADTNLVVLETTNSLLNPELYKLIRPYSGVLSWIRITITNRLSNDGKSWCETFSRYNSGTYNNQYMVIDYKKFTPYKELKDGALYVLEQIPEYIEYDDQTVLLREMYFSSFNIPFYETIYNMSGYNNFTSNNYTNSKIYYLSYQTCPRSEIFRRDVGSIESLDSFKALLRYNKFQTDPLSHGTPFYAICSRYDLLSDDPKPFGCTDTKVTSYNNLLENSVLAISGPTTDNQKPFVWSSNSNFMNVAHNGIPNEFNFDWVVFKNNSFNNY
The following text describes a protein:
Function:
Has hexosaminidase activity. Responsible for the cleavage of the monosaccharides N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) from cellular substrates. Has a preference for galactosaminide over glucosaminide substrates (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Extracellular vesicle.
Sequence:
MSSPTPFKMRLVHLDLKGAPPKVSYLSEVFPLFHALGANGLLIEYEDMFPYEGHLRLLRAKHAYSPSEVTEILRLARLSELEVIPLVQTFGHMEFVLKHAAFAHLREVALFPNTLNPHEAESLALVQAMIDQILELHRDVRWLHIGCDEVYYLGEGETSKQWLQQEQNSHAKLCLSHMQAVASHVLTQHPGVTPLVWDDMLRDIPQEQLKASGVPQLVEPVLWDYGADLDVHGKVFLIGKYQECGFQRLWAASAFKGATGASQALPPVEHHIRNHELWLQVAGSGPKDALQGIILTGWQRYDHFSVLCELLPVGIPSLAACLQSLVHGGFAEDVRLRAERFLGVSSLEIADTVSEGAGSFPGSDIHALVTQISLHLRSSVDTLLERNRYVTGWFSPYHRRRKLVHPVMIQHIQPEALSLLSRWNNLVQQLEVALQPVFYPDTIEEWLEENVLPSLQRLQDLLQDLGEAAARQPPPTSPGWDTGQNP
The following text describes a protein:
Function:
The homodimer inhibits HMG-CoA reductase (HMGCR) (32% of inhibition produced by 0.6 uM), a glycoprotein involved in the control of cholesterol biosynthesis. The inhibitory effects of bumarsin are seen at much lower concentrations (0.6 uM) than that for statins such as atorvastatin (5 mM) and simvastatin (10 uM). In addition to inhibition of HMG-CoA reductase, this protein lowers cholesterol levels by inducing steroid hormone synthesis via StAR, and by increasing reverse cholesterol transport mediated by the induction of ABCA1 and APOA1 (By similarity); The heterodimer non-edited LVP1 induces lipolysis in rat adipocytes. Induction of lipolysis by LVP1 appears to be mediated through the beta-2 adrenergic receptor pathway (ADRB2). Intracerebroventricular injection is not toxic to mice; The monomer edited version, similar to alpha-toxins, may modulate voltage-gated sodium channels (Nav) and may block voltage-gated potassium channels (Kv).
Subcellular Localization:
Secreted.
Domain:
Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Sequence:
MISVQVIFIAFISIIAFSMVCGGNVFPNRELGILYGCKGYGNAFCDKVCKMHLARGGGRCGEPNPVMWACECIDIDEDNGYFLNALEKQCPLLKG
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase 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. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLSQSLTWQYANQLPLQDEEFHLDQMQHYLDSDFAYWNPKLTTPPMLYFLNYPFIVLLSKMGLSTLMACRIINTFIYPSITFLVLSKSFQNTEKALLFSILPTIYFYNFLFYTDTLSITLLSLSFQLLQSKYYFISSIFSLCSVMSRQTNILWIVYFCIKDYLDQNQAKLQFKDPRLSILFHVNALLNMILSDIKGIVRKYKYHIFILILFIGFLYTNGGVVLGDKDNHKFVFHAAQIMYFLPVLFIYFPINWNTLFQYTQLSIKRLLLSRNAKFTYLIILIICLEIVHNWTYIHPFILSDNRHYVFYIWRKILSKDVYRYCLCFFYALIIVILSRILISNQTFQLILLFIFTTLSLIFSPLIEPRYFSIPLLFFYYHCQFAEQTLKKQITVFTLMNCIIVYVFCEVKFSCDFPQCRFMF
The following text describes a protein:
Function:
The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force.
Subcellular Localization:
Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Localizes at both cell poles and along the length of the cell.
Domain:
All four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex.
Sequence:
MGIFSRFADIVNANINALLEKAEDPQKLVRLMIQEMEDTLVEVRSTSARALAEKKQLTRRIEQASAREVEWQEKAELALLKEREDLARAALIEKQKLTDLIKSLEHEVTLVDDTLARMKKEIGELENKLSETRARQQALMLRHQAANSSRDVRRQLDSGKLDEAMARFESFERRIDQMEAEAESHSFGKQKSLDDQFAELKADDAISEQLAQLKAKMKQDNQ