lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MGHGFGELAKVRGIVTHKISPFEQRAFANVISKGVPNTLRRIRSQVFIVAPPFVMGYMVYNYIENLHTQMNRKNPAEFENDS
The following text describes a protein:
Function:
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane.
Sequence:
MRLVREFECCAGWAWCACSDSCALEVKVEAPVGNVVGYVKQSKYCSGPKFDVLDAERRPVAKIKGPYCMQLNSFCQGEIDFDVFTVDMATTIGKVFKQRPGCFLKECCTKVDNVGVTFPADLDVNVKATLLAAVFFIDFMFFEKANNNNNNKISDIPVFLGFN
The following text describes a protein:
Function:
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein; Periplasmic side.
Sequence:
MKISPSPRKLSKVSTSVSFLISFALYAIGFGYFLLREDAPEPLAQAGTTKVTMSLASINTNSNTKTNAESAKPKEEPKEKPKKEEPKKEEPKKEVTKPKPKPKPKPKPKPKPKPEPKPEPKPEPKPEPKVEEVKKEEPKEEPKKEEAKEEAKEKSAPKQVTTKDIVKEKDKQEESNKTSEGATSEAQAYNPGVSNEFLMKIQTAISSKNRYPKMAQIRGIEGEVLVSFTINADGSVTDIKVVKSNTTDILNHAALEAIKSAAHLFPKPEETVHLKIPIAYSLKED
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. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Subcellular Localization:
Cytoplasm.
Sequence:
MSIVLHGVAAGKGIAVGCAHLIARGTEEVPQYDVAEADTDAEAERFDAAVKATRKELEQLRSAIPENAPTELGAFISLHLMLLTDVTLSREPVDILREQKINAEWALKQQSDKLAAQFDNMDDAYLRERKQDMLQVVRRIHNNLIGQGNELEVADNLFDETVLIANDLSPADTVLFKEQRIAAFVTDAGGPTGHTAILGRSLDIPSVVGLHNARKLITEGETVIVDGINGVLIIAPDESVLNEYRRRAREYRSHKRDLNKLKKTAAATADGVCIELVGNIESAEDVKPLHNLGADGIGLFRSEFLYLNRDTMPSEDEQYEVYSAIVKKMKGKSVTIRTVDLGVDKNPRWFGKNSTPNGSLNPALGMTGIRLCLAEPVMFRTQMRAILRAAVHGPVRMMWPMITSVSEVRQCLIHLDTAQRQLAERGDAFGKVGIGCMIEIPSAALTVGSILKLVDFISVGTNDLIQYILSVDRGDDSVSHLYQPGHPAVLKMLQHVIRTANRMDKDVSVCGEMAGDTAFTRVLLGMGLRRFSMNPNNILPVKNIILHSNVGQLESDIVKVIRCEDEEKSEKLIKQMNSVSVEEEADFKGRK
The following text describes a protein:
Function:
Possesses arsenate reductase activity in vitro. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. May play a role in arsenic retention in roots; Possesses phosphatase activity towards p-nitrophenyl phosphate in vitro.
Sequence:
MCKPRQTKRGQESPPSPARPRPRSPRRPETMARKGVSYVTAAQLVSMVRDPRVAIIDVRDEERICDAHIAGSHHYASDGFADRLPEIAEATRAKETLVFHCALSQVRGPSCARMFLDYLSEAKEESAVKSITVLELGFNGWELSGRAVCRCKDAPCKGVCS
The following text describes a protein:
Function:
A probably major component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC; expression of this protein alone can also form BMCs (which may be less tightly closed than eutSMNLK shells). The 'bent' shape of this subunit is required for integration of cargo proteins into these BMCs. Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. Targets at least 2 proteins (EutC and EutE) to the interior of the BMC. Proteins such as EutS containing circularly permuted BMC domains may play a key role in conferring heterogeneity and flexibility in this BMC (Probable); The ethanolamine (EA) catabolic bacterial microcompartment (BMC) probably concentrates low levels of ethanolamine catabolic enzymes, concentrates volatile reaction intermediates, keeps the level of toxic acetaldehyde low, generates enough acetyl-CoA to support cell growth, and maintains a pool of free coenzyme A (CoA) and NAD; Expression of the eut operon allows this bacteria to use ethanolamine as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon. EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection.
Miscellaneous:
MISCELLANEOUS: The need for a bacterial microcompartment in EA metabolism can be bypassed by increasing the levels of EAL and an acetaldehyde dehydrogenase (not necessarily EutE).
Subcellular Localization:
Bacterial microcompartment.
Domain:
Adding an N- or C-terminal His-tag to this protein prevents it forming BMCs. One side of the hexamer is concave and lined by hydrophobic residues, the other side has a slightly protruding, 6-stranded beta-barrel (By similarity).
Sequence:
MNKERIIQEFVPGKQVTLAHLIAHPGEELAKKIGVPDAGAIGIMTLTPGETAMIAGDLAMKAADVHIGFLDRFSGALVIYGTVGAVEEALLQTVSGLGRLLNFTLCELTKS
The following text describes a protein:
Function:
May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.
Subcellular Localization:
Cell junction, hemidesmosome. Membrane; Single-pass type II membrane protein. Secreted, extracellular space, extracellular matrix, basement membrane.
Sequence:
MDVTMKNRDGTEVTERIVTETVTTRLTSLPPKGGTSNGYAKIGSFGGGSRLEKQSLTHGSSGYINSTGSTRGHPSTSSYRRAHSPASTLPNSPGSTFERKTHVTRHAYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKIVTASSQSVSGTYDATILDANLPSHVWSSTLPAGSSMGTYHNNMTTQSSSLLNTNAYSAGSVFGVPNNMASCSSTLHPGLSTSSSVFGMQNNLAPSSTTLSHGTTTTSTAYGVKKNMPQSPVAVNTGVSTSAACTTSVQSDDLLHKDCKFLILEKDNTPTKKEMELLIMTKDSGKVFTASPASIAATSFSEDTLKKEKQAAYNADSGLKAEANGDLKTVSTKGKTTTAGIHSYSSGGVGGTGGGGNVGGAGSGPWGAAPAWCPCGSCCSWWKWLLGLLLTWLLLLGLLFGLIALAEEVRKLKARVDELERFRSSMLSDEKLERSSKARLQGMAPTVGADLDKIGLNSNDQEVLWMFVRNKLMTEQENGNLRGSPGPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPEGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEPGPPGSGEKGERGAAGEPGPHGPPGVPGSVGPKGSSGSPGPQGPPGPVGLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGMPGIRGPPGPSGDPGKPGLIGPQGPQGLPGTPGRPGIKGEPGAPGKIMTSDGSSMLTVPGPPGPPGAMGPPGPPGAPGPAGPAGLPGPQETFLSGPPGPPGPPGPKGDQGPPGPRGHQGEQGLPGFSTSGSSSFGLNLQGPPGPPGPQGPKGDKGDPGVPGALGIPSGPSEGGSSSSTMYVSGPPGPPGPPGPPGSISSSGREIQQYISEYMQSDSIRSYLSGVQGPPGPPGPPGPVTTITGETFNYSELANHVVSYLRTSGYNVGLFSSSISSEDILAVLQRDDVRQYLRQYLMGPQGPPGPPGASGDGSLLSLDYAELSSRILSYMSSSGISIGLPGPPGPPGLPGTSYEELLSLLRGSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHTAGLSFIPGPPGPPGPPGPRGPPGVSGALATYAAENSDSFRSELISYLTSPDVRSFIVGPPGPPGPQGPPGDSRLLSTDAFHSRGSSSSSHSSSVRRGSSYSSSTGTGAGTGSLGTGGAFGAATGDGGPYGTDTGPGRGYGAAAEGGMYGGNGGLFGADFAGGLDYNELAVRVSESMQRQGLLQGMAYTVQGPPGQPGPQGPPGISKVFSAYSNVTADLMDFFRTYGAIQGPPGQKGEMGTPGPKGDRGPAGPPGHRGPPGPRGHKGEKGDKVKNELNSAQRSQIRKWHSMPPSSWTRAK
The following text describes a protein:
Function:
Component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi-independent import into the vacuole (By similarity). Positive regulator of defense responses to pathogenic bacteria (e.g. P.syringae pv. maculicola), to the biotrophic oomycete H.arabidopsidis and to fungi (e.g. B.graminis hordei), especially in cell wall apposition formation related to plant defense. Required for both immediate and later responses triggered by pathogen-associated molecular patterns (PAMPs). Positive regulator of abscisic acid (ABA)-independent mannitol (drought)-promoted stomatal closure.
Subcellular Localization:
Cytoplasmic vesicle, phagosome. Cytoplasm. Nucleus. Note=In the cytoplasm, localized in a peri-nuclear pattern.
Sequence:
MAEAGDENLYAAARDIARALGKDPSAAGDILQILSGYGASGNRGGDPRPTPSRGGSNVNFDRALTSLERQISSYIVEDRPIWSDPVDSRTFLDSVDELLAIAGDLRSMAGDKSVAVCQSRADELIQQVMFRLQEEFGFVMDRAPDSFDSDDEFPGEEDNDTSDGVIVARPITDYKIVIEALQSSVIGDLNAIAVRMVAGGFAKECSRVYSSRRREFLEESLSRLHLRGLSMEEVQESPWQDLEDEIDRWIKAVTLIFHVFFPSERLLCDRVFSDLPVSSVTDLSFMEVCRGTTTQLLNFADAIALGSRLPERLFKVVDLYEAMQDLIPKMETLFSDRYCSPLRHEALAIHKRLGEAIRGIFMELENLIRRDPPKTAFPGGGIHPITRYVMNYLRAACKSRQSLEQILDQTGNETGSDTRPLSVQIIWVLELLESNLEGKKRTYRDPSLCFLFMMNNDKYILDKAKDNELGLVLGEDWIVKHAAKLRQYHSNYRRSSWNQVVGLLRTDGPYPKLVENLRLFKSQFDEVCKVQSQWVVSDGQLREELRSSVAGIVSPAYSNFIRRLKESPEINGRRGEPFIPYTVEDVEFIIKRLFKESSS
The following text describes a protein:
Function:
Promotes the degradation of p53/TP53 protein and inhibits its transactivity.
Subcellular Localization:
Nucleus. Note=Colocalizes with p53/TP53.
Sequence:
MNSRRRPVKKDSEALEISIPFDETPHLDPQIFYSLSPSRGNFEEPSEAASPTAALMNGVRAQLHLALERNSWLQKRIEDLEEERDFLRCQLDKFISSARLDADDHCRGKPGPRRAEGDGRGGTGGEASDPESAASSLSGASEEGSTVERKRQKQKGGPGRRRFGKPKARERQRVKDADGVLCRYKKILGTFQKLKSMSRAFEHHRVDRNTVALTTPIAELLIVAPEKLAEVGEFDPSKERLLEYSRRCFLALDEETLKKVQALKKSKLLLPITYRFKR
The following text describes a protein:
Function:
Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MPVIKLKHVVSCSSADTTHTAENLLKADTYRKWKAARPGEKQISVILQFEKEEQIHSIDIGNEGSAFVEVLVGRSTSISEQEYEVLLGMSSFMSPSESKNESNLNRTRMFGPDKLVKGAAEKKWDRVKIMCTQPYTKNLAYGISFIRLNSPPEDGSPTAPSPKVTKLGQFMVKEEENSSPSMRPGSLFFNRTSKPQVTPPKTPPATQSYAAAALQGTAETSSSTEKQIKTPPSNNITKEPSSSKRKFEFNKEPSSHSAVKKPDVKESPSSTKAKTSSQPAPKKPKVETPPTKKPSPSEKPNQKKSPPSSQPMDLGRILQGTVFVLSGFQNPFRSDLRDKALEMGAKYRPDWTPDSTHLICAFANTPKFSQVKAAGGIIVRKEWVLDCYKKRQRLPQKQYLLGTAESSSDEEDDSEEDEPPKAPQHKPHPDPSRTNHKKPSPSPAKVKEKRAPIKSEDEDTEDENTRIVPSKANHKPKQEDEYDASTDEEATGERQQHEDDSGEDTEDELRRFQEEKQGKKAAVKVERVDPYAGSTDENTDEEEKPELDLPIPALPDLFLGKKFFLYGEFPAAERRVLSRYIIAFNGELEEYMNEKVQYVITAQEWDDSFEDALNENTNVSFVRPRWIYNCNERQKCIPHQPYVVVPKV
The following text describes a protein:
Function:
Mediates H(+)-dependent pyridoxine transport.
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein.
Sequence:
MSERMRHGRNEEQDQTGLLSQAIDDHSEESHAHSNNGALLTSMEHSTNGVIAHRDEGDLNSVLLSSTRSRKEYVVYTERWFILAVFSLLALVQSCGWNTWGPIENTASVVLGWKHSTFALLANWGAIVFSLTVFFFTWLLHTKGLRVSVLIAAGALVCGMGIRCLPVPVHSMIWTANIGQVIIGLSAPVLMAGVTTISAVWFPTNERTTATAISSTMAYLGVAASFLIGPQVVSDILPVHANSSTISPFDLTAEDDNLEVNPADYDPVEIQHCLRQIKLLLFIEFIWTLLLFVVALIYFPSAPISPPTASAIAKREDLKAGLLEIVKKKQFWIPALIFGMTTGCFNSWNTQLVAIFDNKVSQTVSSWIGFYSNLAGVFGGIIFGTFVDRLGGKMKAILMLLMCGACGGFVWVLLLANGLIPFSTVYLYASVILFGFFVNSMVPIIFEVTAEGAFPTGEETSCMFMAWLANVTGLVFLLLPIFISNSSLTWLNWVMLGALGISAVLLFFYKEHYVRKEFDVTHHDDVDVEEECEHDPPIST
The following text describes a protein:
Function:
Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular Localization:
Host cell outer membrane; Lipid-anchor; Periplasmic side.
Sequence:
MMQKKKLQPPLLVTIAALVLCLPLLLTGCGNSKNAPVPSVVILPEIDTELTEATPVPPMPQPLTWGASLLWNADLLMALGQCNRDKASVREQEIRRKEIYERRPEPGGGAAAR
The following text describes a protein:
Function:
Catalyzes the conversion of L-aspartate-beta-semialdehyde (L-Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch-point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.
Sequence:
MVAKEIYVAVIGAGGVGKCFLSQLEALSQRYTSSKISLIFVSRSKKVLYSPKYTPLSYSNLSTTLADSTQEPLSIPKIIEYLAAAPAKVVLVDNTSSQDVADAYPQVLSKGISIVTPNKKAFSGSFKLWQDVFSAASSSGAKVYHESSVGAGLPVISTLKELVDTGDSVTKIEGVFSGTMSFLFNSFAPTEGSGGKWSAEVAKAKELGYTEPDPRDDLNGLDVARKLTILARLAGLEVESPTSFPVQSLIPKELESVSSGEEFLQKLPEFDSQMEETKIAAEKEGKVVRFVGSIDVAKKEVKVGLEKFDRSHPIAALKGSDNIISFYTKRYGSNPLIIQGAGAGGDVTAMGVTGDLIKVLERLS
The following text describes a protein:
Function:
7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7-oxosteroids. To a lesser extent, can also act on taurochenodeoxycholate, taurocholate and glycocholate. Can also use glycochenodeoxycholate as substrate. Is not able to use NADP(+) instead of NAD(+) as the electron acceptor.
Sequence:
MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN
The following text describes a protein:
Function:
May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.
Miscellaneous:
MISCELLANEOUS: This protein has four functional calcium-binding sites; potential sites II and VI have lost affinity for calcium.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MARGGRLGLALGLLLALVLALRAKPTVRKERVVRPDSELGERPPEDNQSFQYDHEAFLGKEDSKTFDQLSPDESKERLGKIVDRIDSDGDGLVTTEELKLWIKRVQKRYIYDNVAKVWKDYDRDKDEKISWEEYKQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKASDLDGDLTATREEFTAFLHPEEFEHMKEIVVLETLEDIDKNGDGFVDQDEYIADMFSHEDNGPEPDWVLSEREQFNDFRDLNKDGKLDKDEIRHWILPQDYDHAQAEARHLVYESDKNKDEMLTKEEILDNWNMFVGSQATNYGEDLTKNHDEL
The following text describes a protein:
Function:
Catalyzes the NAD-dependent oxidation and decarboxylation of (2R,3S)-homoisocitrate, (2R,3S)-homo(2)-isocitrate and (2R,3S)-homo(3)-isocitrate, into 2-oxoadipate, 2-oxopimelate (2-oxoheptanedioate), and 2-oxosuberate, respectively. All these substrates are intermediates in the biosynthesis of biotin and of 7-mercaptoheptanoate, a moiety of coenzyme B in methanoarchaea. Is also able to produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate in vitro, but this substrate is probably not physiologically relevant. Is unable to use any isomer of isocitrate or isopropylmalate as a substrate, and NADP as an oxidant.
Sequence:
MMKVCVIEGDGIGKEVIPEAIKILNELGEFEIIKGEAGLECLKKYGNALPEDTIEKAKEADIILFGAITSPKPGEVKNYKSPIITLRKMFHLYANVRPINNFGIGQLIGKIADYEFLNAKNIDIVIIRENTEDLYVGRERLENDTAIAERVITRKGSERIIRFAFEYAIKNNRKKVSCIHKANVLRITDGLFLEVFNEIKKHYNIEADDYLVDSTAMNLIKHPEKFDVIVTTNMFGDILSDEASALIGGLGLAPSANIGDDKALFEPVHGSAPDIAGKGIANPMASILSIAMLFDYIGEKEKGDLIREAVKYCLINKKVTPDLGGDLKTKDVGDEILNYIRKKLKGY
The following text describes a protein:
Function:
Acts on leucine, isoleucine and valine.
Sequence:
MSRPVPAVFGSVFHSQMPVLAYREGKWQPTEWQSSQDLSLAPGAHALHYGSECFEGLKAFRQADGKIVLFRPTANIARMRQSADILHLPRPETEAYLDALIKLVKRAADEIPDAPAALYLRPTLIGTDPVIGKAGSPSETALLYILASPVGDYFKVGSPVKILVETEHIRCAPHMGRVKCGGNYASAMHWVLKAKAEYGANQVLFCPNGDVQETGASNFILINGDEIITKPLTDEFLHGVTRDSVLTVAKDLGYTVSERNFTVDELKAAVENGAEAILTGTAAVISPVTSFVIGGKEIEVKSQERGYAIRKAITDIQYGLAEDKYGWLVEVC
The following text describes a protein:
Function:
Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. Prevents actin filament assembly by forming a 1:1 complex with actin monomers, and inhibits the nucleotide exchange reaction of actin monomers (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSASVELKPTEKFSKFLEEYSSVPVRAAIISISNENSFDVKTMVEKSESIESDFKKVRECLLGSEEPAFVLVYDDSKKNLLQLISYVPENANVRRKMLYASSRAAFVRCVTLAKLDESYFASTPEELDYQQIMKSLSKQEDQSPLRQDELERKEYNESMQSSVTHKRPLVTRGVAMSIDDKALKALSDLKSSTENNLVILSIDKEVISLSQEKQNIPPSDVKSFFSSTEPNFAFYSLPKDGSSKILFIYICPMQATVKHRMVYSSSKLGLLDSIKAELGIVIDGKIESNDAADITEKEILHAAGISSPQAETSTTKTGFSRPRPPRRR
The following text describes a protein:
Function:
Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome.
Subcellular Localization:
Cytoplasm, perinuclear region. Note=Localized to the perinuclear region, the growing tips and septum.
Sequence:
MSSKPPSNTPKFSYARALASSQSNKSNSTKASENNTATAEKQAVKPSGVEPTNTSRANAQKKTESTGKITSEADTEKYNSSKSPVNKEGSVEKKSSEKSSTNNKPWRGDNTSKPSANSSAERTSSQHQKPETSSQIGKDNAAPVENVNEKSTSQETAPPVSTVPIQFGSITRNAAIPSKPKVSGNMQNKSGVSSYSSKSQSVNSSVTSNPPHTEEPVAAKPEASSTATKGPRPTTSASNTNTSPANGAPTNKPSTDINTTDPATQTTQVSASNSPALSGSSTPSNTSSRSNRQNHGNFSEKRHYDRYGNSHPSYNKYSHYQHGFNYNNSGNNRNESGHPRFRNSRRNYNNQGAYPTYMSNGRSANQSPRNNPQNVNNGSTPIQIPVSLQTPYGQVYGQPQYIVDPNMVQYGPILQPGYVPQYYPVYHQTPYTQNFPNMSRSGSQVSDQVVESPNSSTLSPRNGFAPIVKQQKKSSALKIVNPVTHTEVVVPQKNASSPNPSETNSRAETPTAAPPQISEEEASQRKDAIKLAIQQRIQEKAEAEAKRKAEEKARLEAEENAKREAEEQAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEEKAKREAEENAKREAEEKAKREAEENAKREAEEKVKRETEENAKRKAEEEGKREADKNPEIKSSAPLASSEANVDTSKQTNATEPEVVDKTKVEKLKASEGKSTSSLSSPSHSTSSKRDLLSGLESLSLKTNPKSEQCLESLLNSQFITDFSALVYPSTIKPPSTEEALKAGKYEYDVPFLLQFQSVYTDKPMKGWDERMKETVASAFSDKSSRGMYSSSRQSSRSGSNTHSHAGPGFGGPSERKGISRLGIDRGFSSSGAGFGSGSNYKSAPSRGVSHHGHGGMSGSHRGSQRGSRRGGGERDKPDPSSLTIPVDQVAPLQLSANRWQPKKLTEKPAETKGEDEEALLPPEVVQRKVKGSLNKMTLEKFDKISDQILEIAMQSRKENDGRTLKQVIQLTFEKATDEPNFSNMYARFARKMMDSIDDSIRDEGVLDKNNQPVRGGLLFRKYLLSRCQEDFERGWKANLPSGKAGEAEIMSDEYYVAAAIKRRGLGLVRFIGELFKLSMLSEKIMHECIKRLLGNVTDPEEEEIESLCRLLMTVGVNIDATEKGHAAMDVYVLRMETITKIPNLPSRIKFMLMDVMDSRKNGWAVKNEVEKGPKTIAEIHEEAERKKALAESQRPSSGRMHGRDMNRGDSRMGGRGSNPPFSSSDWSNNKDGYARLGQGIRGLKSGTQGSHGPTSLSSMLKGGSVSRTPSRQNSALRREQSVRAPPSNVAVTSANSFELLEEHDHDNDGGQKDSNSKTSS
The following text describes a protein:
Function:
E3 ubiquitin ligase that plays important roles in the regulation of neuronal apoptosis, selective autophagy or cell proliferation. Stimulates the degradation of kinetochore ZW10 interacting protein ZWINT in a proteasome-dependent manner, leading to negative regulation of cell proliferation. Inhibits autophagic degradation of diverse known targets while contributing to autophagy of midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17 assembles into complexes with the key autophagy regulator BECN1 (By similarity). Controls neuronal apoptosis by mediating ubiquitination and degradation of MCL1 to initiate neuronal death. In addition, regulates NFAT transcription factors NFATC3 and NFATC4 activities by preventing their nuclear localization, thus inhibiting their transcriptional activities. Decreases TRIM41-mediated degradation of ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in neuronal cells. Prevents the E3 ubiquitin-ligase activity of TRIM28 and its interaction with anti-apoptotic BCL2A1, blocking TRIM28 from ubiquitinating BCL2A1 (By similarity).
Subcellular Localization:
Cytoplasm. Lysosome.
Sequence:
MDAVELARRLQEEATCSICLDYFTDPVMTACGHNFCRECIQMSWEKGKVKKGKKKQKGSFPCPECREMSPQRNLRPNRLLTKVAEMARQHPGLQKRDLCQAHQEPLKLFCQDDQSPICVVCREAQEHRMHRVLPLDEAAREYKLKLEEDIKYLREEMMKTETLQAKEEQTLTEWQERVKERRERILEEFQKVVLFLVEEERRILQVLKKEEEDTLGKLQDSKASLDHQSRSLDLILLQLEERSQQEPLQMLQDVKDTLNRKESFSVQYPEVVLPAAIKTLCRVPGQIEVLKSFQEDVMPDPSSAYPYLLLYESRQRRYLSPPPEGSAPYSKDRFVAYPCAVGQKSFSSGRHYWEVGMNLTGDALWALGVCRDNVSRKDRVLKSPENGFWVVQLSKGKKQLSLLPNSTLVTLTEPPSHMGIFLDFQAGEVSFYSVNDGSHLHSFSQAAFPGPLLPFFCLGAPKSGQMVISTVTMWVKG
The following text describes a protein:
Function:
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
Sequence:
MWELTKSFRFEAAHSLSGTTFGAASEEIHGHSFRAEVTVRGTPDPETGMVVDLGLLQRAIEDVRLTLDHKFLNKIEALGKPTLENLSRFVWERLQHIGKLTRVSIHRDSCNESCTYYGPQG
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Sequence:
MDLNNSLILNSIENEYNDIFQIPLELLVEDQEGLKDLTCAICLQLLQSPSQCSFGHMFCLACIEKSIKKSPQCPVCRGFLNMKILSRSLFVERTIGKLKVYCRYRFKVEPRQKTPLKQLASPTSTTTIASDSSSNNSSSNSVGNSGIVGAAEPDFSFDLEGCNHTDSLENISNHEKTCIYRFEKCKYNINYLNNIGVSGIVVSNLNSSSKSISISDTNSVNNSPNNKSPRVVLTNSPGSDNGNSNDNNGSSVNIKKLKQDEKNKIIISTSIKSASSPKSCSIIRFKDLEKHYEVCPYRPVLCGYCKTEFYDLKIKEHEENCEMRKVECEKCKSQVAKKELKLHLSDSCPNQTIKCTFGCDKEFERKDLIDHLNESIAIHMVMMKQQHQNEISSLKKEFNLQMASKEDKIKSLEKTLRERVLDSKIKVEWRIKNYLECKKAGYVQSEKFIIKGFSFFIGFFVDGDSNDSKGYISIYLFLDTTDIQKGKSLSLDFSLKFTNQKDQNQSLQREYKHIGFPLGSDGQGWGDRRSIKTSILESAGFIKDNSLLIASEITVKKEFYQVEESSIEKH
The following text describes a protein:
Function:
Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.
Sequence:
MIELGPDVCSTSGNISEDKDSKVCVVSLIGKSSISSTKSSLFNEFAWANIFPKELKKVWRTKSICIEGHYLEQQSVFLLHLTSTQDVLHLYNVMHHFKKYNKNKEKMKKFLKKCEHDHLKALVLIFSVSHIILVNIPGSTFDTNYVKLFKDVEGLRQLFKPHITKRLELNCPNLPRAWIANGRLCSPRVLFILGSCILPLEATPDSADADASVNSGVESSGKPKNKNSALRDLQHFIEDMVYKILRNDRIITNVSNNSLFAIPANQEFVLINHQAGPSSSTPSQSSANQSSNNSNSSFDSLSFLTEHLSQSCKFPSAESSRKAKSYSASRSQLMPTVQSTASLKKASSSASPSSSDILETPSILTRLRCDEPPICSFLRPHIDIALKKGFDDNVGRQHVSPVFELPTVNQMLDVVSQLHALIFKHESGLGGGHTIDRDKFLNDMKEVDAYFANNVDLLEKFLENLNNKLLPLAEEMYCEGLPKFYTKDYHTTKLEQARNYFVANARGPDVLKYWRQLEVKFTDMWMNGRRLCEAISMLGHQCCNELHRLPEDKKSERLVLNEEDEVNEADSSLPAMEHTSNVVTRATCNCGGTQNDRDDPFDFKAANYDFYMALEEKCCHKYEHYVFTTANSEKGANFDFNMLPDESSFSPTGHEEPLYDPILMSSPLHQYNSSNKSDGTKCSQRSSNTNADDGELCSSNASKQDATDDFYANANFSLGGFLYLINYLLTYLFIFLTFPSPIATCDLFTLDKLDQSGDFMGMVYVGGGNEIRYSDIPGDVINDDDAYVDAVDDDDDGGGHFQLSQVDDISAPDDSFTEIPDDFYSKDNSGDCIIDYDDDDDDNNNGDDDDVEDSGGGDDNGGGGGGGGGGGGGGGGGGGGGGGDLQEDGKEYFSNFENSLGMSNRSFLDFSSIISQSEPKESGLSISSADVGLLTDLHVQKPLKPVKPKRLSLAMLNSVSIQHGILPAFPSWSLLKVGKYCSYEASTGINQPNFTHQANFLLPIDAKLQVATPSSNLWPTSASKKPATKLLRMYVGLEYECFKGHRFFLSSPNKMFKAPVSGVFKETGHKIVNQDMPMYFPCSCRSSLVYLAQLMRIHVAVPEGDIEVRLKVKVQPGPPPCPVFFPEPTESIVLEPGWWVMRLPYVYYDGATSYFMPSDTKLLSSCKLLKNFISVTQRSS
The following text describes a protein:
Function:
Has a role in meiosis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MYRKWDLCITRHLLPYIEHSVIPIIALLVLSLIFYILYICFGTTSYILSGIILGAYVNSLFHNNHSVILNIKHPELGEPLKPYQTPLPPELEAPLQLLISKLTQHYINGWYKHVSEDPSFIREVQSTIEYIMRQFYAYVSSQESSHIIYELLKNAISTTTLVLSDLNHFRSKKIPLTEFALRYPESAVSKLLDQASIERTLRAQASAMIVKFSRPEDSACLPLHCLLREVLAMQVFKRITTHCSSPRFVNRCIILYFSSSEDKSDCLAKKNYVNKCLMAKALKDYPVHTNIDPDAGKLSFDDAFYEAHIELHYQFLKEASLNTLIKDKKMLKFIITVRPVHLHVSPWVVYRRYRGFKTLYYLLKKQSARNGRAVPSFPVWRGNTYEKFREGLYFFIEALLHDSHFATNVDVRKFFAKSMRSHPLVDDIYNGFDVDKKHQSSSVPTLPNLTNISRVLSNKTSKSAKPKRSERTGLLSHQSTLAPEPLSQQRDSFELCTTGYRDTGSCTSDDEDSIHEPYRPASTQPTENPPAMPDHNGSPTTEPPKPNAFELKEERLKEIISGGFALVDELCSLNSKLWFFRKSVLTIMKTTVLHGPGRFSAQVERMLKNQIYDKLSNTQLVGDLLTSLILNVWPDEKKAMESHSTRAHRRSTESKISFDSEADSLFEEASKSVPEDPVSVFCDEESDESLRLRAEKTLVENALSENFTLMLGQSTSEESLKIIFELLQEPQFVQGFLAHLLSNALRSII
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.
Subcellular Localization:
Cytoplasm. Secreted, cell wall.
Sequence:
MPTAPLRITVIGSGVIGLSAAHELAAAGHQVTVAYDQELAECVSSVAAAIWFPYHSENSPAADKLLADSLARFEQLSEHPETGIDLRRGLNVDHLPGADRSWTRIVAGTEEASPADLPDGAHAGVWATVPIITMSTYLGWLRGRVEELGADFAKGTVTDLAQLKGGADLVVLAAGLRGGELLGDDDTVYPIRGQVVRLANTKNLTQWLCDDNYPDGVSYIIPRREDIIVGGTDTANDWNREVEPQTSIDILERAAKLVPELEGLEVLEHKVGLRPARETIRLEHVAGHPLPVIAAYGHGGAGVTLSWGTAQRVAELAAQLAGEPAS