lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity).
Subcellular Localization:
[Isoform 1]: Secreted; [Isoform 2]: Cytoplasm, cytoskeleton. Note=A cytoplasmic form may also exist.
Domain:
Comprises six structurally related gelsolin-like (G1-G6) domains, that, in a calcium-free environment, are packed together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. Binding calcium may release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. G1 and G4 bind two Ca(2+) in a type I and in a type II manner. G2, G3, G5 and G6 bind only one Ca(2+) in a type II manner. Type I Ca(2+) binding sites are shared between actin and gelsolin-like repeats G1 and G4. Type I binding governs the strength of interactions between gelsolin and actin by direct participation at the binding interface. Ca(2+) binding to G2 and G6 disrupts the interactions between G2 and G6, releases the C-terminal tail, and induces large interdomain rearrangements that result in the exposure of the F-actin-binding site on G2 and contributes to the activation of gelsolin. Binding to phosphoinositides may inhibit the severing and capping properties of gelsolin.
Sequence:
MAPYCSSLRSALLVLALCALSPSHAATASRGRAQERAPQSRVSETRPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFQGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNNIYQWCGSGSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGSEPEAMLQVLGPKPDLPQGTEDTAKEDAANRRLAKLYKVSNSGGSMSVSLVADENPFAQSALRSEDCFILDHGRDGKIFVWKGKQANMDERKAALKTASDFISKMQYPRQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGPGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVLVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSRDGGQTTPASTRLFQVRASSSGATRAVEVMPKAGALNSNDAFVLKTPSAAYLWVGTGASDAEKTGALELLKVLRAQHVQVEEGSEPDGFWEALGGKTAYRTSPRLKDKKMDAHPPRLFACSNRIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVRQGFEPPSFVGWFLGWDDDYWSVDPLDRALAELAA
The following text describes a protein:
Function:
Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MILVGLSKTLIGFLSDLIKRFFQPVQKDGSFKKPNLSSSSSPTPAVDGETKTPAVVEDEENKSQKKEPTKLLTWNANSFLLRVKNNWPEFAKFIDDIDPDVIAIQCIGRGIYISEALHYQTWSKALFLKCYALYLVRGIETGSITERYDEFRCGKTQLCHTLCITCQCVTCQVVVKGRPQRLLQIADRFGLNGNDVLKNVAYARAYNTDHQSRLLLEAASMMEGRRVHVIERDLTEPDRIVGELLQPGGYLKLIELGLEDCVDGTEAQQVFGYAIYMDGQNTKLSYPLEKFESDISGRSFHNGRFIQRMREKAASLPKYSL
The following text describes a protein:
Function:
SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells.
Subcellular Localization:
Nucleus.
Sequence:
MDGEEKTYGGCEGPDATYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFRERPSHVLSKVCMYFTCKVRCANSSIEIPEFPIAPEIVLELLMAANFLDC
The following text describes a protein:
Function:
Probable transcription factor that acts in a feed-forward loop with nhr-68 to activate genes involved in the vitamin B12-independent breakdown of the short-chain fatty acid propionate. This pathway is triggered in response to a diet low in vitamin B12, when canonical vitamin B12-dependent propionate breakdown cannot function; the resulting accumulation of propionate is probably sensed by nhr-10 and/or nhr-68.
Subcellular Localization:
Nucleus.
Sequence:
MTGGGPSSNNSSQPEEVCLVCSDISTGYHYGVPSCNGCKTFFRRTIMKNQTFSCQFQGKCPVDKSIRCACRHCRFEKCLQVGMDRNAIQQNRDPIGYTKRTRRYPPIKKVEASDECSPAMVSENDRSEDNFLTLLSSTEQKCCALRLAEYMPSRTLIEAVVSDCLLTDEVFMAEHAILSPRHRVTSLRFANQSDYHYWHERDWFVMIEWAKTLPVFQSLPFTDKLALLRHSAITYPSLVHVFNSPDHGLDTIVFPDGAYFDRTPEPTRPLGFNKKKYQMLDQLLKPMRSMEIDMTEFAAFKAIFFLNPDADDVDSNAKKTLSDGRSAITNALYRYMVKKKGAEDAGDRFGRLLLLGTVLATMAVEMKEAVLVADFFDQIQFSTFAKQLLFGIKTE
The following text describes a protein:
Function:
Component of the set-2/ash-2 histone methyltransferase (HMT) complex (Probable). Required for the di- and trimethylation at 'Lys-4' of histone H3, a mark associated with epigenetic transcriptional activation. Implicated in the epigenetic inheritance of lifespan over several generations. Functions as a transcriptional regulator. Acts in the germline to limit the longevity of the soma, probably by regulating a lipid metabolism pathway that signals from the germline to the intestine, thereby preventing accumulation of mono-unsaturated fatty acids.
Subcellular Localization:
Nucleus.
Sequence:
MRSSKGGRGRQAAPKTAPTTVCYCDGKRELGSVEVVCSTCLKWFHGRCLKEFHELNSNGVPFMICYTFTCKQCRPTAEDWKAKKADLVQMCVTVLATLSAERLKADGKLSAEHVPEDFTYLSLKDEIVPYMNENWYMLTAIKQKKEWHQNLAPTLLKEKNIFVQHNDDDDLFALAEKNLSLLGPLHEAVKLIGKRPIERENREPRHIELPPIEGPKTRGASKRRHAEAPVTGKKQKLAADYSSTAAPNGVQIDIPFSKDNYRYYLTEVDPNVPEDPAWNQNQSSAYVIPSFHYRELLNPTVNVSSNDRAFQLSINGNSITGFEGYSMARASHGVSKGTWYFEVNFDDQPDDSHIRIGWSQSYASLQACVGYNKFSYGWRSKHGTKFHEAKGKKYHFGGFKQGDVLGCLIHLPVDKKLQIPANLPSEKYLPVSHKGFNLISFKANYFFEVQEESADIAKTLVEMPGSYIEFFHNGKSCGKAYENIYAGAYYPSISIFKSATATMNLGPKFRNLPRGATGIHARADEQQHEQTLSDMLYLVSKEVNLDHPPRVKREDDDDVKDIKKEIKQEI
The following text describes a protein:
Function:
Myosins are actin-based motor molecules with ATPase activity. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. May link the complex to the actin core bundle of microvilli.
Subcellular Localization:
Cell projection, microvillus. Cytoplasm, cytoskeleton.
Sequence:
MSAFRLGDHVWLNPLSANKTSVAIGSIVKETKPGKILVVDDEGKEHWIQAKDLDTLSPMHPNSVQGVDDMIRLGELNEAGMVHNLLIRYRQHKIYTYTGSILMAVNPFQVLPLYTLEQVQLYYNRHMGELPPHVFAIANNCYFNMKRNKRDQCCIISGESGAGKTETTKLILQFLATVSGQHSWIEQQVLEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNPNGVIEGARIEQFLLEKSRVCRQAPEERNYHIFYGMLLGMTAEEKKLLSLGTPSEYHYLTTGNCTSCEGLNDAKDYAHVRSAMKILMFSDSENWDLSKLLAAILHLGNVEFMAAVFENLDSSDVMETPAFPTVLKLLEVEYQALRDCLIKHSIIIRGEFVTRPLNITQAADRRDAFVKGIYGHLFLWIVKKINTAIFTPPAQDPKNVRRAIGLLDIFGFENFQNNSFEQLCINFANEHLQQFFVQHVFTMEQEEYLSENIAWDYIHYNDNRPTLDLLALKPMSIISLLDEESHFPQGTDTTMLQKLNSVHANNKAYLQPRNIHDARFGIAHFAGEVYYQTEGFLEKNRDMLSTDILTLVNSSKNKFLKEIFKLESAGTKLGQSTIIQASAGSQLFKSADSSKQPSTLAGQFKKSLDQLMKILTSCQPYFIRCIKPNEYKKPLLFDRDLCLRQLRYSGMMETVHIRRSGFPIRYTFQEFAQRFGVLLPSAVRLQLRDKARQMTLRIAEMQLGTDKEWKVGKTKIFLKDNQDTLLEVQRTQTLDKAAINIQRVLRGYKYRKEFLRQRRAAVTLQARWRGYYNKRNFKQILLGFERLQAIARSQWLAKQYQTMRQRMVQLQALCRGYLVRQQVQAKRRAVVVIQAHARGMAARRNFQQQKANGPLVIPAEGQKSQSILPTRKRKSIYDTITDTEMVEQVFGFLPSMIGGQEGQAPWRFEDLEAKSQKLPEVDLDTVPLVEESEDDVDGLAEYTFPKFAATYFQKSASHTHIRRPLRYPLLYHEEDADCSAALAVWNIILRFMGDLPEPVLFARNGPPGGSVTRQIRDSLGREGGTRSPPHCGSTQKSSRRDRGSKDISSMKLKRSSKITSQVTSQLNIGEEAFEPDGPISDRPMSNLEKVHFIVGYAILRPNLRDEIYCQICKQLSENFKTSCLARGWILLSLCLGCFPPSERFMKYLLNFIGQGPAGYGPFCAERLRRTYANGVRTEPPTWLELQAVKSKKHIPIHVILVTGESLTVMVDSASTSREVCLHIAHKQGLSDHLGFSLQVAVYDKFWSLGSGRDHVMDTVAQCEQLARDRGENERQSPWRIYFRKEFFTPWHDSQEDPVSTQLIYRQVLHGVWSGEYNFEKEDDLVQLLAKHCYVQLGASVGSEAVQELLPSCIPSKLYKTKPPEKWASLVTAAHAKAQYTQKQAKPLAVQEQVVDTARLQWPLLFSRLFEVTTLSGPRLPKTQLILAVNWKGMYFLDQREKILLELSFPEVVSLITNREAQGGQRLVLSTLHEEEYKFMSPSSVAIAELVAMFLEGLKERSVFAMALQNRKATDDTTILPFKKGDLLILTKKQGLLASENWTLGQNDRTGKTGLVPTACLYTIPTVTKPSAQLMSLLAMSPEKRKLAAQEVQPTEPLPEEQPKEKPHTLEEFSYEFFRAPEKETVRRTMLPLGRTQGHLWAHSSEPLRQPLLKQVHANAELRDPACQIFIGILRYMGDYPSRQAWTSVELADQIFSLALQESALRDEVYCQILKQLTHNTTRYSEERGWQLLWLCTGLFPPGKALLPHAQKFVDTRRKKLLAPDCSRRIQRILRTGPRKQPPHPVEVEAIEQNISRICHKIYFPNDTSEMLEVGTYTRVRDVCQGIATRLQLSSWEGCSLFIKIADKVISQKEGDFFFDSLRQVSDWVKKNKPQKEGAPVTLPYQVYFMRKLWLNVTPGKDVNADTVLHYHQELPKYLRGFHKCSQEDAVHLAGLIYKAQFDNNRSQLASIPKILRELVPENLTRLMSSEEWRKNILLAYDKHKDKTVEEAKVAFLKGICRWPTFGSAFFEVKQTSEPSYPDIILIAINRHGVLLIHPKTKELLTTYPFTKISSWSSGSTYFHMALGSLARGSRLLCETSLGYKMDDLLTSYVQQLLSAMNKQRGSQTPALADP
The following text describes a protein:
Function:
Functions as an activator of the E3 ubiquitin protein ligase ITCH in the ubiquitination of the CXCL12-activated CXCR4 receptor. Thereby, triggers CXCR4 endocytosis and desensitization, negatively regulating the CXCL12/CXCR4 signaling pathway.
Subcellular Localization:
Early endosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Recycling endosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Note=Enriched in endosomes compared to the cell membrane.
Domain:
The cytoplasmic PPxY motifs mediate interaction with the WW domains of ITCH.
Sequence:
MILLVNLFVLLSVVCVLLNLAGFILGCQGAQFVSSVPRCDLVDLGEGKICFCCEEFQPAKCTDKENALKLFPVQPCSAVHLLLKKVLFALCALNALTTTVCLVAAALRYLQIFATRRSCIDESQISAEEAEDHGRIPDPDDFVPPVPPPSYFATFYSCTPRMNRRMVGPDVIPLPHIYGARIKGVEVFCPLDPPPPYEAVVSQMDQEQGSSFQMSEGSEAAVIPLDLGCTQVTQDGDIPNIPAEENASTSTPSSTLVRPIRSRRALPPLRTRSKSDPVLHPSEERAAPVLSCEAATQTERRLDLAAVTLRRGLRSRASRCRPRSLIDYKSYMDTKLLVARFLEQSSCTMTPDIHELVENIKSVLKSDEEHMEEAITSASFLEQIMAPLQPSTSRAHKLPSRRQPGLLHLQSCGDLHTFTPAGRPRAERRPRRVEAERPHSLIGVIRETVL
The following text describes a protein:
Function:
Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow. Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration. Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically, the immunoreceptor tyrosine-based inhibitory motif domain is phosphorylated by the Src kinase LYN, which in turn leads to the recruitment of the protein tyrosine phosphatase 1/PTPN6, leading to the negative regulation of BCR signaling. If this negative signaling from is of sufficient strength, apoptosis of the B-cell can be induced.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MRHQLRDFFIFRLIASRFPEFWHIKVWLLHGHTMWCFLWMFFFEGVLCFENAIVISPNLLTAWKGSCVLIPCEITSKLRNISLIWWYNPFWHPSLKDYYGIMLYNASTASINHTSPVSTHFQDRVRFTGDLHNRNCSLKISQLQKSDTGMFGARLQGFDQYKHFKKWFLSTDITISDSPPKPKITFSPQEIQEKEKTYVTCSVSYHCPDEPVMVILTGLEEGRMIPQKAIERKRVAQTYLSFMPTWKDHRKQLTCLLKSHNGTEISRDAVELDVKYAPRGVQLTATPGITVTEGMKLSLKCLVNSSNPAASYQWKKNSGIIYYTEDQIEFDSVQEKHSGRYKCTAKNQFGTVDSNELTIDVQYPPKETKVQCPSCGNIREKNPVVLQCSSKGNPSIRRYEWFKHSEQSKISMQKELRFKAVQPSDSNTYFCKAYNGIGNSTSLPFTLDVQYGPKDVQIDILNLFPIKEEDIITFNCSVGSSNPKTNTYKLLNSRDVPVKSTTESNLITFPAKPGPITSYKCEACNDIACTQSPEITVDVHFAPKEVRAVRQPSGLIDEGAIVKLSCEVGRANPEELTYIWYKDTDQVLSETPILTIQKVTSRASGNYHCKAKNSVGIVSSSAVLLDVRYGPKDIHVSLNLQEAVIEGKDALLQCKNTANPSANVYKWYWNGEEMAQKNTPVLELRKVQVGQSGDYSCKVSNQVAEGQSQPMALIVYYSRATVLKRSLIGLGTVLALLALLGLLAYVLWRRKKNIDSDTGGTQRSGSFFVKKTKGERLCNNNNRENEVRADGSVGFLNQGSEGSVTYATVQFRSNLSEDRVVYSSINQPKPAVDPSDTSDIYSVVKKPGNTTTGDTKHDYENVDKMEEELHYSSLVNLAPRPGPTYGDSETESESEDSIQYASLKH
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MAEIVEADNYEGIITRIEHKSRKIESLLKQYKPVEALKTALEGSPPKTKDERCKSANWIVVHRAIMANKDVDSLFSALDPEYYDILMNIRGYTNILPLKQDDNFKQFTADLVSFGSGLVFNLKSAFILISVKKKKELCDARYLYRGLSTGDRPTCDQCLRIHEKLTEKAGLGCILRCLADTVNTV
The following text describes a protein:
Function:
Transcription activator. Negatively regulates chlorophyll biosynthesis and seed germination in the dark, and lightinduced degradation of PIF1 relieves this negative regulation to promote photomorphogenesis. Binds to the G-box motif (5'-CACGTG-3') found in many light-regulated promoters. Promotes the expression of SOM, and thus modulates responses to abscisic acid (ABA) and gibberellic acid (GA).
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice site.
Subcellular Localization:
Nucleus.
Sequence:
MHHFVPDFDTDDDYVNNHNSSLNHLPRKSITTMGEDDDLMELLWQNGQVVVQNQRLHTKKPSSSPPKLLPSMDPQQQPSSDQNLFIQEDEMTSWLHYPLRDDDFCSDLLFSAAPTATATATVSQVTAARPPVSSTNESRPPVRNFMNFSRLRGDFNNGRGGESGPLLSKAVVRESTQVSPSATPSAAASESGLTRRTDGTDSSAVAGGGAYNRKGKAVAMTAPAIEITGTSSSVVSKSEIEPEKTNVDDRKRKEREATTTDETESRSEETKQARVSTTSTKRSRAAEVHNLSERKRRDRINERMKALQELIPRCNKSDKASMLDEAIEYMKSLQLQIQMMSMGCGMMPMMYPGMQQYMPHMAMGMGMNQPIPPPSFMPFPNMLAAQRPLPTQTHMAGSGPQYPVHASDPSRVFVPNQQYDPTSGQPQYPAGYTDPYQQFRGLHPTQPPQFQNQATSYPSSSRVSSSKESEDHGNHTTG
The following text describes a protein:
Function:
Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CATSPER1 stability before intraflagellar transport and/or incorporation of the CatSper complex channel into the flagellar membrane.
Subcellular Localization:
Cell projection, cilium, flagellum membrane; Single-pass type I membrane protein. Note=Specifically located in the principal piece of sperm tail.
Sequence:
MLVLMLAAAVATMVRAHTLCRVHTVRTGKVFKSNIQLQGDPLFYAFPNTFVLKNVCKADISVYLGQKVFLTIDNFESSLLPLTVPKSLAVGVPSITSAHFVSGSLVLFVISGKGYSYDYYENTWRKLEGISEPVSHISGDVCCFKGSFCLELSNNLFAYLRGGQIPGTNIYFSDNGGFSFQLMNTDKLSHLTGTLGGIFHLHSMSQVGVLMVENNLGTFHYMEYPLNHSMGIAFSYKNLLEVIMKPYQRGFMVLWNQKSILVSSNSGQIVEHVRLIDQKIFTDLDVEHANINIYSVASNAYELAFLVAEDHLYYGSQSYMGTYVIKLPHQPLWSTHTSIYFEDIGILQVLTPVADPHFAAYDFDKCTVNVQSSLMDEKLALQPCNVELLESTMINTMFTIDMNSKLKLSALMIPRKGENPTPLVMVSNPHALGFKANLNEFGNTFDGNSKYKLDIELKQQHHWGNSDFNFTASIKRHAISSVTVDIADKTLSCVDLKPLSTLISVGCDMTKKIVVQNKISACTMGILNPVQLQKNYTYTIEKEAYDPINHNGEAQDDLIVFYEYKDLGCPRLVYYDKPWKPVVELWKNGIVEEIMNAEYVISEINGLVTYSYSLTAATANCRSQPQNWSTFESDIENEEPFLWNRENYVSCHEDNKDNPLLWPNVEYQVLGGQTNNKIIFGQRNGIYTFHLSVVDPYYSYCNLNTIFSVYVHGALPVTKFQPLLTILLMVTTTLLTAWLAYAIPKQLRSEKGQRLLGFCYQILQLCLGVCFCTWLRGKLRQWLRPRRVKDQNRGKVRVAQKHPET
The following text describes a protein:
Function:
Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MESISRPTLTAHATSLICADTDLRGPISVGPNVIIHPRATIYAAAGPIMLGEGCIVEEGCIIVNRKKDTMKIGENNHFMVGCRIESPSIGNNNIFQPKSTASGGVIVTDNCIISAGTILLPSPTGTDQEPETLPPYTVIYGADSSRRTWDGSGHVAEMALRSKQAEYLREIMPKFNRLRPTT
The following text describes a protein:
Function:
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Subcellular Localization:
Cytoplasm.
Sequence:
MKEKIRKKILLAPEEPGVYIFKNKGVPIYIGKAKRLSNRLRSYLNPQTEKVFRIGEEADELETIVVMNEREAFILEANLIKKYRPKYNVRLKDTDFYPYIRISDDEIPYVEIVKRKLWDGTYFGPYTSVQFVRNLLEILQKIMGFRTCKSDLKRIKRPCFLYHLGRCIGPCIGNIESHEEAIRKLREFLSGNMEEVFDYLKEKMETHSKMLDFENAAKYRDLLLNLSNVLESQGVVFEENINCDVLVHAHDLFVVLRVRNGYLVGKISFEMEGGNVEDFIREYYISGRGDIPKTLILESDLDEMDYSSLGFEYVGPPRSTTEEDLLEKAKKNLENELKMRGLRKEALEELMKLLNMKDFPYRIEGIDISHLQGKYTVASLVVFEDGFPKKGDYRRYKIEQDHPDDYESIRTVVKRRYSKHPLPNLLFVDGGIGQVNAAIEALKEIGKDCPVVGLAKKEETVVFENREIHLPHDHPVLRLLVQIRDETHRFAVSYHRKRREKESLRSVLDNVPGIGPIRKKKLIEHFGSLENIRSASLEEIARVIGSTEIARRVLDIL
The following text describes a protein:
Function:
Involved in transport.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MERNVTLDFVRGVAILGILLLNISAFGLPKAAYLNPAWYGAITPRDAWTWAFLDLIGQVKFLTLFALLFGAGLQMLLPRGRRWIQSRLTLLVLLGFIHGLLFWDGDILLAYGLVGLICWRLVRDAPSVKSLFNTGVMLYLVGLGVLLLLGLISDSQTSRAWTPDASAILYEKYWKLHGGVEAISNRADGVGNSLLALGAQYGWQLAGMMLIGAALMRSGWLKGQFSLRHYRRTGFVLVAIGVTINLPAIALQWQLDWAYRWCAFLLQMPRELSAPFQAIGYASLFYGFWPQLSRFKLVLAIACVGRMALTNYLLQTLICTTLFYHLGLFMHFDRLELLAFVIPVWLANILFSVIWLRYFRQGPVEWLWRQLTLRAAGPAISKTSR
The following text describes a protein:
Function:
Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=12.5 uM) and against Gram-positive bacterium S.aureus (MIC=50 uM).
Subcellular Localization:
Secreted.
Sequence:
SFLNFFKGAAKNLLAAGLDKLKCKISGTQC
The following text describes a protein:
Function:
Represses expression of BhsA/ComC by binding to its promoter region in the absence of copper.
Sequence:
MATDSTQCVKKSRGRPKVFDRDAALDKAMKLFWQHGYEATSLADLVEATGAKAPTLYAEFTNKEGLFRAVLDRYIDRFAAKHEAQLFCEEKSVESALADYFAAIANCFTSKDTPAGCFMINNCTTLSPDSGDIANTLKSRHAMQERTLQQFLCQRQARGEIPPHCDVTHLAEFLNCIIQGMSISAREGASLEKLMQIAGTTLRLWPELVK
The following text describes a protein:
Function:
O-methyltransferase that catalyzes the conversion of macrocin to tylosin, the ultimate step of tylosin antibiotic biosynthesis. Also able to mediate the conversion of lactenocin to desmycosin.
Sequence:
MAPSPDHARDLYIELLKKVVSNVIYEDPTHVAGMITDASFDRTSRESGEDYPTVAHTMIGLKRLDNLHRCLADVVEDGVPGDFIETGVWRGGACIFARGLLNAYGQADRTVWVADSFQGFPELTGSDHPLDVEIDLHQYNEAVDLPTSEETVRENFARYGLLDDNVRFLAGWFKDTMPAAPVKQLAVMRLDGDSYGATMDVLDSLYERLSPGGYVIVDDYCIPACREAVHDFRDRLGIRDTIHRIDRQGAYWRHSG
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MSWRGNLSRNLKELRFLFCQTSPTSAQTRHLSLFLYNFNGFGLFVLKNYKDLKTMNPKLPILIRECSGVDPQLWARYDMGVERYVRLDGLTESEINKILEDLIKSGTSTNA
The following text describes a protein:
Function:
Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Sequence:
MLDFLTELRSSGSRADQLPGNIYTEFFANVIEEPREHGCKSADQDFTQGFSMLRTFDTENSNQLEPPAATDADVWIFGYGSLVWKTDFPYIDRRRGFVWGFKRRFYQHSIDHRGIPERPGRVVTLLPGDPAQDRVYGVAYRIAASQKGAVLDHLDYREKNGYERCSLEFHEYPTDGAEPIQVIMYVATQANDSYAGDVWQVPCIARQIFSSAGPSGPNREYLFNLAAAMDQLFPGAVDEHLEELVACVKRYIVEDEPQLIRHALLHEISGILEEEQLAEQAHQLEKLLERCQKPGGREWLIYAALQAKNKS
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:
MAFRNRARGGGRRRGMVRVDGPRAGQAAEGAWHAAADQEGGGACAGHLPAAAIWLLRRRRRKHPASLVDEEEGGRRLEAASRPASMVVSSSLAIVCFACKGEKGSEHSATVALQPPFAVYNGRFGPGLGQSMVCADTTDHAKQFEGIFHWRRARAKTERVNRLVKARKPYLQESRHLHALCRARGSGGRFLNTKKIQQSDLGNLSSVSSLSGSEVSSIYDHEDVDHYHSFHHLYIPFTHSRASWTWPAASEGCCDLLRA
The following text describes a protein:
Function:
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons). May be involved in the maintenance of osteochondroprogenitor cells pool.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MLHSNEINAIPDKVFRDLRSLQVLKMSYNKVSVLRQDAFYGLKSLVRLHMDHNEIEFVNPNAFYGLTSLRLVHLEGNLLKQLHPDTFVTLSYLQIFKASSIRHVHLSDNALTSLPREMLSYMSELESIYLHGNPWSCDCDLQWFAEWAKQRPDVIKCKKDRSSGAQQCPVCASPRNCKGKNFVGIPPAALTCTKPVIHHTLKLKNLTVPEDGDLGSVSAKDFLAPIGSVVLNMTDQGGNRGNLVCNIQKPKEMSPISLHKEDNVTVLRTPFSSFLVCEIAYGHIQQLWSILALYSNSPLKLERSALTTETPFITYRYKQIYSEKDELFTNVEAELRAEPSWLMQNKVALQLDRTATTLSTLHIQYFTDAQIILPAVDQKKVGNNWTVISRANKTQTEHTVLVGGTVQLDCQAIGEPAPAIEWILADGSKVRAPYVSEDGRIIVVKSGTFTLRTADTFDTGLYHCIGTNYNDADILTFRITVVDPYVEHSSVNGAQLSAAVGSILDLPCTSTAVPDAAVSWVLPERVVLHHSVRNRHIFDNGTLRIQGVTERDSGYFRCVAASQYGVDLLVFQVLVRKDKSTPQEVPIAAGEWEESDASGDAMPPSARGKLNSSAALLSWMDQEPSAPARRQQGTHSARTGSGRRRMMSRQHRGKASRRLRGHRRHFGSSAKRANPQRWAAFLEKAKRNPPGIEKQEVETNLPVQLHEFSTVPADEEVTSGAAISPEQEFMIAETERATMSSLGSTAGSTTPVGAGTPPPAPFPQPIPSASPTPADLNPTATTSDSWERPHLSRSSANGGKQSTAAEGAGRTSTLSSAQQRPASPGERNSGRLEAVSATTMGNVTASSTPTTSQNAVGEMHGFTELTDEISTQTGQASAATVSEPNPQFGHVHFHSAPEAVTPALPPGPNIVTHQHTHTIWDVTTHTPRAQQQYGRRRKISGRRKMVRPGRLLRMREHRHNLGKQGSAGGQTATAPAVLLSSTHSPNLPAISNSHSSIDPLRPEAPLSSPSTTNMPSEHPAGTALSTAFRTEENGVPTARQGAASTAVPVGTESTGDAVQQEAESRAPRHSSTYRAQPVSSRLTTTATCTAHTAEITLMMSTRTASAPQSVFSRSSTKDTLGWKITRAFLFGNDTQKEVLRTDAFPPTEVSALLPKTTAAAPRPHVSPLPFTPISAGVHHSGGFPSLGKPTDSSSTSEKPPDGSPAASTAGGMGRESPKPTTTASTAPQRDTKMITSKVFRKGRRRGQRRRRPPKTAPSQSSATGTRTTADTASATTATVSPPAVPTRHAPAAMVSDSPPADWVTALWTLTPPGTAQHGPTAALQTAAAPSMGVSTPPVSLLPRSPRPQTPTAMTPTPPLPSEPLGATRVHPAAVSAAAHSEPTQQLKAFIPVAEWPHLGTDEEATRGGPVAQHMDPGSTELSSRALGTAAPQAQHPTPALPMGGIGAGLPSVEWGGKTFTVDTPTMPTPRQVAAPHAHLGGSSAYSWAGQRQRHETTTSIPLSLSSLSRNYFTKPRIIGGKLAAFTVLANSDAFIPCEATGNPQPTIEWTKMSPDTDAPASGSRWMVLPNGTLAIAQAALQDGGQYRCTATNVLGTARLLATLAVVAYPPRIAGSTRLLTAHAGMPVAMRCPAEGRPPPSISWVLANGTHVSSSSQGNQKVLVRPDGTLTIKDVTVYDRGLYTCTATNPAGTDVLTVKLQVIAAPPIILEEKRQQIAATAGQDLNLPCTAEGNPQPHVHWVLSKGTAVKPLQFVNTRVLLLPNGTLRLSSIVPADSGNYECIATSSTGSERRVVILTVQHRDTLPRIAAASQGMTQLSFGDKLLLNCTATGEPQPRIMWRLPSKAVVDQWHRMGSRIHVYPNGSLVIEAVTEKDAGDYLCVARNKIGDDLILMKVSITMKPAKIDQKQYFKKLVPYGKDFQVDCKASGSPAPEISWSLPDGTVINNAMLADDSGHRARRYVLFDNGTLYLNRAGVTEEGDYTCYAQNTLGRDEMKIHVTVVTAAPQIKHSYKTYVKVKAGDMALLDCEAAGEPKPKIFWLLPSSDIISSSTDRHLLHVNGSLSVRRAKLLDAGEHMCVARNAGGDDTKLYKLDVDAKPPIINGLYTNKTIIKVTAVRHSKKQIDCRAEGTPPPQIMWIMPDNIFLTAPYYGSRIVIHKNGTLEIRNLRPSDTADFICVARNDWGESVLVVRLEVLEMLRRPMFKNPFNEKIIAKPGKTITLNCSVDGNPPPEVSWMLPNGTWLSKGTGTSEFLPGSNGTLSIRNPSRDKAGKYRCAAKNQVGYIEKLIVLEVAQKPTILTHPKGPMRGISGESLSLHCLSDGSPKPSTAWTLPGGHVLDRPQINSRHILLENGTLVIRAATIHDRGNYVCRAHNPAGDFSITIPVTIVAYPPRITNRPPQTIHTMPGAAVQLSCTALGIPRPEITWELPDHSILSTGNHGRASGSELLHPQGTLRIQNPQPSDSGTYKCTARNHLGSDFTVTYIHVI
The following text describes a protein:
Function:
Laccase that catalyzes the oxidation of certain aromatic compounds, including L-dopa, to quinones, which then polymerize to melanin. Able to oxidize a wide variety of aromatic diphenol and diamino groups in the ortho, meta, and para positions but not monophenolic groups such as in phenol, tyramine, or tyrosine. Plays an important role in virulence. Plays a role in dissemination to extrapulmonary sites but is not involved in pulmonary growth or in elicitation of cellular immune responses in the lung.
Subcellular Localization:
Secreted, cell wall.
Sequence:
MLPGPVIEANTGDTIIVHVNNHLPEGQGIHWHGLRQNGTALMDGVPGITQCSIPPGGSFTYNFTVSHQSGTFWWHSHYSNSMADGIWGPLIVHSANESLQRGRDYDEDRIVFITDWMHDNSEVIVAALISPEGYRGSTVPPQGDAILINGRGQTNCTATGSSSCFYPPPPEIQVPVDRRVRLRMISASSHAMYRVSIDNHSMEIVETDGTAVYGPTIHEMSISSGERYSAIINTTEGKEGDAFWLRTSVALACMSQGSTQVGLAVLRYTGNGNITTAEPRTEAWTDLARHDTPCVGLDEMYALSPREPLNASKTALQSRVLNSKLGTFVDVYGTSFEGYGFNNVTYQNQINDPLLSIVQRGGSCNHSLITNATFPDIGAGNIIINNLDAQIGHPYHIHGNEFQVIARGFGALTLDDLSNIDFILDNPLRKDTIWMQGGSWLVLRIITDNPGVWACHCHIGWHLAKGKMAVVVVQPKAIEDIQWSESWTNLCANTDPNAFGPARRSFP
The following text describes a protein:
Function:
Sugar transporter.
Miscellaneous:
MISCELLANEOUS: [Isoform 2]: Incomplete sequence.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAEESLLPSHTEDVSASPNKSSSLLSEISNASTRPFVLAFTVGSCGALSFGCIVGYTAPTQSSIMKDLNLSIADFSFFGSILTVGLILGALICGKLADLVGRVYTIWITNILVLIGWLAIAFAKDVRLLDLGRLLQGISVGISSYLGPIYISELAPRNLRGAASSLMQLFVGVGLSAFYALGTAVAWRSLAILGSIPSLVVLPLLFFIPESPRWLAKVGREKEVEGVLLSLRGAKSDVSDEAATILEYTKHVEQQDIDSRGFFKLFQRKYALPLTIGVVLISMPQLGGLNGYTFYTDTIFTSTGVSSDIGFILTSIVQMTGGVLGVLLVDISGRRSLLLFSQAGMFLGCLATAISFFLQKNNCWETGTPIMALISVMVYFGSYGLGMGPIPWIIASEIYPVDVKGAAGTVCNLVTSISSWLVTYSFNFLLQWSSTGTFMMFATVMGLGFVFTAKLVPETKGKSLEEIQSAFTDSTSEDSTIF