lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MAADDAARSSRRMDLNLYLGLPRAPRLRRPDLGSDLALGTPMLSSSPSSSAASADAPPLETEPLHPPYSPPPAELVRPPTPLPEPYDPSAPEAHPPYVPPPVPPPEAIPELADDLEFGFSHPPLLLRPSELLGWVDRPSSSTASSSFRPERVDRYRPPVICLNSRQSRCLRPRRFRSDLPPLGSEAPALENDAAAQPPPQEPMQDTVEENKVVADGAIVGASEEEPAERGKSVAMFECNICFEMASEPVVTSCGHLFCWPCLYQWLHVHSTHKECPVCKGEVTEGNITPIYGRGNSTSDAEKKVAEEGNVSGPTIPPRPHGNRLESFRQKFHHLRPISRRLGEAHGILSSWRRILDQQIMNSVSRFEGPPESTVQEMIDHAHHASRLGRITTRMRARRLQREAENSTFVASSAAESGLPANSTSDLPRRSSSPFSSERIDLLQHFVDLASTERLASAVSDLRRMVRPSPYGASTSSNPPNPPNTELLPVDGNHVAVALAADQASNSSTMAVIQEDAAFTESTGEPSNAGSSRSLRRRGRNDALGSLDVDGVGLHRNKRRRLN
The following text describes a protein:
Function:
Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ).
Subcellular Localization:
Nucleus.
Sequence:
MAAPRRKKARIAETEKCEHRVLFPETNIFIVDRKMTKTRHDFLQALARRKGFAVCDQYGSAVTHIVAEDLSTEQVMEYFHNKGVTSLYPGQELLTMEWFTKSMEEKQPVPCTDHLRLKPAQAAVPVSTEKMTLPKHECQRITRLKHHNHRFTTALEVLEEHAGYLQVGQKTDSRARAFRRAACSLKALPHPLTNVEEARTLPHVGTHSLSVIQDILEDGYSQEVQDISDGDFYGTMQLFTGIFGVGSATARKWYERGFRTLDDIRNDSTLSLKKDQTIGLELYQDLNTPVTLAEADIIQEMVRAEVQKLLPGATVVLTGGFRRGKTKGHDVDLLISHPTEGKETGLLSAVLAKLREKDLLAYETTSANTYDPSSVSRKEYTLDHFERCFSIFKLDKSLISSNQNTKQAPPSPVGAVQQGSSRPDLLHHKDKVSLERAGGTASFLDEEKTEEKTWIGRRVDLIIAPASQYAYALVGWTGSKHFNRSLRLYADNEMNMKLTNHVLYDSVKNQYLPASSEEDVFLHLQLPYREPAERNC
The following text describes a protein:
Function:
Inhibits P/Q- (Cav2.1/CACNA1A) and N-type (Cav2.2/CACNA1B) voltage-gated calcium channel by modifying voltage-dependent gating. It selectively and reversibly blocks the calcium channels coupled to glutamate release. Also inhibits potassium channels (Kv2.1/KCNB1) with lower affinity. Has also been shown to weakly inhibit Kv11.1/KCNH2/ERG1, Kv1.2/KCNA2, Kv1.3/KCNA3, Nav1.5/SCN5A, Nav1.7/SCN9A and TRPV1.
Subcellular Localization:
Secreted.
Domain:
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Sequence:
MKAQIFVVVLGLAALSVLCYGSEADESALHEEIFQLLAASDEVPKPQERDCVRFWGKCSQTSDCCPHLACKSKWPRNICVWDGSVGK
The following text describes a protein:
Function:
Plays a role in spermatogenesis. Involved in germ cell survival during meiosis. Lacks protease activity in vitro.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MGGFCGADRGGFLALLVWLQLLQPLFSGTYKPREDSGVMHRPQRPRRPRSDPEAPAQQSRLKSLSISHPSGVPVSVDRTEIPGSGSPSGTTTKITLENRRSSLGGPFFTDTCGHRITEVDPGSLSAGRKWPWQVSLQSQNEHVCGGSLISHRWVLTAAHCIYEQEEYMVMLGDDMLHSESESVTLVPVQDIIFPSNFDIQTMRNDIALALLYFPVNYSSLIQPVCLPEEPFRVKNGTVCWVTGWGQQNEIDAGFASILLQEVQQRILLQKHCNTLFQRQLGTSKNLVIKGMICGLQDSGQSLCWGDSGNPLVCESDNTWTQVGIMSWGINCNGVPVLSVYTDIAEYNEWVSYVLSQASRMDPMGVLVLYLSLVFPLALLVAL
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; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MEFGLGYIGVGIAAGVAILGAALGIGRIGGSATEGISRQPEAGGKIQTAMIIAAALIEGAALFALVIAFQAAGTLNEGLKATVAHQTKASAVVTEEKGK
The following text describes a protein:
Function:
Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MVPSPPPTFCGRVVHHLKSDDDFRTATDAFMILFAVVGSVSAATSSYLLGLVAIAIVMPIAYLIGRKRPNKAILLPGAFLGCAVAVNLAYTVSHEGETWEHLTRYFVFLFLFHFTEFVFTALTNRRSLRPDSFLLNHSVGYWLAAGISWVEFGIEAYFFPGIKSYPVLWIGTIGCIIGEICRKLAMIHAGLGFTHRLAMKKRVDHRLVKDGIYAYMRHPGYFGWFVWAVSTQIILCNPICFVVYAYVTWHFFASRIYDEERDLIAFFGDAYVEYQREVWIGVPFVSGYQRP
The following text describes a protein:
Function:
Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones. This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MREETSSPLGAPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEAGVADLTWVGDRGILVASDSGAVELWELDENETLIVSKFCKYEHDDVVSTVSVLSSGTQAVSGSKDFCIKVWDLAQQMVLNSYRAHSGQVTRVAASPHKDSVFLSCSEDSRILLWDTRCPKPASQMGCSASGYLPTSLAWHPQQSEVFVFGDENGTVSLVDTKNANCALSSAVHSQCVTGLVFSPHSVPFLASVSEDCSLAVLDSGLSELSRAHRDFVRDATWSPLNHLLLTTVGWDHQVIHHIVPTEPLPAPGPKSVAK
The following text describes a protein:
Function:
Potential calcium sensor.
Sequence:
MWQQLVASIDRGLVLSVSSLLIISRGVRAVSRALVRLALLLVHVVDEDDDYRYCAADAGDDGVVQPPRLRCCERCAAAPWLSRHDVAAVVASLGLVAADEDDEEGDHQAPCGACEAVAAVEKLAESKVAGEGELREAFRVFDRDGDGYVSAAELRSVLRRLGMEEGARHGDCVRMIAAHDGDGDGRISFQERGDATRAAARGSAQWNGRHGSCAG
The following text describes a protein:
Function:
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Sequence:
MGCCGCSGGCGSGCGGCGSGCGGCGSGCGGYGSGCGGCGSSCCVPVCCCKPVCCCVPACSCSSCGSCGGSKGDCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQCNCCKPCCCSSGCGSCCQSSCCNPCCCQSSCCVPVCCQSSCCKPCCCQSSCCVPVCCQCKI
The following text describes a protein:
Function:
Involved in the fatty acid remodeling steps of GPI-anchor maturation where the unsaturated acyl chain at sn-2 of inositol phosphate is replaced by a saturated stearoyl chain. May catalyze the first step of the fatty acid remodeling, by removing the unsaturated acyl chain at sn-2 of inositol phosphate, generating a lyso-GPI intermediate. The fatty acid remodeling steps is critical for the integration of GPI-APs into lipid rafts; Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MGLTGTAPLPAHWLRAWRPRPLWVTPTWRPRPRVARAPPLHVEAGRNWERWDIRGALGCNGCGLRGHWAVLVLYWGALGRGWTCHDDCKYECMWHTVRLYVQGGPPRAAVPWQVALLAVPLCPGASLCLRLPPQRPGQLRDAAALQSCRAPHLPHVPHLRRLCLGLRQCLVLVHRLPHAGHGADRETRLLLRLSRRPALRVPVLGQVSSVPALGTTLPLGLGVCHCRPPAHRTMGLRRPALIGVFRAFLLLFLACHISYLTLVRFDYGYNMAANVAIGLLNLLWWLWWCLRNRPRLPHVWKCAVVVLLLQAGALLELLDFPPLFWVLDAHALWHISTVPLNILFYSFLVDDSLYLLKANSDLSKAD
The following text describes a protein:
Function:
Involved in oxidative stress response and redox homeostasis. Required for hydrogen peroxide-induced oxidation and nuclear localization (activation) of YAP1. Functions probably in concert with HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
Miscellaneous:
MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MEPIDDILFEVTDAFKTQKEDLLELVTLIDIYGEQVNQEGSYEEKTRFIETLNTLLEDNPSTTGEIGWDLPKGLLKFLSKDNVDVNGRLGTNMIVQGVMKCFYAISIQGEPKKCLITGLELLSSLCSKDFSKSDQQNKEDFVDKKANTLPPEGVIENSSNRKDFPSYGESKSSNEFFLKLKSYILFEFIGASLKRISTLFPSKYLGAAVSTIEKFVYSHADTFEDALFLLRRVYTFCRNYIPPDPPKDIQLNEDFTREMFDKVVEEESELQVRLLRRLCTFGISTPIKTVTTNADVKYYCALNQQKFELSAYYTEYLELFCRYYQMAFSLDVDIEGEFQNVIKECRIIYKSVPQEISAVNDEAKLVLERMVYKLAYTFEVQKAAKEKNVGLDYNGVILFSGIHYLETNQHLVKEMNITDAIYLYLRFTTPSLYSKVYYNVAVESVSRYWLWYAITTEPLEDVKKELKNLSVFVTKTLLHVLLQKNCIQVNQQLRMITFTLLTRLLCLIPEKVAFEFILDVLKTSPLPLAKTSVLCVFKDLSRRRISTKDNDSETDLIVEKLSKLKVNDSNKAQQSNIRHYIQLDSSKMKAVHDCCLQTIQDSFTADAKKSDILLLLTYLNIFIVLKKTWDEDLLKIVCSKIDSNLKSVEPDKLPKYKEIVDKNESLNDYFTGIK
The following text describes a protein:
Function:
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan.
Sequence:
MEQNKCALVTGSSRGVGKAAAIRLAENGYNIVINYARSKKAALETAEEIEKLGVKVLVVKANVGQPAKIKEMFQQIDETFGRLDVFVNNAASGVLRPVMELEETHWDWTMNINAKALLFCAQEAAKLMEKNGGGHIVSISSLGSIRYLENYTTVGVSKAALEALTRYLAVELSPKQIIVNAVSGGAIDTDALKHFPNREDLLEDARQNTPAGRMVEIKDMVDTVEFLVSSKADMIRGQTIIVDGGRSLLV
The following text describes a protein:
Function:
Component of the ribosome.
Sequence:
MSGKANKQKQAKQTNPLIVANKKVFGKGNVAHPRDLTRYVKYPLYVRIQKEKRLLMKRLKTPPAVNIFANHTLDKTNATQLFKILDHIKPEERAAKLQRIRAAAKELAEKTQKGEKATASKKTEKPATLSYGINNVVRLIERKQAKLVVIAHDVEPLEMVVYLPYLCKKLQVPYCIVKGKARLGQLIHRSTAAVVAVTEIKKEDKAAFESLVQNVKSIYFENAHMYREFGGRINGFKHNEKQKKIQSKLNKDLADKAKQQAALTVTTAVEEKAAPVAEEKKADKTA
The following text describes a protein:
Function:
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. TlpQ is a chemoreceptor that binds and mediates chemotaxis to histamine, a key biological signaling molecule. It binds histamine with high affinity, which permits responses to very low histamine concentrations. Chemotaxis to histamine may play a role in the virulence of P.aeruginosa by recruiting cells at the infection site and consequently modulating the expression of quorum-sensing-dependent virulence genes (Probable). TlpQ also binds and mediates chemotaxis to polyamines such as putrescine, spermidine, cadaverine, agmatine and ethylenediamine. In addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm formation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFLRRLSIQWKITLLAGLCLLGVVALLVGLSVYRMQHSSVLVKSASTQMLDESARLRLEARGELQALRIQRYFMDAFQYGKGFSRQILFLRDQAQKRFLDAYDLREDLTRQVRTALAANPEVLGLYVVFEPNALDGKDELFVDQPALGSNDKGRFSLYWAQATPGQLESESMIESELADTSSGPSGAAYNAWYTCPKESGQPCVLDPYFDKVGERQLLMTSIAFPLELDGKVIGVMGLDINLSNLQALSEQGNRELYDGVGQVGILSPAGLFAGNSRDAGLLGKNLAKADPQHAGELLQLLAAGKSRLFNENDDLKVLQPLQPIPGAKPWGVLLEVPKSALLGPALALERQLDDMRREGTWVELGLGLGAAVLGLLVLWLSARGVTRPILGVAHMLRDIASGEGDLTQRLPHTGRDELGELAGWFNRFLDKLQPIIRDVKVSVRDARSTADQSAAISSQTSAGMQQQFREIDQVATASHEMTATAQDVARSAAQAADAARGADQATRDGLALIDRTTQSIDSLAANLTSAMGQVEQLASSSEEIGSVLEVIRAIAEQTNLLALNAAIEAARAGDAGRGFAVVADEVRNLARRTQDSVEQIRGVIEGLQQGTRDVVDAMHGSHRQAQGSVEQVDEAVAALQRIGEAVTVINDMNLQIASAAEEQSSVAEEINRNVAAIRDVTESLSSQAEESAQVSQSLNRLANHQQGLMEQFKA
The following text describes a protein:
Function:
Confers resistance to late blight (Phytophthora infestans) races carrying the avirulence gene Avr1. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm.
Sequence:
MFSGEYLSSTKHHPLKFLQRIEDEWGSYMPETIKERVYLLKTEFKFMDMFLSIQSFTDKPNMLTVTQKVHALFQDSAFDVSKIYQNLNRLTSLLQNKIRVTKMEIGANYSFFSEISLQQLSEKSGVDNSEFVMKFINGVVENVSELAEMDDLCSREIQEVLKELKLLKSLVGFLSNRWYAEPQSVRTFFGHVLFVAGSAAMVVWLYIPSYDNNRDQDLVPGEMNFLLSYLVRMRIKPVNPCIRKIYVDVLQALKWTMQSELSLNIQNVYVAEIEAGFIEILIHNLEEIRSISTLSRIEFLNHLMATLVEMLKFLRASLIHLPKLGLEFHLKDIDTISIDVGLLVYSLYDREEQDEEVNQTLFRDMPKSIQHIKEVIFLVSRKAFQSNLPRVHGLGCVDFLLNNLKEFQDRYSDSQYSFVKSQLQVIQKELEGLQPFLKDVAEEWYNKHERLHHCAALLNGKAYEVEYIVDSFIKKEVPEWCLVRWLFDIIKEVILIKEEVTKIRKKELLKFDFVLNDTLDTTPAHISSESINTPRITDEEVVGFEDVMEKLREQLIRGTKQLDVISVVGMPGLGKTTVANKLYSDELVVSRFDIRAKCCVSQAYSRRSVLLSILRDAIGESPTLTKLPTDVLADQLRKTLLWKRYLILVDDIWEASVWDDLRCCFHDSNNGSRIILTTQHADVAENAKSVSDPLHLRILNDDESWKLLKQKVFGEESCFMLLSNVGQEIANKCRGLPLSIVLVAGMLTKMEKSEKCWKQVAKNLCTNVLSNSKAIIEQSYQNLPYHLKPCFLYFGVFLEDKEINISILTWLWISEGFIKSCDDKSLEDIAEGYLENLIGRNLVMVAKWGSGGKVKTCRIHDLLLYFCKEIAREKNLLLWMRRDQNVNTSSSIYSHKQLVQRRMSINSQVVDLVKWSSLVGTVRCREDRNKGSFSIVQFSHIYFRFLKVLNLELIVIDSFPTELVYLRYFAARTSQKSITSSIVNLRNLETLIVKPMGGKLILPLTLLKMVKLRHLQIYSKAHFSTLNAADELLENSKFDNLITLSSPTFCCVRDAELMLRTPNLRKLRCSFVGWGYPSHVMSSLTRLETLSIKMDSCGSSPSNFPPNLKKLTLSNFTMHWLQSSIAMLPNLQVLKLVAVFFSKAEWEVTSDKFHQLKVLKVVDCPCFKKWNVSDNAFPCLEHLVLRRCRYLEAIPSRFGDITSLISIEVKSCKESLVESAMVIRESQVEEMQNYDFKVFINK
The following text describes a protein:
Function:
Expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic.
Miscellaneous:
MISCELLANEOUS: P.bifermentans strain Cbm (subsp. malaysia) is toxic to Anopheles mosquito 3rd instar larvae and less toxic to Aedes aegypti larvae.
Sequence:
MSKKPLDFLRIYDWHKTEAMNKISKLDFERIIPKHFSKEIKNKHLSVKITGNWKIWKLTDEGEGQYPIFKCIVEDGFLKIKNECGNKKYSLDNAWIKICTKIKYDNENGKDIYSIDEKNLTLYSVNNSFNSKYKNNIVDAFLDNLLIACIEDNIKDLNKFFKLYKVKTAIKEDLSLLGWDTGYSTSFTHVNKTIENQQNYPKQFKYESEGPYNIDISGEFDSWRLTTGSDGQNVNFICPIKNGEFNFLGTEYKFSQGEQVNIQLKLKYLNIEEPTFEDSTSLNDGNQVDLIVKTDEDENENPPVTIIKVVLLGEIDAIGKMLLEGTFREWFNENIDAFKQIFSSFLLEDTSKNPDFQWLKPTKAYYGVASAEPIDGKPDLDSSVFSVMSMVEDNKNDKPSHTVDGRILDAVNNESAFGIRTPLFVKKWLIAGLEMMQIGKLEDFDLINNGMGFINNKKLLFGTFENADGEDVPAYVEKDNFRLEITNNQLKIEITDIYWQQSRRLTGHVMYSQYFDLELRSGTDITGAEYKNILIPVENSEPTLVVNISQDEFDIWGDIVGEIVGGIVVGIVTGYLGSILGKGVGKYLEKFLTKTSGGRWVLKMNKEMYDYLNNLFKGDRRVFNEVAIDEIELISTLGTSQAISTIANTPTNFASKIWVNKSKFIGGLIGGSVGSVIPSVIIKSIDAWDKQNYSVLPSINAFVASSVGSVKWPDTSEFKIESAELNGIFLLGGKLERYEK
The following text describes a protein:
Function:
Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled (By similarity). Required for the polysaccharide cross-linking at the septa and the cell wall (By similarity). More specifically, transfers chitin to 1,6-beta-glucan in the cell wall (By similarity). Plays an important role in fungal pathogenesis via its functions in cell wall assembly and regeneration, filamentation, and adherence to host cells.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Sequence:
MKFTTLATIASTLLFAANANADTCNPLKSSDCSPVPALGSSFLEKFDNGLGPHFESLKKQGTIDSGSNGLSLTMKKRFDNPSFKSNFYIMFGRVEVVLKGAEGKGIVSSFYLQSDDLDEIDIEMFGGDPYQWQSNYFIKGNTATYDRGGYHDIANPLKDYHTYVIDWTKDAVTWSVDGSVIRTIPKDNAQGFPQSPMAIYAGIWAGGDPSNQPGTIDWAGGITDYSQAPFTMGIKSVLVADYSSGKQYSYSDQSGSWESIKADGGKVNGRYDQAQDDIKKLESGQSVDSNDSSSSPSASSSDSSSTSSASSSSSSSSPSSTTSSSSSSSSSSSSSSSSSSEKSNAVPSASVIVFIGTKGGDKTTVTSSSGVSVPTSASVSTAAGTTSGSANSAPASAASSTASTVFISTGDAAPSSSASEKPSVSTTENNGAVSVAKTTSLFGFVALIGFLFV
The following text describes a protein:
Function:
Sodium-phosphate symporter.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVTGPDMLWLVITSGIACFFMAFVTGANDIANTFSTSIGSKAISIKKALIVAFFFEALGASLLGGTVTDSIRSKIINFQVFYDTPEFLMLGMCCALMGATVWLAVATRAGLPVSTTHSIIGALLGFGLATGNMKSIKWEKINNIVISWLAAPILAGTCSAIAFTVLRMLILRKKNSFEIIKKMYWFLIFLITLPFSVFLIFHNPIVINTQCKMKKDGKVIVSSPCYIEDWSAAHSFYASIICILLSSLLTAIGSFVIYIIYNKRINNYNLKKKIFCEELADIEKNPQNNFCAINNSSLNSVASNETQLTQAHNNTSNGTKQNQVGNGTKSNNNNVLVLPGDKNVKSQQDDSKTNGTQKTGSVEAHHVVHIKDNGSEDKSHENMLKKNLDKVTNMNENNNNSNKNNNSNKNNNSNKNNNSNKNNNSNKNNNSNKNNNSNKNNNSNNGNSNEGNGKGGDPKNMENVIIENFDPQTEIVFSSLQIISAILGVVAQSANDTANAIGPFAAVFNTYNNGIRGKIKVQWYILLFGGLSMSLGLSIMGYRVIKTVGMKLIKITPARGFTIELISGLVVLFFSICGIPLSSTHCAVSSVIGLGLVEAKMNADNKRHARKSMDKDIIQVDKDKSFTLTEKIKYPFSFLNTSCVNLRLFRTVFLSWILTVVFSATVTAGIYSFAAYSPSYIMKMQTV
The following text describes a protein:
Function:
Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (tTJs).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cell junction, tight junction.
Sequence:
MIPPRALLLISVWMVSGGRTLLVTVQDTQRYTMLFSSIILKCDYSTSAQIQDVAVTWRFKSFCKDPIFDYYSAAYQASLSLNQDPANDCNDNQREVRIVIQKRGQNEPVLGVDYRQRKITIQNKADLVISEVMWWDHGVYFCSVEAQGDTSGDPDKEVKLVVLHWLTVLFIILGALFLFLLIGICWCQCCPHCCCCYVRCPCCPTRCCCPEEALARHNYMKQMESMTPWMLDRPYYAGADRNSQHSSYQLNPLLQRDLSLQSSLPMPAPMSFSPPNNKVLDFLETEIKNLNTAQPLMSAPHYGGASHHPSMLSSLSEVGVREVDRRVIQLPPLVEHIVSSHRSSNSSHQRRNMGSWDPLDGERDRRRNRQLDDSLSNETNWRAQERQHSDRSSGHRRDPPNNRRPRRDVSPPRRYGDSYSDESANNDPRGRSNPHSDRARPTERRRSPERGDQGRRGSPDRYSRSQRHRRSYSPPHRRDSWSSEDETRNNQRGRGRRERSYEWPEEKPPSYKSLEICAGKAPTQRPGAVRQSDRASSRSGRSMVI
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MSRTLSRRVLTQSPLSSIAEFANIHTLPLRCSRPFSSTSNQRAEGDDPLSNYVPHNSSTLRYGGASGAIARASAARSASLNPKATRSSAAGGGGIANIFQGMMEVSKEKKGAFQNTSVPKDGTLIGDRIVEDEPHHFHVYATRHNTHITLTRPNREPIISVSCGNIGFRHSGRKHYDSAFQLAAFVMSRIHERAIGRDIQKLELVLRGFGAGREAVTKALLGTEGRWLRGKVVKVTDATRLKFGGTRSKKPRRLG
The following text describes a protein:
Function:
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MAIGESKDERDQRVAKLWESLDVQKKGQLDINGLKKGFKRIDHPLKNADDMIRNILQTVDTNGDGYIDFSEFRAFVDHTEHRLWRLFESIDRNQNGVIDKNELRAAFSRSGITLSSAKLDAFFEDVDSNKDGVISYPEWRDFLLFLPAHSPSDLHAVFSYYTATGNLNPEGDVHINDLQGLGTDHSFLTRYLLAIKDILYNIFPVHSLTALVPPAYAEAGGTLLLGAALEHDSLALDDDFELEWLPIPRTVAMWMSFRNFEQKLTENTPQLGYFLAGGIAGAVSRTATAPLDRLKVYLIAQTGAKKSAAQVAKDGAPLKAAGFASRTLVGAVKELWRAGGIRSLFAGNGLNVVKVMPESAIKFGAYESAKRAFARFEGHNDPKRLQPTSQFLSGGFGGMVAQCFVYPLDTLKFRMQCDTVEGGLKGNQLIAATARKVWNKAGLLGFFRGLPLGLVGMFPYAAIDLSTFEYLKRALLARQARINHCHEEDVPLNNFTTGAIGALSGGFSASVVYPLNVLRTRLQAQGTVLHPTTYTGITDVARKTLQTEGPRGFYKGLTPNLLKVAPAVSISYVVYENAKRMLGLR
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Miscellaneous:
MISCELLANEOUS: Was identified as a high-confidence drug target.
Subcellular Localization:
Cytoplasm.
Sequence:
MATGIALVGPGAVGTTVAALLHKAGYSPLLCGHTPRAGIELRRDGADPIVVPGPVHTSPREVAGPVDVLILAVKATQNDAARPWLTRLCDERTVVAVLQNGVEQVEQVQPHCPSSAVVPAIVWCSAETQPQGWVRLRGEAALVVPTGPAAEQFAGLLRGAGATVDCDPDFTTAAWRKLLVNALAGFMVLSGRRSAMFRRDDVAALSRRYVAECLAVARAEGARLDDDVVDEVVRLVRSAPQDMGTSMLADRAAHRPLEWDLRNGVIVRKARAHGLATPISDVLVPLLAAASDGPG
The following text describes a protein:
Function:
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Subcellular Localization:
Cytoplasm.
Sequence:
MKILVDENMPYARELFSRLGEVKAVPGRPIPVEELNHADALMVRSVTKVNESLLSGTPINFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSALLMLAERDGFSLRDRTIGIVGVGNVGSRLQTRLEALGIRTLLCDPPRAARGDEGDFRTLDELVQEADVLTFHTPLYKDGPYKTLHLADETLIRRLKPGAILINACRGPVVDNAALLARLNAGQPLSVVLDVWEGEPDLNVALLEAVDIGTSHIAGYTLEGKARGTTQVFEAYSAFIGREQRVALETLLPAPEFGRITLHGPLDQPTLKRLAHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVMCDDETAAALLCKLGFNAVHHPAH
The following text describes a protein:
Function:
Negatively modulates the activity of the FtsH protease for membrane substrates. Overexpression or stabilizing YccA counteracts the FtsH-mediated degradation of SecY when the SecYEG preprotein translocator is jammed.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Note=There are conflicting results regarding the localization of the C-terminus of this protein: According to a report, the C-terminus localizes in the periplasm. Another report gives the C-terminus in the cytoplasm. We show the periplasmic location.
Sequence:
MDRIVSSSHDRTSLLSTHKVLRNTYFLLSLTLAFSAITATASTVLMLPSPGLILTLVGMYGLMFLTYKTANKPTGIISAFAFTGFLGYILGPILNTYLSAGMGDVIAMALGGTALVFFCCSAYVLTTRKDMSFLGGMLMAGIVVVLIGMVANIFLQLPALHLAISAVFILISSGAILFETSNIIHGGETNYIRATVSLYVSLYNIFVSLLSILGFASRD
The following text describes a protein:
Function:
Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3. Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR. Desialylates EGFR and activates downstream signaling in proliferating cells. Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Membrane, caveola. Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein. Lysosome membrane; Peripheral membrane protein. Note=Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to cytosol and the catalytic region facing the extracellular space (By similarity).
Sequence:
MEEVSSCSLRSTLFQQEEQNRITYRIPALLYIPPTHTFLAFAEMRTSSRDEDAVYLVFRRGVMKGCSVEWGPQQPLMEATLPGHRTMSPCPVWEKNTGRVYLFFICVQGHVSERWQLLWGRNAARLCFLYSEDSGCSWGEVKDLTEEVVGSEMKHWATFAVGPGHGIQLQSGRLLIPAYAYLISCWFLCFPCSVKPHSLMFYSDDLGVTWHCGKFIKPQVTGECQVAEVPGKAGNLVLYCSARTPNKFRAEAFSTDSGDCFQKPTLNQQLCEPRGGCQGSVVSTRPLKMPYTCQDSSGKDVPSTQKCPLMDRSLEVEEGAGAPSGTWLLYSHPTNKKKRMNLGIYYNQNPLEVNYWSRPWILNRGPSGYSDLAVVEGQGLFACLFECGERHEDEKIDFCLFSDQEVLSCDDCTSPSSN
The following text describes a protein:
Function:
Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity.
Subcellular Localization:
Apical cell membrane.
Sequence:
MEDLHTDIRSPLTQTWNGGVWSSAQIRKRLLNHTRYTLLPGEDMADPDETVPMQSKSTEVEEVEFMPGESLDTNSPKNDRIRIAMSLIAVVVLVGVAFAVGYIVRLVLFKCGPEDEGKTLDLTAKLVKEASDSISSSRIESQLRYFTKIPHIAGSQESYDQALYMQKEWLKYGVDSAELKKYNVLLSYPTRPGLASIWNTNGSEMFRASQREKSLNKDEEKPNVLPPFHAYSPSGQVTGRLVFVNYARVEDFKMLKTMGVPVAGHIAIAKYGAIFRGDKVKFASEAGAIGLLLYSDPDSSPEGPGKVYPDAYWLPPTGVQRGSVYLEDGDAVTLGYPAVDGAYASPTKDAGFPKIPSYPISSQDAEHFLKLLTIKEAPKEWKGGLQMTYYTMMDPNDERNVSLDVEMSLETKPVYDVVGIIRGSVEPDRLVMFGNHRDAWVFGAADPSSGTASLMELVRVFGELKANRNWRPRRTIVFLSWGAEEPGVLGSTEWAEEFSNLLSYRAVAYLNVDIAVQGNYSLRLKSSPLMDYAVFDVAKKVLVRTVLGHGSRPIYTCLRKTEPLDAVIKSFTASAKSFHEHLESINLKDPLAVRMANDRLVQFEKSFINPEGLPGRPYKRHVVFAPSAHNLYLGVSFPGLFDALYEAQDLGKGDWVQVNRQLEFVVHHIRMVGNLMSINTV
The following text describes a protein:
Function:
Involved in resistance to stress. Facilitates intracellular growth of M.tuberculosis. Associates with and regulates lipid droplets (LDs) homeostasis under conditions of stress and may regulate non-replicating persistence (NRP). Could be involved in preservation of envelope integrity and tolerance to surface stress. Has an inhibitory effect on ClgR activity. May block ClgR activity after stress and then, form a multiprotein complex with Rv2743c-Rv2742c, leading to the release of ClgR.
Miscellaneous:
MISCELLANEOUS: Overexpression of PspA results in altered lipid droplet morphology.
Subcellular Localization:
Cytoplasm. Note=Localizes to the surface of lipid droplets (LDs).
Sequence:
MANPFVKAWKYLMALFSSKIDEHADPKVQIQQAIEEAQRTHQALTQQAAQVIGNQRQLEMRLNRQLADIEKLQVNVRQALTLADQATAAGDAAKATEYNNAAEAFAAQLVTAEQSVEDLKTLHDQALSAAAQAKKAVERNAMVLQQKIAERTKLLSQLEQAKMQEQVSASLRSMSELAAPGNTPSLDEVRDKIERRYANAIGSAELAESSVQGRMLEVEQAGIQMAGHSRLEQIRASMRGEALPAGGTTATPRPATETSGGAIAEQPYGQ