lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes.
Subcellular Localization:
Cytoplasm. Nucleus, nucleoplasm.
Sequence:
MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDQPSGSRDTVRLNGDIVTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKNRLREKERALPPETPAPGAEPPVRPPGPLSAWAPAPCPASLKARLPPAGPKATRPPPAPGPLPWQTPGESDGALDLSLKPGPRRPPVRPPCALQTAPCRQKQPGAQPVVKEEPDSESEREDGSSSPRSAHSPLRPPGVTAAEPLVGGLGPLPVRGVGSGAPGPEAERGELEAALRPSGRLCLCPLCGKLFPGAHVLQPHLSAHFRERDGGRARLSPDGAAPTCPLCRKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHAVVHTREKPHACRWCERRFTQSGDLYRHVRKFHCGLVKSLLV
The following text describes a protein:
Function:
Lysophospholipid acyltransferase with broad specificity. Mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes the acylation of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Can convert lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). Exhibits preference for C18-unsaturated acyl-CoA when transferring an acyl group to lysophosphatidylcholine. Can also utilize lysophosphatidylglycerol (LPG) as substrate in vitro. Has neither activity towards lysophosphatidic acid (LPA) nor lysophosphatidylinositol (LPI). Lysophospholipid acyltransferases catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. The primary function of the Lands cycle is to provide a route for acyl remodeling to modify fatty acid (FA) composition of phospholipids derived from the Kennedy pathway. Is involved in PC acyl editing and phosphocholine headgroup exchange between PC and diacylglycerols. This processes control the majority of acyl fluxes through PC to provide polyunsaturated fatty acids for triacylglycerols synthesis in seeds. Involved with LPCAT1 in the direct incorporation of newly synthesized fatty acids exported form the chloroplast into PC through acyl editing.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MELLDMNSMAASIGVSVAVLRFLLCFVATIPISFLWRFIPSRLGKHIYSAASGAFLSYLSFGFSSNLHFLVPMTIGYASMAIYRPLSGFITFFLGFAYLIGCHVFYMSGDAWKEGGIDSTGALMVLTLKVISCSINYNDGMLKEEGLREAQKKNRLIQMPSLIEYFGYCLCCGSHFAGPVFEMKDYLEWTEEKGIWAVSEKGKRPSPYGAMIRAVFQAAICMALYLYLVPQFPLTRFTEPVYQEWGFLKRFGYQYMAGFTARWKYYFIWSISEASIIISGLGFSGWTDETQTKAKWDRAKNVDILGVELAKSAVQIPLFWNIQVSTWLRHYVYERIVKPGKKAGFFQLLATQTVSAVWHGLYPGYIIFFVQSALMIDGSKAIYRWQQAIPPKMAMLRNVLVLINFLYTVVVLNYSSVGFMVLSLHETLVAFKSVYYIGTVIPIAVLLLSYLVPVKPVRPKTRKEE
The following text describes a protein:
Function:
Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.
Subcellular Localization:
Nucleus, nucleolus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MNKHDQKKKRNKQHTDNVMGKKSKGFIKNKKNIGESGNEKKRNNNFNNIWKKKKRSGNSEKDQVDILGLLKGDSENMNDDDDNNMNDDYNNNNIKGDYNNNNIKDDDVDDDDYDDDDDDNFDENKNCNDNCSSKHKRNVPSKKEHDILELNNINFNETRKKMINYKNIFDGKFCDLKYILSESLINTLEKNEFIKMTSIQKMSIPLFFKPNDIFLKSMTGSGKTLCYAIPSIEKILNMKEKVKITRDMGIFVLVLSPTRELAIQINNLFCILTKPYPYIVASCITGGEKKKSEKNRLKKGISILTCTPGRLLDHLENTKSLKLTFLKMVILDEADKIIYLGTQDKIKLIYDMIRKIKQEEFSKVHKKKKKEENEVLDHINDTNMSDMNNISNDHSNDYEQFILDKFQMIFISATLNHAMKTLANYCLTNNTMWIEKEKKNGINGGNKNDETKQKSNDMISCMNRENSPLNIHNNDDNDDNDDNDENNGDNNNNNDDNNNNNDDNNNKNNDDDNNNTYELPEQLKQYCILIDMKQKFICLIYMLLDCIEKKKKPVVFLSNHHSVEYLQILLKNIYWPTDVNKKNIEVNKKLNEKITPVLEREDEKLLRKHLEQNILNNNYYNNNYNVGNISYKNINLEEIQNEDELNDEPGNLYNINADKHKRIYLFNNVNIYILHGNLSKEDRLGNFMDFSKTNNSILLCTDIISRGIHFDSLSVVIQYDPPQILEEYIHKVGRTARLNKQGSAYLFLLKSQKQFLNILKNKNIQLKIILGNTIINHFKKFCIPNFLKSVGKDILNFLHNHMQTIVKSNNTLMEKGTSAFLCTITSFYSTSKNLRSIFNAKDIHLGHLAYTFLLEKTPKQISKYKKEQNYINIKKQTVLSKKEKRLLKSKQFQKKQKRK
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Required for autophagy (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Note=Peripheral membrane protein of pre-autophagosomal structure (PAS) and vacuole.
Domain:
The first protein part may form a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
Sequence:
MKKNGDGSSPKSPDGVVSRSARSSFRALSNCLKVISSGASTVARSAVSAASSAVESHHDQVLWAGFDNLQKEDGDTRRVLLLAFKSGFQVWDVEDTENVHVIVSAHDGQAFFMQMLLNPINSGVLDDRFYKSRPLLAVCGDYSSKKISSDNPGSETVATPTNVYVYSLKSQSYVHTLKFRATIYSVRCCSRIVAVLQAAQIDCFDAATLEMDYRIVTNSIVCGSLGVGYGPLAVGPRWIAYSGSRIATSSSAIFTSEIVSLSTSSPSVAQFARDSSKQLASGIANLGDKGYRSLTKYCSEVLPNPYIPGLKGIGVGNEKVADAESIGMVIVKDITNKSVITQFKAHKSPISALCFDQSGLLLVTASIQGHNINVFRIMPTISTSRAVKTTTFAHLFRLQRGFTNAVIQDICFSKDSNLIVVGSSRGTSHLFEINPEKEGDAPVPMSAISRIRSGNSSGWIGTVSGAASAAAGMVAGSVPGTVTSTFCYCDEKSNNNYYGSVADMCSKTNLLVFAPSGCMTQYALREHQVGVGHETAAMTGFDSESGLETEGKLAVDPIRRWSMIQNQSRRETHDPHSDIYGGGTSVDSKSKVFPEVVRKQSVEEAWKVSKKGTTRVVDKRHLYIYEAEQQQTHLPTQLPLWARRKFRFQELVLNRGEEISGGGGREMEIEGIQTRTIEARTRDLVPVWGYLQSPRSQQVINESIQSPSTTTQDDKVATLEGHGTETDLGAVHSEEQTQSEPVDKEGIAEEKNHSEDEDEEQVD
The following text describes a protein:
Function:
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Sequence:
MRKCLSIHVGQAGIQIGHACWELFVWNMASSCAFSVPDFQQSLFTVQVDSALMPSDKTVGGGDDAFNIFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLSPPPPPPPPEQLISGKEDAANNFARGHYTVRKVIKDLALDKIRKLADMCTGLQGFMTLSVDYGKKSKLSMFVFPSPQVSSAVVEPYNRILSCHGLLEHTEVNLDIERPTYTNLNRLITQTNLVPYPRIHFMLSSYAPMISAEKAYHEQLSVSELSNSVFEPSNMMAKCDPRHGKYIACAMMYWGDVVPKGVNVSLGTIKTKRTIQFVDWCPRAPDRGPGRRSGQGAARCVHDRQQHCGGGMLAMLNHKFDLMCAKRAFVHWYVGEGMEDGEFSEACNDLAAL
The following text describes a protein:
Function:
Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSAILSEESYGTGKKKLSIYIVGMILCVILTLVSFMTVMYSAFPPTTLVAIIFVSALIQFIVQVVCFLRLNAKNEQSRMNLMSFIFTIVILFVLIGGSLWIMWSLHYRMMH
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAKKKSSKLRQRAAEERKQEEQVLSRRKGAATQDEAQNPFELQQQRRKHDVLGQKVKGERGNKARARDAAIKSREKSLLVEYRQRHKDSRFTDKRFGEYNTGMSVEEKMLARFAAEQRKKHSRSSVFNLDDDDEDAEELLLTHNNRPLSEAMDSYIPSDEEMDEDAQDFGARATNADMVSRFHFGGGDAGDEEEQDDGQPQRKRTHREIMAEVIAKSKSYKHERQRQQQETEDMTNAVDDQLNDILGLVFGESNRAEQEGRVLAAPADSTYDTAIVQLAADNKARATDRLKTPQEEAEEARERLERLEAQRQARLRGEDPEAEQSSNLKSSSEYVGAGDDSDAEEDGAGLELLPMGDGTAKLVSKSGQAVDLNSSAKPGSGVADDDDEEASDDEDDEEAELDDSDAADASEDEFGLEPDFGASTSGAPEHESDAEEDFEVPFVFKPVSSAEDMMTLLEAYPISKRRILLERLIACHNVHLAAANRAIQETHFMALWQCVGQSIQQGEALSALEPLIWSLYTLMLQVKAAAATTARNRIFELHEKTRGGSWPSFPKLRHLIYFQIVPELFPASDRWHAVATPALLAAMHLLTNCNVANMRNMAAGLYLCSCAYVYVQESHRIVPEALAFLNSFLQCCTAAPSEAGSRLLLPAFSLLKPAQRKSLRCTPASWKGLKPAAMPLERLEAGFKGCALEQVKLDLVALALQLTHKFARLYQTHAAMPESLACAQAAARQLEQVPCLKAICTPLVELFDACAGMRDAVRFQAHKPVPLEMLEPDYNAHGFGKRSDQDQTDRENERLRRELRKERKGAVRELRKDARFLSKVKLNDIIENDRDRNQRLKSAFATLQSDQADFNKRDAQKR
The following text describes a protein:
Function:
Together with PDP1, PDP2 and PDP6, interacts with MSI4/FVE and MSI5 to suppress FLC, MAF4 and MAF5 expression by regulating the function of the PRC2 complex and modulating H3K27me3 level, thereby promoting flowering.
Subcellular Localization:
Nucleus.
Sequence:
MEIEVVLGIGEDAGPKPCSAEIESAEKTLKDDGVVQENGVRVSDNGEKKSDVVVDVDEKNEKNLNESGVIEDCVMNGVSSLLKLKEDVEEEEEEEEEEEEEEEDGEDEEEEEEEEEEEEEEEHGYCVGDFVWGKIKNHPWWPGQIYDPSDASDLALKIKQKGKLLVACFGDGTFAWCGASQLKPFAESFKECSKVSNSRSFLGAVEEAVEEIGRHIERVLVCDCAEEKKHEFDSPLVNNAGIKEGVLVRDVRREMISSLLIGKHGEILKDVKSFAETVSFSGLLELEILKRKVSAFYRSNRGYGLTEYHEPQSVPGLEDKNNDDDDDDEEKNVNDGLQWRAKRSRVEEVAALDHEESSSLQRSLEKCSGFPDHRLPHRRKEKSITEIIEKESAAKVRFETEPADGDVKSNVKSGRKKTKRHDEVNGDLENVTTTALWRRRKSEVATIEDGGNKQVVESSKGKTSRKKKKMDVDDGDDDGSGDKEESEEKEISDLEINIDSTSLASLRKKVRFDDSVVERSTENGETATQTSKRERKKSKYLSPDFLSDFSRKGRKKSTIESESSKVSSQSQVDERVTDASDSLMEVEEDTLDKPCEPSSDNGLGQEELSRELSNAVDFLRLGATPKEMQDLIRVAALGTQYPKDSSSRDMVREFMTIYRSFTYHDGANHKFLGSYDSSDKEKEELSEMGKPVTKGKEKKDKKGKAKQKAEEIEVTGKEENETDKHGKMKKERKRKKSESKKEGGEGEETQKEANESTKKERKRKKSESKKQSDGEEETQKEPSESTKKERKRKNPESKKKAEAVEEEETRKESVESTKKERKRKKPKHDEEEVPNETEKPEKKKKKKREGKSKKKETETEFSGAELYVTFGPGSSLPKKEDLIEIYEKFGALDKERTDTVDNNFSAHVAFLDVADGEKAFESSLEKCPFTSNSTVKFRLKYPNERTEEKKTEAEVAETTMEVEYLKKKLDEMKLLLDGCEGGMTEEVKVKLEGEMVNLLEKVIEMRSS
The following text describes a protein:
Function:
Involved in dorsal-ventral patterning. Appears to function predominantly as a ventralizing factor, through its actions as a BMP signaling agonist, acting through both chd-dependent and chd-independent mechanisms. May also antagonize BMP signaling, probably via formation of ternary complexes with chd and BMPs, resulting in dorsalization.
Subcellular Localization:
Secreted.
Sequence:
MGSSSSSSVVLLLLLLSSLSIALACNKALCASDVSKCLIQELCQCRPADGNCSCCKECMLCLGSLWEECCDCVGMCNPRSMSESPATGRSTVEDLFQPIPSLFRALTEGDAPTHTLVLTLPLAEELQYQHNLHNYLETLHNTQHNNTTSVPENSIHSSYHTQDKQCTVVYFDECVSIRQCKQYCESMGGSKYRWFHNACCQCIGPECVDYGSKSVRCLNCLY
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA.
Subcellular Localization:
Nucleus.
Sequence:
MKVFQYLTTLDARDLEDLYKDSWTCQAIVRSLPPRAKQYIFKMLMVDTYPLTIAKDWSQHSSNHQHKEALKKLFDLKIILLNRGKQQSEQSIQLNPLFQENIKSALVEFDKVIFSNSSNIKDTNKIPNINDLDNYSKKQWEQVLYFLSDDAAQPSKFISDLLLSSNLTRRDQDGSLSITSDGFKFLLKDVYTQIWTLLIVYLNDLEKKRREGLTQGSRNDLLGFLFRLSFLQLGKGYLVGELTELQKEYLICLKQFGLIYMKSDASLFFYPTRLIISLTTGKTLSLIQTLAVDKINSSSNSANTVASSTIEKKESGYIVLETNYRLYAYTASSLQISLLSLFVKMLYRLPNLAVGIITRESIRTALIHGITADQIIDFIRHNAHPNAVNNGQPIPDVVAEQILLWEQERNRITYTKSVLYNSFPTTDCYHATLKFAKEQDYYIWSNDQLKTLVVNENGNDPIRNFIKKNFA
The following text describes a protein:
Function:
Thiol-disulfide oxidoreductase involved in the redox regulation of a number of cytosolic enzymes. Activates the cytosolic malate dehydrogenase (MDH) probably by reducing an interchain disulfide bond of the inactive MDH homodimer. Possesses insulin disulfide bonds reducing activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MASEEGQVIACHTVETWNEQLQKANESKTLVVVDFTASWCGPCRFIAPFFADLAKKLPNVLFLKVDTDELKSVASDWAIQAMPTFMFLKEGKILDKVVGAKKDELQSTIAKHLA
The following text describes a protein:
Function:
[Isoform 1]: Essential for normal retinal maturation and development. Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors. In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors; [Isoform 2]: Signaling receptor for cyclophilins, essential for PPIA/CYPA and PPIB/CYPB-dependent signaling related to chemotaxis and adhesion of immune cells (By similarity). Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Acts as a coreceptor for vascular endothelial growth factor receptor 2 (KDR/VEGFR2) in endothelial cells enhancing its VEGFA-mediated activation and downstream signaling (By similarity). Promotes angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA and KDR/VEGFR2 in endothelial cells (By similarity). Plays an important role in spermatogenesis; mediates interactions between germ cells and Sertoli cell and is essential for the development/differentiation of germ cells to round spermatids.
Subcellular Localization:
[Isoform 1]: Cell membrane; Single-pass type I membrane protein. Photoreceptor inner segment. Cell projection, cilium, photoreceptor outer segment; [Isoform 2]: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Basolateral cell membrane; Single-pass type I membrane protein.
Sequence:
MAAALLLALAFTLLSGQGACAAAGFLKAPLSQERWAGGSVVLHCEAVGSPIPEIQWWFEGNAPNDSCSQLWDGARLDRVHIHAAYRQHAASSLSVDGLTAEDTGTYECRASSDPDRNHLTRPPRVKWVRAQASVVVLEPGTIQTSVQEVNSKTQLTCSLNSSGVDIVGHRWMRGGKVLQEDTLPDLHTKYIVDADDRSGEYSCIFLPEPVGRSEINVEGPPRIKVGKKSEHSSEGELAKLVCKSDASYPPITDWFWFKTSDTGEEEAITNSTEANGKYVVVSTPEKSQLTISNLDVNVDPGTYVCNATNAQGTTRETISLRVRSRMAALWPFLGIVAEVLVLVTIIFIYEKRRKPDQTLDEDDPGAAPLKGSGTHMNDKDKNVRQRNAT
The following text describes a protein:
Function:
Mediates influx of magnesium ions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MPNSNRKLGLLPGSVVYTGENPNYNITVTVIYYSKTFHKKDVFSADDKIDIDLEFDGNIWINIDGINDVSLIKRIGKIFNIDSLSLEDIANPEQRVKIDDRDSYIHIILKMLQMEILTKDVQYEQLSLIIKDNILITFQETPYDLFESIRSRLENPRTKLASKDVSYLAYILIDTIVDNYLLVLDEVENEIDDIENKLIESADKEDLENILALKQNIAVLKKFISPIRELISKLQARSMLNYFHEDMKYYLGDLNDHGIIVFDTVDMLNNRATELIQLYHSMISNTMNEVMKILAIISTIFMPLSFIVGLYGMNFEYMPELKWHYGYFITLGLMAGLVILMIVYFKKKKWF
The following text describes a protein:
Function:
PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Subcellular Localization:
Secreted.
Sequence:
MAHARSGSGRLRVHLLAAIIGLLACCAAALDVGLQYAGDDVSKQQACSRTCESDHCTTAPFLRYGKYCGILYSGCPGERPCDPLDACCMHHDNCVQAKNDYLSTQCNESLLECLGELRDGTGTFEGNKCMIDEVIDVITIVIQAAVVAGRVLHKP
The following text describes a protein:
Function:
Involved in gene expression controlled by TOR kinase and nutrient signaling. May also be involved in positioning the proximal bud pole signal.
Miscellaneous:
MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium; MISCELLANEOUS: Deletion leads to a K1 killer toxin hypersensitivity.
Subcellular Localization:
Cytoplasm.
Sequence:
MDLLAASVESTLKNLQDKRNFLSEQREHYIDIRSRLVRFINDNDDGEEEGEGQGMVFGDIIISTSKIYLSLGYEYYVEKTKEEAITFVDDKLKLMEDAIEQFNLKIEEAKKTLDNLNHMEDGNGIEEDEANNDEDFLPSMEIREELDDEGNVISSSVTPTTKQPSQSNSKKEQTPAVGPKEKGLAKEKKSKSFEENLKGKLLKRNDEVKKKVQPSKVDTENVYTFADLVQQMDQQDELEDGYIETDEINYDYDAFENSNFKVNDNYEEDDEDEDEEEYLNHSIIPGFEAQSSFLQQIQRLRAQKQSQDHEREEGDVNKSLKPILKKSSFAENSDKKQKKKQVGFASSLEIHEVENLKEENKRQMQSFAVPMYETQESTGIANKMTSDEFDGDLFAKMLGVQEADEVHEKYKEELINQERLEGEASRSNRRTRVSRFRKDRASKKENTLSTFKQETTRSVENEVVEKEPVVGDIIEKEPVVGDVIEKEPVVGDVIEKEPAVTDIVEREPAVNDIVERKPVVGDIIEKEPTINDIVEKEPEINSKSEFETPFKKKKLKSLQKPRSSKSMKKKFDPKILENISDDDYDDDDDGNKKLLSNKSKNNTDEQDKFPSKIQEVSRSMAKTGATVGSEPVRITNVDYHALGGNLDDMVKAYSLGLYDDDLEEDPGTIVEKLEDFKEYNKQVELLRDEIRDFQLENKPVTMEEEENDGNVMNDIIEHEFPESYTNDEDEVALHPGRLQEEVAIEYRRLKEATASKWQSSSPAAHTEGELEPIDKFGNPVKTSRFRSQRLHMDSKP
The following text describes a protein:
Function:
Mitochondrial protein enriched in neurons that acts as a regulator of mitochondrial respiration. Associates with the ATP synthase complex and facilitates ATP synthesis. May be a chaperone protein involved in the turnover of the subunits of mitochondrial complex I N-module. It facilitates the degradation of N-module subunits damaged by oxidative stress, and contributes to complex I functional efficiency.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MPVHYSSFGAALRPLGRQCRRGSPHLSTPPPSIITTARVNVANNLKVSRNFTISRTLQTGRQEPEHHNNHYETLNVHFDATQAEIKKSFYHLSKTHHPDHNPSDPHASHRFMRISEAYSTLSHADKRARYDRDVLRLHLRARAHGSHHSSSVGPAGGRPASGLSKRRSTTQGAPPPSFFKQGGYGEQKVKREWQQSTGYSSQQQQQQYGGGPGPGPGPGPGQTRGEGASTGGPKQEWSQAFNPASAPHFNSEQHTRTHEQLWENLKKSHARRSEAARQQARWQQQQEEEDEEGKQQWWSGSGSGSTGYHQQEQQQPYKQQQWGESKKVMPEIQQGNWASFFAVTAVLLVSSFGPYWLFGEWMSTGGGGGGGGGGGKKRSGSGGSGGSGGSGGGSRKPTAV
The following text describes a protein:
Function:
Contributes to K(+)/H(+) antiport activity by supporting proton efflux to control proton extrusion and homeostasis in chloroplasts in a light-dependent manner to modulate photosynthesis. Prevents excessive induction of non-photochemical quenching (NPQ) under continuous-light conditions. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MAKKKAFTPLLYLASIVFLPWWISLSFNKSLKSWITNWWDTRQSETFLNDIQEKSILEQFIEVEELFLLDEMIKEYPETHLQKLRIGIQKETIQLIKLHNEDHIHTILHFSTNLICFVILSGYSILGNEELLILNSWVQEFLYNLSDTIKAFSILLLTDLCIGFHSPHGWELMIGSIYKDFGFAHNDQIISGLVSTFPVILDTIFKYWIFRYLNRVSPSLVVIYHSMND
The following text describes a protein:
Function:
Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLELRHRGSCPGPREAVSPPPREGEAAGGDHETESTSDKETDIDDRYGDLDSRTDSDIPEIPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQVKCFHEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLIRYHRFISFALYLAGFCVFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMIWFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVVDVNSFVTECEPSELFQLQTYSLPPFLKAVLRQERVSLYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRGPNPSKVLQQLLVLQPEQQLNIYKTLKSHLIEKGILQPTLKV
The following text describes a protein:
Function:
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Sequence:
MNKGIFITFEGIEGSGKTTQGKLLAEKLKKEGLKVLYTYEPGDTEAGRHIRKILLNSEIKINPLCELLLYFADRVQHIEEKIKPCIESGFIVICDRFTDSTLVYQGYARGISIDLIKQLNKIVLDEFMPDLTVLLDCPANIGLKRNQKINKKDRFEMENLAFHEKVRQGYLKLAELYKKRFFVLDATESIDKIAEDIYRKVKSILSHGL
The following text describes a protein:
Function:
Appears to function as an adapter protein that bridges proteins together or proteins with mRNAs. May function as a ubiquitin ligase-substrate adapter. Additionally, associates with translating cytoplasmic ribosomes and may promote the expression of specific mRNAs.
Subcellular Localization:
Cell membrane. Cytoplasm, cytosol.
Sequence:
MVIHVYIASSSGSTAIKKKQQDVLCFLEANKIGFEEKDIAANEENRKWMRENVPEDSRPPTGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFLGLTAPPGSKEAEAQAKQQA
The following text describes a protein:
Function:
Secreted scaffold protein that plays an essential role in dorsoventral patterning during early development. Stabilizes axial formation by restricting chordin (CHRD) activity on the dorsal side. Acts by facilitating the association between the tolloid proteases and their substrate chordin (CHRD), leading to enhance chordin (CHRD) degradation (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MRALQLLVLVLSGLVGAQQQALMDYLERRLLAIEDRISLWHEQTSRYASELREFKQQMVAQLEGLDKSKEALRSELDTVGTRVDRVEREMDYLETQNGAQPCVDVDDKLVEQQVTFVKERNKAKYAKLTDCSDMISSIKAMKILKRVGGAKGMWTKDMGSATGKVYILNGTDDNTVFEFGTVREFTSSQGTSGATTIQLPSAWRGMGHAIYNNHMYYLKQGEEMKLIKFDLQKNIIVDSAVFPVKNQLPVYSLNPETFIDLAVDEEGLWAIYATQENERHISLAKIDPKTLDIQQMWDTPCVRENAEAAFVICGTVYVVYNSKLPSRSRIQCVFDVSDMVNNDEAPHVYFPKRYGTHSSLKYSPVEQLLYAWDDGYQILYKLQLKKKLEV
The following text describes a protein:
Function:
Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation.
Subcellular Localization:
Nucleus.
Sequence:
MEPVASNIQVLLQAAEFLERREREAEHGYASLCPHRSPGPIHRRKKRPPQAPGAQDSGRSVHNELEKRRRAQLKRCLERLKQQMPLGADCARYTTLSLLRRARMHIQKLEDQEQRARQLKERLRSKQQSLQRQLEQLRGLAGAAERERLRADSLDSSGLSSERSDSDQGECPEAEGLCGPRGKPGLLTRPLPAQRSWRWMWRAWCLGVRPSCCGASSPARSTATRTAAAPGYDVPHPGRASALYSCQAHLPGRSPPQAFRAARSHLLEWTKRTLVWEQVLPKHPAAGCQAGPLEGKGQDSSGPPWTPAGQAAWAAQAFGSAAPKGTGSLLGLFPSWTRPPAFASRKLYSIFIKSLFHNFPSIVLPNENGGTPNHRPTGRGNNISSHH
The following text describes a protein:
Function:
May act as a phosphoinositide 3-phosphatase by regulating PtdIns(3,4,5)P3 levels.
Sequence:
MREEGSELEMEKGFLKWKPVNLMKKILSLPMKKTKNDIGLRLDISYILVNLIVCSYPVNTYPKLLYRNSLDDLILFLTVYHGKGNFRIFNFRGEKEDSDYKDNDLIGIAAKFESKDFEIQELRSTLINDGKIPISPIDLETRTLVEEETNNVICERIGWLDHFPPPFELLEEIVDGIENYLSVSKNRVAVLHCRMGKGRSGMITVAYLMKYLQCPLGEARLIFMQARFKYGMTNGVTIPSQLRYLRYHEFFITHEKAAQEGISNEAVKFKFKFRLAKMTFLRPSSLITSESAIVTTKIQHYNDDRNALLTRKVVYSDIMAHECGGNMTFIFGRDYLTLENDCRIEFTLGTSKSKAASSIISWTSCASCWLNIYLETLMHIIKDDSSPDYFQVERLKRDEMLGTTISWQELDGFGELSTHGLKLFQALKLEWEII
The following text describes a protein:
Function:
May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Subcellular Localization:
Lipid droplet. Membrane; Multi-pass membrane protein.
Sequence:
MADRMQPHQVQVHGLKGHQQQGPSASKALAVLTMLPLGGGLLALAGITLVGTLIGLAVTTPLFILFSPVLVPAALVIGLAVTSFLASGAFGLTGSWSLSWVGRYIQEATQTMPESLDQAKRRMQDMAGYVGQKTKEVGQEIQRKAHDGK
The following text describes a protein:
Function:
Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context (By similarity).
Subcellular Localization:
Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2 (By similarity).
Sequence:
MEIATRCEVGAMRGPSSDSVSHDIPQPQSPPSVKIRKTAFKFFGGRKSICVLPSFFGGRGRSQRKGSSKTGVTKSQTYDGVSRACWDDLGRSSSEVASGDFEFCSEPQKSQEDHGKSQSLPRQRRGLRGLFSSIRRHRKNKNVEVEKREALEMSSSFHAKTVPGALPSVSDRGDYHGDSQGEELVPDVPNQTTGSECELPLAATECTIDVTLVPEKRRSRVEMDKRRRAEEEGIGEDEKTGRQEGLMTYHQPLSAESELDRLAEQNVDVPDGEPPVASCSSENLVFGDVSSLKSFDSLTGCGDIIADQDDVSVAESSVSADRGSRNAGKRSSCFVTYQGGGEEMATPDEIDADYLQSLWESETSNEVCYIPSDRGSDSPSLTPDQQLSSIRATSSSSPMGITETALTPADLLSPQSDRQESVPNSDEGYYDSTTPGMEEESRERPHQERLPRDSYSGDALYELFEPDDRLLSPSLPPKDAHSFVGAPLQADKSPTNPLYSLASTAIETGAMETEEERLSKIQHALLCCELQNLRSPSKNQLLFHSDCFYDDSNLPVDDSKQDLQEVINQRYPQSPPRSQAVKEGVPRIRGQVQESSLFAPCADSVLNPQVIETTRPQPQSDDQGSLRPSRGCSQSQEELMVCFSQALVDFTKNTRLYRNSTESLDGSESSSPFGPSLRALPAIVTFDVVDMENEGECEQQTDLAEEEEELASPYEPFEDDGCYLQQDAFAECDQRTFDAYEQSLLLSNAWGIASLPRHLSLGRPCPPVPAPLALNRRSRSLDTDSLEFQTSEIYTSVTKYDSKGTAFSQSRTVDCNDMDFPRQPCRITVDSWRRGYRQNFDSSNASQQELKLPHLSQSTVRPSHLPLKNNCRSRNLPAATRVDGEGEILFGGGDALYPCSYPPMGTQWKNRPVGVTQGVPHLRSEQSADH