lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcription factor (By similarity). Plays a role in regulating the developmentally arrested larval state known as dauer, when induced by long-term exposure to the Gram-negative bacterium P.aeruginosa PAO1, but dispensable for dauer formation induced by starvation. Involved in regulating expression of microRNA mir-243, during long-term exposure to P.aeruginosa PAO1.
Subcellular Localization:
Nucleus.
Sequence:
MNSSSSRSSMSMPMPMDMPQMHMGMNNNCEMNQMMHPIPNFPMKWEPCTPPDEKPHPSMLFPPLSGIFNQSRHSSTGEDYHGSSSGSPSSSLSSPNEFKDEPLGLDVHFGNSLFNAPFSPSATSSHSPSSYGMMHGSHSMASHQLHQQQLSPLPSVAHFSHSHHLQHHVVQHPSQASLQMNMNQIFSGPSHQYASSSVPHTFLFKDSTIYEGMGGMGLAAAQQQLKARNKMHEMAIRQHLITDQNITANGDLVLSAEERRTLVQEGYSIPQKYPLTKSEEESLKIVRRKIKNKLSAQESRRKRKEYIDALEGRLHCFSEENKSLKKQVHQLEASNRDLQQKLHQYESKEKM
The following text describes a protein:
Function:
Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. May phosphorylate the CDC25 phosphatase stg, which promotes its degradation. This results in increased inhibitory tyrosine phosphorylation of Cdk1-cyclin complexes and consequent inhibition of cell cycle progression.
Subcellular Localization:
Nucleus.
Sequence:
MAATLTEAGTGPAATREFVEGWTLAQTLGEGAYGEVKLLINRQTGEAVAMKMVDLKKHPDAANSVRKEVCIQKMLQDKHILRFFGKRSQGSVEYIFLEYAAGGELFDRIEPDVGMPQHEAQRYFTQLLSGLNYLHQRGIAHRDLKPENLLLDEHDNVKISDFGMATMFRCKGKERLLDKRCGTLPYVAPEVLQKAYHAQPADLWSCGVILVTMLAGELPWDQPSTNCTEFTNWRDNDHWQLQTPWSKLDTLAISLLRKLLATSPGTRLTLEKTLDHKWCNMQFADNERSYDLVDSAAALEICSPKAKRQRLQSSAHLSNGLDDSISRNYCSQPMPTMRSDDDFNVRLGSGRSKEDGGDRQTLAQEARLSYSFSQPALLDDLLLATQMNQTQNASQNYFQRLVRRMTRFFVTTRWDDTIKRLVGTIERLGGYTCKFGDDGVVTVSTVDRNKLRLVFKAHIIEMDGKILVDCRLSKGCGLEFKRRFIKIKNALEDIVLKGPTTWPIAIATNSVP
The following text describes a protein:
Function:
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Sequence:
MLRIGNGYDVHKLVEGRKLMLGGVEVPHTKGVLGHSDGDVLLHAITDAIIGALGLGDIGLHFPDNDENLKDIDSAILLKKINNIMKEKNYKIVNLDSIIVMQKPKLRPYIDSIRDNIAKILEINSELINVKAKTEEKLGFTGDETGVKSYCVVLLEKKKC
The following text describes a protein:
Function:
Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
Subcellular Localization:
Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex.
Sequence:
MARNAGGVCPYFLRGNCRFGERCWNEHPRYGRPSQALPQSSGANDNVGTDGVKDEEEKLLEIIVKDMEIWESSGQWMFSTYSPMKDKPNISGFQDFLPEELRLEYYNCQANNAVQNYINSIQQLLTQWRSRLHELKNINASNKTRLIAELKNVAAQPQPAFGFGVQQLPAFGTSTFPVDNQNSTQAFSFKSTPELSNVPPRSTPAFGNLTSIQGATVPLASNSVGFRNPAASAAAPSFSFKATAASDGFGVPGFSNFGKSFPSSSSDTAPALGFGTAAVPSAMDSGNSLFGQTPSAFGSQAASTPPEIPTTVSSGKQFTPMNELSEEELKQFKAKKFTLGNIPLKPPPLELLSNGLSNVAFK
The following text describes a protein:
Function:
Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MKDSTIGKIRGSKQFIQPYVSCFIYRFGQCISRNPWYFILVFTVLSMTGIYPALVALKQTINDPALSSWSSWVAEDANASPNVAVKQLIMLHSNNSMSDNTFLEDVLDWQRHFDDLLAQNDFPCIQRDETACLTLDPIPEYMNTLENRVYNFSVTDVNTSALDMLSYETGSTNGSTANNDATVRAYVLTYFLLQEHVDTFDRLLHGCSLSSGTKLYTNVMDEAPSTIIAPVVGMMSPTSWSVILTIALFLFTYMHISLVRLHDIKAKFGLTVTVFIQGVTSCLTACSILYFFERSGPIYPFPLVYPVIVVMDMENTFRLIKNVISSVPTKSISIRITEGYLRSFFPTFLSLVSKLVTLLILSFFLHPMVQEYCLFLAAALTIDFILHNSFFLAVLSVDIRRLELQDLLNDCVSKVRFDCWDAWLGYCAEKLWFPWLSDNVGTISIYLGVISAQYIYTHKVYGSWQLKSPDPYFLLSLVGRIGRVLKDRHILPLVKTGWLGQPEIIDLLANGAGVEKGDLTLSMYRPLVGDRLPRTEFQSVYKSLYARRLWRWSTFFYTLLLVDFAVGLLVKILLHGSDDDDQEGLQSLLQDEVLSIYRLPTHHSLDVTRLSITANGAFLLSIGLDRKVVVWNLLQNELLVELDDYKLPEVIKAVALNSLGTYLVVFSVDRFYIYDTQLASIVAKGKFSTPNNVRLTAYWLDTEGNNDEAQRFVAIAGDGHVQSFVMTRDAEKLTLRSDADILIGSMVRKTVSINARVGQRFVSLSDDGVVFVASYVSSKWVFSKLEIQGQTKLAEEKVADICAIAGVDVILLVKDSGIQMVELTTRQEVHTFGISCVKEGTLHAAVSNLRVVKGEYRVSSVSLCFLHKKTGALQYYHYAHDDPEAYSILCYYARQSSLMDLHDPDGPNLEKRISIMQQTVREKFNCGSWAMTTDGLSVFGVRRKTAFSRRWQSSSLRRRRRYSIHRAAVDSYTSLKELATTKSPADNASPDEYWEVWMLSQSDDVSLTRKVPLQDQLLIANAGPSLQLTNHCVAVALGNVINIIGLGGNNFADLFLKSINQGNRVLRRRRRTNSLRNQTTL
The following text describes a protein:
Function:
Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity).
Subcellular Localization:
Mitochondrion outer membrane.
Domain:
Consists mainly of membrane-spanning sided beta-sheets.
Sequence:
MEAETECKVPGVYSETGIPVEDPAPGLNSDVSKKDAPPAVAAPGPGLYFEIGKKARDLLYKDFHTDQKFTLTTYTNNGVVITAASTMKDEAIFSEIQTKLKSNNVMLDVKATSDSQVLTTITTEDLGVSGLKQIVSLPFPYQTAGKAELQYLHDYAGISLGVGLTSKPLVNLSGVFGNKSVAVGADVAVDTSTGDFTKYDAGLTINNSDLAADLTLNNKGDSLTASYYHLVNKESGTAAGAELTHSFSTKENTLSFGMQHALDPLTTVKARYNNHGMVSALIQHEWRPKSFLTLSAEVDTKAIDKASKVGLSLVLKP
The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTTPHRTGASAGPRAGGPRRRRQVQGGAPLPLLVPALIGLAFLVLPLVALLIRAPWASMPELLTSTEVWQALRLSLICATAATVVSMVIGVPLAWLLARVEFPGRGLVRALVTLPLVLPPVVGGVALLMALGRNGVVGQWLDSWFGITLPFTTTGVILAEAFVAMPFLVISVEGTLRAADPRYEEAATTLGASRFTAFRRVTLPLIAPGIAAGAVLAWARALGEFGATITFAGNFPGRTQTMPLAVYLALQSDPEAAVALSLVLLAVSVAVLAGLRDRWMTAS
The following text describes a protein:
Function:
Phosphorylates aspartate, the first 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.
Sequence:
MNKQNRRGLQLQLFPYSRSIAQRDTMRSIADQKTNWVVQKFGGTSIGKFPTNIVNDIVKVFSHDYGKNVAVVCSARSSYTKSEGTTSRLLMACDAAASYDETFQDIVRVIREDHVENASHHIKDAEIRVRLVEQTNDELDQVERYLQASQILGEVSNRTMDLVMSVGEKLSCLFLTALCEDCGVTAEYVDFSSIVPTDFRCAEGSLDNSFYALLVVAFKERLAQIVQANKEGKRIVPVITGFFGLLPMGLLNGVGRGYTDLCAALVAVALNADELQVWKEVDGIFTADPRKVPQARLLETVTPEEAAELTYYGSEVIHPFTMEQVIRAKIPIRIKNVQNPTGDGTVIYADNIAKKGESTPPHPPISVSSSFFEQRKRGATAITTKNDIVVLNIHSNKKTLSHGFLAQIFTILDNYKLIVDLISTSEVHVSMALPVPDSDSQRSLRNAVEELKKLGTVDLIKKMAIVSLVGKQMKHFIGIAGAMFTTLSEQNINIEMISQGANEINISCVIDEKNSVRALQSIHAKLLEPLAPTSSGAVLNGRLEQLKSLDLS
The following text describes a protein:
Function:
Stimulates transcription from the HSP70 promoter.
Subcellular Localization:
Nucleus.
Sequence:
MESKSFSGGQNKEDIGDGADIGEDPENGFTLDEVLRLGGTKQDFIMLAGVNEEEEIIGGDKKGEIDDLEEGELQAFIEKLGIKKLSTDSIDQESSAKQKKEKTEPKDSTVNKSTQITVATNSNKELKKKKSNVVQQNDANRATSKIKGKAVFEFCERTILLIKPGGKWFDHEYTHDFTLHPQNEDEVNKYKSLAEKLYEHDRNLYKNRKELQKGANSAWMKTVVSTGTLGDRMAAMTVLIQDAPVHTLQFVENLVNLVRKKGSKQQNLMALDTIKDLLLSDLLPDNRKLHTFLQHPFDKLEEASSGNRDARDRRLILWFFEDQLKKQVAEFVKVLETLSHDNLVATKAKSLNVAHELLCNKPEEEKSLLVLIVNKLGDPQYKIATKASYLLETLLSKHPNMKTVVCLEIERLLYRPNISEKAQYYGICFLNQIIFSHEESDLANQLITVYFCFFRACVKKKDIDSKILRALLTGVNRAYPYAQTGNEKVKEQLDTLFKILHVVNFNTAVQILMLLFQVMDSQQTVSNRYYGALYRKLLDPGLSQASKQAMFLNLIYKSMKADVVLRRVKAFLKRLLQIACCQKPSFICGTLYLMSEIIRIKPGLKILLQENGENDEEEYFHDLSDDDDDEDDACIDGQKNIKSGPDGKTLASENKPTSASWVHQETLQGIKNSSNYDPFNRNPLFCGADNTSLWELKKLSEHFHPSVALFAKNILEGNPIQYTGDPLQDFTLMRFLDRFVYRNPKAPKVTENNRGYLLHRRKKHYMNEEKLPVNSPAFLEKEETEIPVDEVFFHRYFTKLSKERKKIKRNEDEESVEDVDDDEFEKIIDSFEGDSFYSGTTDVIDFASNLKADGKTEKKKSEADDSDSDWDIDGEDDDEEISLDSMCEEDFEDINDDGNENGGIFMDTENDDCPGKKKAKKKSLKQEDMFASAEEFGDILDENTGSKFDNVGLNAMANRDNASTKQLKWETERDNWVHNKDLKNILKRKRTFSKQKLHKKVKK
The following text describes a protein:
Function:
Probable mannan synthase which consists of a 4-beta-mannosyltransferase activity on mannan using GDP-mannose. The beta-1,4-mannan product is the backbone for galactomannan synthesis by galactomannan galactosyltransferase. Galactomannan is a noncellulosic polysaccharides of plant cell wall.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MIFYLSLGVLFTIYALDLIWLVGVAAVARSAEVASLLRKRSKENSGKREQARLKKKQEKDAKKKELQLQKDTDKERVKAVADIAGVTNAADGGGGTAAAAKAATGGAATSPATAASAPISSARYIRPPAGAVTVPGTGGGGGGAVLGGSPGGSSEFCSTDADSGSSRDNDDGDGSSSTDGDDGLARAEIITGPALAAAGHGGGAAAAAAAAANGTTAITVPDDPWSGCQPPKVLVQLPMYNEEAHAAAIIQACCRIRYPRDRLLIQVLDDSTKEAVRQRVDSAAAACIEEGHPVQVMRRDNRSGFKAGAMVEGLNRVEGLGYEYCAIFDADFSPPADFLEETIPVMHRDRRLAYVQTRWAFSNAGQSFLTWAQKVNLCFHFDVEQRARSYLGWFFNFNGTAGVWRIQSIHDAGGWQSDTVVEDMDLSLRCYLRGWDALYLPHVDNPNELPCTLSSYKTQQFRWLSGPMQILIKSFSNIWHAKDIGIGRRLNAFWFFMRYVLFAAITVGVLAVPPVALWVEVWEWSWPQIYFIVSINFALAVYLYVTPFSIFYLFFSVAIGYFKLWAMISGLLGLEKSKTWKVTQKFGAKQTGGGLLHRIHKPYALETCLALYYGGMAAAAGVYGSWIMVGYCGLMTLVFLAISFGDAYM
The following text describes a protein:
Function:
Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
Sequence:
MSTIGKSVRIERIFNRNTGNAIIIPMDHGVGAGPISGLTNLQEAVNKVAEGGANAVLGHMGLAKHGHRGYGHDVGLIIHLSASTSLALDPNHKVLVTTVEEAIKVGADAVSVHINIGAEDEFEMLQDLGYVAGKCDEWGIPLLAMMYPRGKKVRSEYDVDVVKHAARIGAELGADIVKTNYTGSPETFKEVVSGCPVPVIIAGGPKMGSEKELLEMIEGSLEAGGRGVAIGRNVFQAEDPTGLVRRIAKIVHEGMTTEEVIKLGSNV
The following text describes a protein:
Function:
Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Sequence:
MAEHGAHVASASAGDDDRPSIFEVVAQDSLMTAVRPALQHVAKVVAESDPARYGFLWRWFDELFALLDLLLQRRYLSRAGGSFSENFYGLKRVATGAGPGRPAGGPGLPREQLRRSLLLLVLLPYARLKLEKLASGLRDEDDYSIRPAASRRKRLSRAFLAAYPFAHLAWEGWFLGQQLCYTLGWAERHSPLLGLAGVRLARLTPEDVRARLERAAFCPGVPPPPVRSARDKLLRGLRRAAGAAGSSLSAGLSAAVFFLQFLDWWYAADDQDAVKALTAPPAPPPPVHLDHPADAPLLPKLKTACPLCHKVRVNATALATSGYVFCYRCVYPYVRNHRACPVTGYATEVQHLVKLYAPDG
The following text describes a protein:
Function:
Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Sequence:
MKIFFSGSIRGGNKYRRQYGQILAFLQAFGETISEHSDRPEAFDDGGLKGDAAIYARDTHWIREADLLVAEVSQPSIGVGYEIAYAEARNIPILALYHVGAESPMSAMVFGNPKITSIRYDSLSELWPVLKDTLAETHLPPK
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. DYNC2I1 plays a major role in retrograde ciliary protein trafficking in cilia and flagella. Also requires to maintain a functional transition zone.
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MLARNNRISSPPLGLEGSIDLLKYFHFPSRQMISFLFSRVRSKNYCVLIEIIRFPRYFILVLILQFIDGKDNHVKYLLNKDEDRERRHKRQKEQIRETKDQEKSALREKREGLSREKSSSLPGKDGEEKHKEKQQKERPSFGDDRQRSTMEKKERKAREEPTKKGDLKQDDHRNQGASSKRESGLHSWNIQNSIKTIGKENKDTKKKPSQEDHMSVWTSAQKPASDEADDMEKEDINSENGANDDFDENYEDDFEDYEEDFDDFDDDEEEEEESKEKKEDIPLAKKIEIEEIQRAINAENQRIIHALPLKQVQTEPEREPRMEGKDSPSRGSLCGILMDFVTAKERQVSRNLALKQKKRSTKLLRLIDLDFSISFSILDLPPVNEYDMYIRNFGKRNTKQAYVQCNEDNVEREIQTTEIETSEAWTQHPGESNLVSGGNKNSRDSLVESALVPKVDTQRLSNFLQAACKVIAVLLEEERAAAEPSWNLPPQENTLSISDSCFQLNTDLPFLHNRKVSSLHISEVQRQMLVSVHELPKKPYSDQLDKKFILCIWDIWQPSSPQKILICESKVKCCCFSPFKATLLFAGTMDGSVVVWDLREDSRIHQYLKLKGSDWIFRTSTFSTDGVFTTVNHKSPVQAIEQVSTSVYKKPSCVLSPLSSQEEMSDLLFQIASLDESGILNLWVVVELQKADLAGSQSDLGLIPGGKIKLVHSSVVLLNTSFSPKEDMGLGTVQALNVKFLPSDPNRFIFGTDIGLVRQSARHDLRVCPKFFKPQQKGTRPIRVNAIEFSPFGEPIFLVGCSDGSIRLHQLASEYPLGQWNNSTGGQPITAVQWALTRPAVFFVQDASSTIYIWDLLESDLGPVAKQLLSVDKLTTMKVLAEPGKTNGLLGLALAKESGTVDIQFVKKKWAFPLEDEQKKLHVLLQQSF
The following text describes a protein:
Function:
Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein. Cytoplasmic vesicle, autophagosome. Cytoplasm, cytosol. Nucleus. Chromosome. Note=Is trafficked from tubular ER to growing autophagosomes via its cytosolic LIR motif. Also found in the cytosol, nucleus and chromatin. In response to formation of covalent DNA-protein cross-links (DPCs), localizes to the nuclear periphery, and associates with DNA replication forks.
Domain:
The LIR motif in the cytosol-facing C-terminal region is involved in the interaction with ATG8 proteins; The disordered region is required for autophagosome binding and reticulophagy, probably via bridging the long distance between endoplasmic reticulum and autophagosome membranes, because ribosomes exist on endoplasmic reticulum membranes that attach to autophagic membranes.
Sequence:
MPDLLLLGLIGALTLLLLLTLLAFAGYSGLLTGVTVSAGSPPIRNITVAYKFHVGSYGDTGHLFTESCSISPKLRSIAVYYDNPHTVPPEKCRCAVGSILSEGEESPSPELIHLYQKFGFKIFSFPAPSHVVIATFPYTTPISIWLAARRVHPALDTYIKERKLCAHPRLEIYHQDKIHFMCPLARQGDFYVPEVKETERKCRELAEATDTQTDGTGADTSDASSVSLDVRPGSRETSATTLSPGAGNRGWDDGDNRSEHSYSESGASGSSFEELDLEGEGPLGEPRLNPEAKLLGPPRELSTPERGEE
The following text describes a protein:
Function:
Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Phosphatidylcholine-selective. Regulates root-hair morphogenesis. Contributes to the supply of inorganic phosphorus for cell metabolism and diacylglycerol moieties for galactolipid synthesis in phosphorus-starved roots. Involved in root elongation during phosphate limitation.
Subcellular Localization:
Cytoplasmic vesicle.
Sequence:
MASEQLMSPASGGGRYFQMQPEQFPSMVSSLFSFAPAPTQETNRIFEELPKAVIVSVSRPDAGDISPVLLSYTIECQYKQFKWQLVKKASQVFYLHFALKKRAFIEEIHEKQEQVKEWLQNLGIGDHPPVVQDEDADEVPLHQDESAKNRDVPSSAALPVIRPLGRQQSISVRGKHAMQEYLNHFLGNLDIVNSREVCRFLEVSMLSFSPEYGPKLKEDYIMVKHLPKFSKSDDDSNRCCGCCWFCCCNDNWQKVWGVLKPGFLALLEDPFDAKLLDIIVFDVLPVSNGNDGVDISLAVELKDHNPLRHAFKVTSGNRSIRIRAKNSAKVKDWVASINDAALRPPEGWCHPHRFGSYAPPRGLTDDGSQAQWFVDGGAAFAAIAAAIENAKSEIFICGWWVCPELYLRRPFDPHTSSRLDNLLENKAKQGVQIYILIYKEVALALKINSVYSKRRLLGIHENVRVLRYPDHFSSGVYLWSHHEKLVIVDNQVCFIGGLDLCFGRYDTFEHKVGDNPSVTWPGKDYYNPRESEPNTWEDALKDELERKKHPRMPWHDVHCALWGPPCRDVARHFVQRWNYAKRNKAPYEDSIPLLMPQHHMVIPHYMGRQEESDIESKKEEDSIRGIRRDDSFSSRSSLQDIPLLLPHEPVDQDGSSGGHKENGTNNRNGPFSFRKSKIEPVDGDTPMRGFVDDRNGLDLPVAKRGSNAIDSEWWETQDHDYQVGSPDETGQVGPRTSCRCQIIRSVSQWSAGTSQVEESIHSAYRSLIDKAEHFIYIENQFFISGLSGDDTVKNRVLEALYKRILRAHNEKKIFRVVVVIPLLPGFQGGIDDSGAASVRAIMHWQYRTIYRGHNSILTNLYNTIGVKAHDYISFYGLRAYGKLSEDGPVATSQVYVHSKIMIVDDRAALIGSANINDRSLLGSRDSEIGVLIEDTELVDSRMAGKPWKAGKFSSSLRLSLWSEHLGLRTGEIDQIIDPVSDSTYKEIWMATAKTNTMIYQDVFSCVPNDLIHSRMAFRQSLSYWKEKLGHTTIDLGIAPEKLESYHNGDIKRSDPMDRLKAIKGHLVSFPLDFMCKEDLRPVFNESEYYASPQVFH
The following text describes a protein:
Function:
Transcription factor that acts as a transcriptional activator of a number of genes encoding proteasomal subunits. Plays a role in ergosterol and plasma membrane homeostasis, and subsequent azole resistance. Regulates the expression of 212 genes, activating 80 genes and repressing, likely in an indirect fashion, 132 genes. Targets comprise several proteasome and ergosterol biosynthesis genes, including ERG1, ERG2, ERG3, and ERG11. Directly regulates ERG11 expression through the 3'-TTGCAAA-5' binding motif.
Subcellular Localization:
Nucleus. Note=The localization to the nucleus increases upon fluconazole stress.
Sequence:
MTSIDLGLKRTLTDVLEDELYNMRLREQETAQEQLDLREAGKVRQVQLQQQQMFSQYADPSVTMMSGDVACEGVLSTAPANLLANPDIRQAPAPQAQAQMLQVNPEVLISYANKNSAHMNVSAVDDKLNRGLVDENSYYDDVDYSSMNAKMADWQLDDNVAMLDNNDARLIFDNEFADDDDLSDDENLFDEGLENYHNELVSSNSPIESLDVAEHKESVDDRLRKYHLDNIQNILSKTSTNDKDILQIKLPSDFTTTNLHSTNPSGLIEDPSQLVLGSSKKITEDTHVEEESKNLPDLTELTSATEIEDILLAVDSDDDDLYTKPIAKQTTKKDNSKPVEKTVVEKTSSVTKAGSNHSRSTLARPTAHARKLSSSRKQAPKVYNPKTTTKSTHTHSKNNATHEAFVCELVNSVTNEVCGAQFSRTYDLTRHQNTIHAKKRSIFRCSECIRALGDEGFQKTFSRLDALTRHIKAKHENLSLEERQQVTKYAKSNIGFVTA
The following text describes a protein:
Function:
Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.
Sequence:
MEKDGLQFLNRLRSLNGSSENVCVIGVFGKGSSGSQCNGLILNNLLDKHIFEKYTVFEHVKSEEQVVRSCYIEPYYDKSRHTLYLQLVSIYDGAQLAQLCRLLPQHISTADSHAYWKSHEGQHARLLLYLFTISHIMMVCHPRAVFDTSYVKLFRALQTTREKLSPQLSSSLKGLSVSRQWQTSGRMCTPRLLFVSQQSDLNDVKDTGQGGQTKKKSQRKALQHHLEDQIYRIFRKTHILTNNMSHCLFSIPLNQAFVHILHSHDQLKDTIHELINSCSLTSSSDISDNHQSEKEVFVMPITMETIPSLTDKPDDSLRAFVHQHVDLILNKKGFDDTLRGAAIAHFEYPSMKTWIEVATSSYQLLMNVTDDPKVTSALTYLQTALDQDLRFSEMRCKKILPMASRSYQENASSHYTSTVHRNKLLQAMKMYSQHARGPAYETFADQLQEECELFWQSGRQLCEVISLTGHHCIHKLHLLPSDPELDPPREIVLSHLPHTNNNQTPCACNCGRSVGTREDPFDVKVANYDFFKEMEEKCCSKLHHYEFTVYSPAPARRPSQLTSEGDSIPVNEGVSDQEDEGRTKAVEKIKLSTDTKESQSGVMTPELSLGQSVPNEGSTDQPVIGTAATLSTQDEQPDLEEDKEKEEDTDEDDAGVSEPHYNRPLEGMLCSITPRGMLPSFSSWSLVCLGPSSLYNPTKGLDHPNFMRDSKHLLAWDIPIPKGSVMDAVWPSPSEMVTTSSKKGGRGRDKKDGSSDGLRAYIGNEYECPRGHRFICSGPDKVVKVASGSGGPKESANKLVTLDMPLYYSCPCRANKPPLGQLIRSFIVTPPKPVHIKLNPKVRPGPHPTPVFTPLPGDEGITLTPSSMWVLRYPFVYGSEAGPVMPPADNQPTPGAKLLKGLYLVTLQAPET
The following text describes a protein:
Function:
Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Sequence:
MPILEREPPKGRRESYVLPKVPVPPLKQTLDMYLNCMKHLVKEEQYQKTKAIVVKFGEPGGTGELLQKKLLERSEKTYNWVYDYWLEDMYLNQRLALPVNSNPAMVFPKQNFKDRKDSLRFAAHLITGVLEYKERIDTRVLPVDFARGQLAGTPLCMKQYYRLFNTYRLPGHKRDTLIIHKPGSTEQEHIIVACKNQFFVLDLVVNKKKLKEMDILTQLEKIVKMAENSEERQPPFGLLTSDGRTEWAQAREVLIKDSVNRESLAVIEKCLCVLCLDNPSGMEVGDTSRALLMLHGGGHEKMGANRWYDKPMQFIVGEDGVCGTVCEHSPFEGIVLVACTEYLMKFMTGSPSKMGRATSVSELPTPARLLWKTTPHIQDLLKASAERLQR
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase involved in regulation of abiotic stress responses. Not involved in ubiquitination of MYB108/BOS1. Has no effect on the stability of the DELLA proteins.
Domain:
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.
Sequence:
MAVEARHMNLFSSQYITNRECVKSQTNMNNGQQIAGGGFPVTIGDRNLQYIDPINSFNKSESELTAISKRQRDSTFDSDALIASQKRRAIAFSPASLIDAELVSQIQQQNSEIDRFVAQQTETLRIELEARQRTQTRMLASAVQNAILKKLKAKDEEIIRMGKLNWVLQERVKNLYVENQIWRDLAQTNEATANNLRSNLEQVLAQVDDLDAFRRPLVEEADDAESSCGSCDGGDVTAVVNGGCKRCGELTASVLVLPCRHLCLCTVCGSSALLRTCPVCDMVMTASVHVNMSS
The following text describes a protein:
Function:
May act as a co-chaperone for HSP70. May play a role in ribosomal RNA (rRNA) biogenesis, possibly in the maturation of the 60S subunit. Binds the precursor 45S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Within the nucleus, localizes primarily to the nucleolus.
Sequence:
MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDDSLDLLRYFTVTCYSGYGDDEKGFYTVYRNVFEMIAKEELESVLEEEVDDFPTFGDSQSDYDTVVHPFYAYWQSFCTQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLYCPACDKSFKTEKAMKNHEKSKKHREMVALLKQQLEEEEENFSRPQIDENPLDDNSEEEMEDAPKQKLSKKQKKKKQKPAQNYDDNFNVNGPGEGVKVDPEDTNLNQDSAKELEDSPQENVSVTEIIKPCDDPKSEAKSVPKPKGKKTKDMKKPVRVPAEPQTMSVLISCTTCHSEFPSRNKLFDHLKATGHARAPSSSSLNSATSSQSKKEKRKNR
The following text describes a protein:
Function:
Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Active on laminarin and lichenan.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein. Secreted, cell wall.
Sequence:
MNRKSTLNQKRSATISEFRFITEENTEANALSQQEQQQPQLKQDQSSLQQHKRTQSQTKLTKVLPYKVTRSKSVHAFQEYGKGFVGSPLMNSSIKSSQINSPQSKKLIKKQITPLQPTPPIISPIPIPQQPSTSIAVASEESRLPVPPPPSPPPVPQPPPPIHPSPFISNTIDDDNAQTSLSYSSNLLNYCQESVATPTYPVVATKNSDSGVRNATVIYRKKNTEELDYNLNEISPISYDTNSLRVVKRQSKLSANSKLEAHTLSNDFKLEKDKILSPDLEIVTAKAEDNDDTNIEIKQKNILETPTSFDNNQTPKIVGDNDSYTSPVSTELFSNITRRGFWWIIVILLGIIVILIGGFAPAVFILGKGTKTSVGKYFSDPKNLPMLYLLSSKYLTKVEEPLEHIHKPNSIEGLSEELRQDSEVVSLMSIVTNALFFGVAYSPSNALEPQCGFTRRDAMLDLARLSTITTKIRNYGMHCDQSEFILDAIEYMNLNMTLAMGVWIGSNDTVNEEQMNTMKRIVAKYPNPSELINSIYIGNEVLFREDKTRDELIEYIQDAKTFLQSKGIDDIPVGTSEIGSLVDSPLLQVCDIVGANIHPFFAGVPVEFATIWSLEFLNFQVQPYNEYNTKIVLSEIGWPSGGGTFGSSVASLSNSEYFANDFLCTFRDLPIEYYYFEAFDEPWKEIFWEGNRRWETQWGVFQDDRSPKFALQNIGCV
The following text describes a protein:
Function:
Component of an histone acetyltransferase complex.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MINVGAVTVEAHYSTNYVENYLDSVENLPDEVQRHLSRIREIDVLYRSHLRDVNSYYEQWSLNQAQAAAASSGATKGSTTETTASSTTGPGTTASAEQSNTLKRVTSRIQKSLIAAQELGDEKLQIIQQLQDLIDHKTRQLDQDFVNLGNEFFVRLDYARDDKTLDGGRDVNGTSLAGAAGGNGSSNGPGQYGVTGNGTAGGSNGSGGYGSSGGNGGNGGIGSNSHIMHTANGTSGNGVGSTLGGGNGSGMYGGNNGSGSLSNERSSKRARRTRNEQTGGSANGSNTPNSMCGVSAMDVDPIEDVIGGSGSGVGGSVGSGGSSGSGSGGNGGQSGSIAISGGSGGTNVGGGIKQESGSGGNGSGGNGGASTSGGSHNSLSGSGSGQAQSSTLGGSGAKSGNGGNGGANSSSSGSGSSGNGGNGNGGNGGAGGAGSSSSQLNSSNQGSGKKGTGSGNHTGSGSGAGGANSGKKKKRKTGGRGSQATREAREDTPAAEETIDPDEPTYCLCDQISFGEMILCDNDLCPIEWFHFSCVSLISKPKGRWFCPNCRGDRPNVMKPKAQFLKELERYNKEKEEKT