lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Specifically required during spermatogenesis to promote expression of piRNA precursors. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons, which is essential for the germline integrity. Acts by facilitating transcription elongation at piRNA loci during pachytene.
Subcellular Localization:
Nucleus.
Sequence:
MCSPASPKILYRNPRFLRLAFLQLHHQQQSDVFCDVLLQAEGEAVPAHCCILSAYSPFFTERLERERPAQGRKVVLELGGLKISTLRKLVDFLYTSEMEVSQEEAQDVLSAARQLRVSELESLQLEGGKLVKAPQGRRLNRECLQPTSAAPISARVVTPSHHPHTPLPATRTPCPLGAIRLKSLGKEEGPQENNRQNADNLSGTLLLKRKARACPTPQEKSSSPSSHSQGPRENKNDTALDPTVLSPPSLYPSVDKHLLPRKIRLSRSKPSPDICTSKPSSILSGPSSVPATPGRRLWRQRSVNKEAPEDKLKPGRASPLQTTPSPSGLGKTGGSKKRSPEVRAPNSESAEEGQVGRVKLRKIVNGTCWEVVQEPPLKNSQDSPQIPDPGGDFREPSGTQPFSSNEQEMSSTRIELCQDSPVCTRLQDILVSASHSPDHPVVKSEFGSSPELVEKEPMLAIDCREPYAFDTALLEQPCEAEEYRITSAAATSELEEILDFMLCGSDIEPPIGSLESPGAEGCRTPTYHLTETGKNWMEGEEWCLPDMELWPRELTELEKEPAGENKEPAELLSPLVMPSEVSGEVLSVGGPWTPDLEITSSQPLDGQEDKLLHVSSLDIPQRSYGDLSPPCSNWVETGLEVSLTTDELLYPSPKAGKEVSGHSELLGSLPASSEEEEIDVVDWTAEGRLVPTSVPSVWPDPSSESETEVDILT
The following text describes a protein:
Function:
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Subcellular Localization:
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Domain:
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence:
MNLEVKKIDTANARLSAKLSIENLEKRYDKIAQKIAQKVKIDGFRRGKVPLSLVKTRYQAQIEQDAQEEMIQEVLKNAFKELGIENKDLIGSPNLTKFEKKDTHFEIEADIGLKPTIVLDKIKECVPSVGVEVPNEEKIDERLKQLAKDYAKFVDTNTQRKAQNDDKLTIDFEGFIDNAPFEGGKAENFNLILGSKQMLEDFEKALLGMQAGEEKEFPLTFPSKYHAEHLAGKEAFFKVKLHQIQAREMLEINDELAKIVLANEENATLKLLKERVEGQLFLENKARLYNEELKEKLIENLDEKIVFDLPKTIIEQEMDLLFRNALYSMQAEEVKSLQESQEKAKEKRESFRNDATKSVKITFIIDALAKEEKIGVHDNEVFQTLYYEAMMTGQNPENLIEQYRKNNMLAAVKMAMIEDRVLAYLLDKNLPKEQQEILEKMRPNAQKIQAG
The following text describes a protein:
Function:
DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Subcellular Localization:
Nucleus.
Sequence:
MAWASIQCTRRQLNLDITLRCGQSFRWKKNDEGEWLSTFANKVWVLKQDLEGNILYKVLDGNGTATSSCNDGLSLAKGANRKRKAKNGLSESQAECQLDDHGHLLRDYFQMNVDLEKLYKQWSAADEIFRDVAVALPGVRILRQDPFEALMAFICSSNNNITRISSMVNKLCEMYGTHLLSSSTGSFYAFPTAEQLDRDSVEPELKAAGFGYRARYVRAAARALSRQDPLWLASLREVSYPEAHSQLLQLPGVGPKVADCVCLMALDKADVVPVDVHVWKLAVRHYLPHLSKHKNLTTTAYREIGGFFKERFGPYAGWAHSVSSHTSLW
The following text describes a protein:
Function:
Putative phospholipase.
Sequence:
MSLQSVHSARWIGSDSIEASAAAADVSQNPAQRQAPELLAGHVEYDLGTRTFKFIKAVVNVDKRKPGPDPGPDFSCPNAAAPACGSFSDPARHRSNFGQLRVTTNAAFPDEIQMQAAGFLEGYLTAERIFDYAYNMKAWLFTQTNDSFAVGDWLFAQDKWTRQQVAAHAAAAADTAAADAAATMHSGVGAAAAAGGAGAGAGGAGVVGGERAAGADQQQAQQGQQQEGGEGAGEPHRRAQGSDAPPASASANYWRTIGLLTAQADGLLAGYSARLADMQQQQQQQQATAASSSAASSPASSAPPCDRLTKWDFLMLNALGDMDDLMAIIFPSDRDGGDMDDYDDSAVAAAIAAGGSSTGGGSSSSAAKRRPVRTPNPERDASFFFRPESPEERRQRLRVAAAEAAEAEAGLTGPVPRTRTASWEGLSPGQVRSRIAKSGRCSALIKVTPDLSDILMGHVTWWGYASMLRLYKHYSFRLTSVRPHNSGGGADGGGADGGGGAIDGRISFSSYPGQVSSADDWYLLGSGLVVTETSLDIYDHTRYNASYGTGPGSLLSWQRALAANLLAEDGAGWAELAALHNSGSYNNQYLIVDLNRFSPGQELQPGLLTVMEIIPGLVVTADATSDLERGHWPSYNIPYFPQVYEATGYRRHAAALAARGADYAAAAADLSYQLSPRAKIFRRDAAGATDLASLRALLRSNAFGARPADPLAADSPWEALCGRGDLDPEDPDVYGCYDGKVTNYRRALALSADAINGPTTSGGQRPFAWADHPRFERIPHRGMLEVFDTAWEEQAP
The following text describes a protein:
Function:
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate.
Sequence:
MRVILFDLDGTLIDSAKDIALALEKTLKELGLEEYYPDNVTKYIGGGVRALLEKVLKDKFREEYVEVFRKHYLENPVVYTKPYPEIPYTLEALKSKGFKLAVVSNKLEELSKKILDILNLSGYFDLIVGGDTFGEKKPSPTPVLKTLEILGEEPEKALIVGDTDADIEAGKRAGTKTALALWGYVKLNSQIPDFTLSRPSDLVKLMDNHIVEF
The following text describes a protein:
Function:
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Sequence:
MYHVIAATTNPAKINAIKLAFEQVFGKDTFDIEDINVDSRVPQQPIGNTETRTGARQRVMAARQVRPEADFWVGVEAGIEDDMTFAWIVIEHEQIRGESRSASLMLPEQILKGVREGRELGDEMAFLTKIDNIKQKGGAIGYFTDGLLSRTSVYQQAIVLALVPVTHDIYKQLNKKDDE
The following text describes a protein:
Function:
Proton-sensing G-protein coupled receptor activated by extracellular pH, which is required to monitor pH changes and generate adaptive reactions. Activated by an optimal pH of 7.4 (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (By similarity). GPR65 is mainly coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (By similarity). May also act as a receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids (By similarity). Plays a role in immune response by maintaining lysosome function and regulating T-cell metabolism. Acts as a regulator of inflammation by mediating pH-sensing of extracellular acidification which takes place in inflamed tissues: activation regulates endo-lysosomal function of immune cells and T-cell metabolism. Constitutively active in endosomes and stimulates adenylate cyclase production from endosomes independently from extracellular pH changes (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Note=Internalizes and localizes to early and late endosomes, from where GPR65 signals at steady state, irrespective of extracellular pH. Changes in extracellular pH may relocalize receptor signaling to the cell membrane.
Domain:
A multitude of proton-sensing residues, which include extracellular histidine (His-12, His-16 and His-245) residues or triad of buried acidic residues (Asp-62, Glu-144, Asp-286), contribute to activation of the G-protein coupled receptor activity and pH sensitivity.
Sequence:
MAMNSMCIEEQHHLEHYLFPVVYIIVFIVSVPANIGSLCVSFLQAKKENELGIYLFSLSLSDLLYALTLPLWINYTWNKDNWTFSPTLCKGSVFFTYMNFYSSTAFLTCIALDRYLAVVYPLKFSFLRTRRFAFITSLSIWILESFFNSMLLWKDETSVEYCDSDKSNFTLCYDKYPLEKWQINLNLFRTCMGYAIPLITIMICNHKVYRAVRHNQATENSEKRRIIKLLASITLTFVLCFTPFHVMVLIRCVLERDMNVNDKSGWQTFTVYRVTVALTSLNCVADPILYCFVTETGRADMWNILKLCTRKHNRHQGQKRDILSVSTRDAVELEIID
The following text describes a protein:
Function:
This protein, presumably an aminopeptidase, mediates the conversion of E.coli alkaline phosphatase isozyme 1, to isozymes 2 and 3 by removing, one by one, the two N-terminal arginine residues.
Sequence:
MFSALRHRTAALALGVCFILPVHASSPKPGDFANTQARHIATFFPGRMTGTPAEMLSADYIRQQFQQMGYRSDIRTFNSRYIYTARDNRKSWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPLSDADADANLGGLTLQGMDDNAAGLGVMLELAERLKNTPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSGVKTPEAVRKLTRDRALAIARSHGIAATTNPGLNKNYPKGTGCCNDAEIFDKAGIAVLSVEATNWNLGNKDGYQQRAKTPAFPAGNSWHDVRLDNHQHIDKALPGRIERRCRDVMRIMLPLVKELAKAS
The following text describes a protein:
Function:
Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase GPI14 (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein.
Sequence:
MQSVRQTVLFESEEAWRAGAEQNATAITVHARGGEVVQTRRTWAAAGGPRVRVTWSGGRTVSEVSPQLAAGLSVYVEGGAHVSRDFVQARGQAVFHSAQLELDAVRAWWPRELAVQPEALRWAECAYDIELGRQVRVDEYCALRAGETVALTAAAGGTDEAKVETGVFYPEISDGADVSLSGFRCTWLRDGSGRTDTCQKTLLMYKPAHVHMPEPAVGIELVQPVTLHPVIEVDLSSVSASGPACAHHVFLQLPAQLFVDKFQQPPELLFGEDDLELPEYKVEAWGSEVIYALEPGRVNRVQLHSRYARPGPGRRYEVVPLRPYVFEACDTGSADIAENPFYSKGMGFEAYFTADTVFKHRNSTRLNIPVPRGNSNDFPSIQYVTVLSILFSVLYISYCLFRRPVAASARASG
The following text describes a protein:
Function:
Plays an important role in the elongation step of protein synthesis.
Sequence:
MKYLAAYLLASLSGNANAASVTKILQSVGVEVDAARVESVCKELDGKDVQALIAAGKSKVGSVAAAAAPAAATSAAPAAAAAAPAKKVVEEKKEESDDDMGMGLFD
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:
MSLSGYFSRLLEASGKKSVGSFFASWEFGKMLVDGNLAHNVLVRATGAGRLVGTDYNGNRYYENEEAAYGRRRWIVYKDKFDYNPTTIPPEWHGWLNYINDYNPTNTQFKQPTYQIEASMTKTGTQTCYNPKGSWFSAKPRNWRKYESWTPANKSA
The following text describes a protein:
Function:
Nuclear genome-encoded probable GTPase involved in ribosome biogenesis in chloroplasts. Plays a role in 16S rRNA maturation in plastids and may contribute to the assembly of the small (30S) ribosomal subunit.
Subcellular Localization:
Plastid, chloroplast stroma, chloroplast nucleoid.
Sequence:
MELSARTLKKQAPIMELALRLSPILPPNKLKISTSSYLSRSCSTTNLFRRRIRTSRRRRSEFGFQVKNNTNTVFFLSNDQQLQKKQQHILVSEGEFDDDDEEEEEEEEEETNTLSLSVKPERNMALLDDYELEELDYASDPNHRSGYVAVVGKPNVGKSTLSNQMIGQKLSIVTDKPQTTRHRILGICSGPDYQMVLYDTPGVIQKQMHKLDSMMMKNVRNAAINADCVLVIVDACKVPEKIDEVLEEGVGSLKDKPPILLVLNKKDLIKPGEIAKKLEWYEKFTDVDEVIPVSAKYGHGVEDIKDWILSKLPFGPAYYPKDIVSEHPERFFVAEIVREKIFMQFRNEVPYACQVNVVSYKSRPTAKDFIQMEIVVEKNSQKIIIIGKEGRALKLLATASRLDIEDFLQKKVYLEIEVKVKDNWRQDEGLLNYYGYGGKIRAL
The following text describes a protein:
Function:
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Miscellaneous:
MISCELLANEOUS: Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQKQKTESRVAVYYELTKPKIWYLLVFTAFGAALTASNIYGIEIAPSTWALMLFSVAAGSAAANTLTNYHDRDIDAIMERTKGRPLPSKRIYPAVKARNFGLALAGISLVLAFGISFTTTLEQGLWATAFIAFGLLNNILVYSYALKRNSRTNIILGGLCGGSPPMIGWVAVTMSDLWTMGLAMAGLVFIWIPMHIWALTLHFKDDYNKVNVPMLTAVQSEKTSARAIAGSTVVMVLFSIAPFFITTQSGEEMVGGVYLWTAIASGILMVALSIWVIVKPMEKASWTLFKFSSPYLAVLFIALMVDSAL
The following text describes a protein:
Function:
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Sequence:
MKLSILPLIALATAVVASPAPDANSMKLMNQAKDFGMSVAQGGLKDIAKTLDDEDIPGDSPISLCDAEYEQLLEIKHLSIDPNPPAKGQNLTIEASGYLYEDVEEGAYIEVEVRYGYIRLISQTLDLCEQSEQVDWSCPIKAGDLKLNKQIELPNEIPPGKYVAVARAYTVDDDLITCLLTTVTFPASL
The following text describes a protein:
Function:
Component of the SMC5-SMC6 complex, that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Subcellular Localization:
Nucleus.
Sequence:
MKDNATVITAEEFNQQVIGLDDNFKSHVRAPAEATIDSRALRFLSETALKKSKLFKIDINAFDPDEFVLRFRQVMTAKAPIDTVGNSSEDEEGAAEEIDWCKVGKRLMRYSRRAPTMDLMYGPLEIQQKKRKLTQRVKLEKHESDMKQPELIDNNDIERSQAEMSALIKRISDLLTTEGGTNGINLFQFFINPGSFSQSVENLFCLSFLIRDGKAAIDCDDEEGVEREFPVVYSTEPAGADVIQEDGFTKTQIILELTMQDWQDAIDLYGIESSIIPDRPDVQATPSNTKKSKWH
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in the phosphorylation of the NAD(+)-dependent glutamate dehydrogenase GDH2. When overexpressed, confers hypersensitivity to rapamycin and induces rapid nuclear accumulation of GLN3 to activate the transcription of nitrogen-regulated genes.
Subcellular Localization:
Cytoplasm.
Sequence:
MFTSQRQLRQNGSPMSSSRSSQHSSGTASPISDSPASNRSYGRDLRGLMGIDIPANEPAFNRANSSDTIYFRPKKIYKMEHEHPSRSTLVQLQTRSQPDDVASSQVNPEGGTDDLELGDPCGNQSLYTIGAEYVPDLDFTKLVNEWQKSTEDLYEFRSSATPQVQIKDSGKGNYELWSSPDAILTQNKLRRDSFSQENSDSLSPEDSILSRNLHSKVKPIPLPRNSQQIFTPLSNLEAERRSSYTTSSNNNSITQNNKFSFAKLKYSLPTQSSAVPASFDSNASSLNFLPTTTLSTLSELQISPNDMMDLIQKLPRNFLNLPYTQRKKVIIEHAPSHDYKAMMSLVKKFMLTSSRSNFSLAGFANNASVSQATANDDNINSRNTPNNSNDTYVNTRPLQRSRHGSIASQFLSSFSPSMTSIAKMNSNPLSGSAGGSARPDDKGMEILGHRLGKIIGFGAWGIIRECFDIETGVGRVIKIVKFKGHQNIKKHVLREVAIWRTLKHNRILPLLDWKLDDNYAMYCLTERINDGTLYDLVISWDEFKRSKIPFAERCRLTIFLSLQLLSALKYMHSKTIVHGDIKLENCLLQKEGKKSDWKVFLCDFGMSCHFDEKHVYRNDTFDENLSSGNSHRKRKSIEQTNLIKYPTTNFLPDDRTNDFDASENLKYQFENRKHQPFTPKGMVSSSSHSLKHLNQPSSSSSSNLFHKPASQPQPQHRSPFHGRHKTTDFSNLEPEPSKYIGSLPYASPELLRYSDARRSKSVEMHIYDSPDSSQSEISAASSSSSNLSSLSSSTKASAVTNSGVTTSSPSGSSTDFPCIVSPLGPASDIWALGVMLYTMLVGKLPFNHEFEPRLRSLIKVGEFDRFSLAQVCKFDRKKNEGTIGQGLYDTVIGCLTIDLDKRWKLKRIEEVLQNEMNLSEAIHDNNGS
The following text describes a protein:
Function:
Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by recruiting telomerase to telomeres and increasing its processivity. May play a role in organogenesis.
Subcellular Localization:
Chromosome, telomere. Nucleus.
Sequence:
MAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQVDRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSLGPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGPELPGEPRSPALSGNPQRGIVMVLPSSMSMSHPARPSVLGSKLSGFLPSSWPGPCTF
The following text describes a protein:
Function:
Actin monomer binding protein that accelerates the exchange of ADP for ATP. Regulates the pool of unpolymerized ATP-actin. Key intermediate between actin-depolymerizing factor (ADF)-mediated disassembly and the profilin-based nucleation and elongation machinery.
Domain:
The C-terminal domain (318-476) binds to actin.
Sequence:
MEEDLIKRLEAAVTRLEGISSNGGGVVSLSRGGDFSSAAGIDIASSDPSILAYEDLISQCVGRALTAAEKIGGPVLDVTKIVAEAFASQKELLVRIKQTQKPDLAGLAGFLKPLNDVTMKANAMTEGKRSDFFNHLKAACDSLSALAWIAFTGKDCGMSMPIAHVEESWQMAEFYNNKVLVEYRNKDADHVEWAKALKELYLPGLREYVKSHYPLGPVWNASGKPASAPAKGPPGAPAPPPAPLFSAESSKPSSSSNQKQGMSAVFQQLSSGAVTSGLRKVTDDMKTKNRADRSGAVSAVEKETRTSKPAFSKTGPPKMELQMGRKWAVENQIGKKDLVISECDSKQSVYIYGCKDSVLQIQGKVNNITIDKCTKVGVVFTDVVAAFEIVNCNNVEVQCQGSAPTVSVDNTTGCQLYLNKDSLETAITTAKSSEINVMVPGATPDGDWVEHALPQQYNHVFTEGKFETTPVSHSGA
The following text describes a protein:
Function:
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MMKLSQQGSPAEMSEPALDFSKVESFLDNHPELFEDYLIRKGKHQMSEKWLRRNQLAKTPSSSSADDKSKDCWTNRGDGLQRRASQKELRKSFARSKAINVNRTYDEHVNSRAQEPLTSMRRRALLRKASSLPPTTAHILSALLESRVNIPQYPSTAIDYIYYLKEHNERAFFLELVKDISNELNLTSLCYKILIFVCIMVDADRCSLFLVEGTANKKSLVSKFFDVHAGTTLLPSCSVENSNEVQVPWGKGIIGYVAEHGETVNIPDAYQDRRFSDEIDKLTGYKTKSLLCMPICSSDGEIIGVAQAINKTPGGAPFIEDDEKVMQMYLPFCGIAISNAQLFAASRKEYDRSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCESCSVLLLEDIESPVVKFTKSFELLSPKCSADTENSFKDSVEKSSYSDWLVNNSIAELVASTGLPVNISDAYQDPRFDVEADQFSGFHIRSVLCVPIWNSSHQIIGVAQVLNRIDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANIPLVSELAIADIHFDDFSLDVDAMISAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQLMFAMLTTAGFQEVLSDTEMLALIVGCLCHDLDHRGTNNAFQAKSGSALSQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSQEYSDLMQLLKQSILATDITLHFERRNEFFELVNKGDYNWNVKNHRVIFRSMLMTACDLGAATKPWEISRQVAELVTSEFFEQGDRERLELKLTPSAIFDRNRKDELPRLQLEWIDNICFPLYESLVKISGKLKPMLDSVTTNRGKWEELHQKQSHGKSSSTSYPTPASSPQPAIECLLKT
The following text describes a protein:
Function:
Calcium sensor of the mitochondrial calcium uniporter (MCU) channel, which senses calcium level via its EF-hand domains. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. At low calcium levels, MICU1 occludes the pore of the MCU channel, preventing mitochondrial calcium uptake. At higher calcium levels, calcium-binding to MICU1 and MICU2 induces a conformational change that weakens MCU-MICU1 interactions and moves the MICU1-MICU2 heterodimer away from the pore, allowing calcium permeation through the MCU channel.
Subcellular Localization:
Mitochondrion inner membrane. Mitochondrion intermembrane space.
Sequence:
MAAAAGSCARLAAWGGRLRRGLAASRRALPSPGPLAAAVAGAALAGVGAAWHHSRVNVAARDGSLTVSAQKNVEHGMIGKLSLRKQRFMQFSSLEHEGEYYMTPRDFLFSVMFEQMERKTSVRKLTKKDIEDTLSGIQTAGCGSTFFRDLGDKGLISYTEYLFLLTILTKPHSGFHVAFKMLDTDGNEMIEKREFFKLQKIISKQDDMMTVNTNETGCQEATVKEPEINTTLQMRFFGKRGQRKLHYKEFRRFMENLQTEIQEMEFLQFSKGLSFMRKEDFAEWLLFFTNTENKDIYWKNVREKLSAGESISLDEFKSFCHFTTQLEDFAIAMQMFSLAHRPVRLAEFKRAVKVATGQELSNNILDTVFKIFDLDGDECLSHEEFLGVLKNRMHRGLWVPQHQSIQEYWKCVKKESIKGVKEVWKQAGKETMEKKPQWPHTTRKIHFAKIVWKRCK
The following text describes a protein:
Function:
Key transcription factor required for motile ciliogenesis. Activates genes essential for motile cilia formation and function.
Subcellular Localization:
Nucleus.
Sequence:
MPVLSTAHRLPLSVERDCSREDDSLTNLQWLQDFSILSTDLSSIANSRPPLPRASQGPCSPPAGDTASCQAPRTGKQRSVAVPTAWASLPTPSPSPVQEVDYRTNANIKPPYSYATLICMAMEASQQRKLTLSAIYSWITQNFCYYRHADPSWQNSIRHNLSLNKCFMKVPRGKDEPGKGGFWQMDPRYADMFVNGVLKRRRMPASHLDPPRCNKAIAHHPYLPVSRPSSHHMQHISGGHRQSRRYEKPNPVLPALRAPERQGDALFTPEDPLQGSNFDDLDLQTALISMCWEGDLAASNLNSTLTGTSGMDMNLQDPPMQDNHWYLSTEGQQTWEQVKEEPVVEQWYNETGFVEDVLYECPPWERVETLL
The following text describes a protein:
Function:
Probably involved in transport through the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDDSQAGPSLTAYASRFLANRMGDRGREVQGSQIFRSPSPSSPTHDPFIPSPSLNASHPHLPGSRSPSRSPTRTPPFPGAGIEAIPDIDGTMGASSVGVGLLFDGPEDDDQPKPQESFTQPPVGFGGNKGKERSRIPNPYESSSESEDEDEGEPEMALDEVDTVRRSLLRPHPQQQREPLSERAKKGWLAHQSVFPPSSSSSSDDESDKETESESGDGESRFTNGGQGLYEGGADSSNLYDTRTIPAAYNVATNLEEPLLAEEDGQRESRVPVRLHVYHGRFGHWEKEGLRKYKDSGFLALWLASLIGIIVGLLFVWGSTDPSPDAPRSPPSILPLLPLLLILLIPPLVLPPAFLFLLQKTVRPVLMGTAISIPFSLFVCGWWALGASFETAGLDGVEQGDRWWGTTGLRVGALLLWALAGWFGRLVWLRRKRLERAASVVELSTKLLLSHPPLLLLTPILLGVFAITSIPFLTLLIRLGMIGYWRHPRENTWVFHIRPYAGWLIFLVTLVWVWTWGVIRGVGRVAVAGVIGEWYFHREEHSRQDPVEVTTAAVHRATGSSLGSICLGAGIIAVVRTVGRAASTLKQYTSPKNTRLPSFLSFLHHLAPVFTIIAGVLDQLNGYALVYVGITGDAFWPSARRAVGLAGRRRVGKLLDYTLIKLLLTLSSTAMGLFTATAGYLYMAHSMGNPGYAPLAGMLCGGVPFLAVRAGAGVLTDAADALFICYQIDRELGGQHSEETKGAFLGEQPRGAGAV
The following text describes a protein:
Function:
Probable transcription factor involved in the development of floral organs. B-class protein required for normal development of lodicules and stamens (whorls 2 and 3). May function as a heterodimer with MADS16.
Miscellaneous:
MISCELLANEOUS: Antisense inhibition of MADS4 expression transforms lodicules and stamens into palea/lemma-like and carpel-like organs, respectively; MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
Subcellular Localization:
Nucleus.
Sequence:
MGRGKIEIKRIENSTNRQVTFSKRRAGILKKAREIGVLCDAEVGVVIFSSAGKLSDYCTPKTTSVFPPLSRILEKYQTNSGKILWDEKHKSLSAEIDRVKKENDNMQIELRHMKGEDLNSLQPKELIAIEEALNNGQANLRDKMMDHWRMHKRNEKMLEDEHKMLAFRVHQQEVELSGGIRELELGYHHDDRDFAASMPFTFRVQPSHPNLQQEK
The following text describes a protein:
Function:
Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a sterol precursor.
Subcellular Localization:
Cytoplasm.
Sequence:
MGSHYKIDLENEREEFIKVYSILKNDVFDELPKMKLASNAIDYIKELLNSPTITGGKMYRGLGFLYSLNTLLIAKNNFDNNNNNNNNKNSETSQHEARIIGWCLEFLSFFLITDDIMDNGLTRRGELCWYRHPSPFNPTEHKVGMLAINDSVLIESFLFFILKKYFKNKSYYVDLFELFHESIFYTATGQLLDSSSFHLKRGDFTNFTFENYSQICINKSSHHVFYLQIKIAILLTDIMDNNEKQKDDTTCKEEKDKEKEQEEELIKNICFNLGIYGQAQDDYFDCFGDPKVIGKTGTDIQENKCSWLICKANTICNNDQLNQLKKNYGNDNENDVSIVKSIFKEINIPKHYENFENEQYNSILKEIQKLSIISLPKSEILLFLLKKLFKRSK
The following text describes a protein:
Function:
Involved in the arabitol catabolism via the arabitol phosphate route. Catalyzes only the transformation of D-arabitol 1-phosphate (Arb1P) and D-arabitol 5-phosphate (Arb5P) into D-xylulose 5-phosphate (Xlu5P) and ribulose 5-phosphate, respectively. It can use both NAD and NADP.
Sequence:
MSKTMKGVSKQAPGYDQMAFIDLSVPEATDDKVLIKVAYTGICGSDIHTFKGEYKNPTTPVVLGHEFSGQVVEVGANVPKVKVGDRVTSETTFYVCGECDYCKEKQYNLCPHRKGIGTQQNGSMANYVLAREESIHLLPDHLSYEGAAMSEPLACCVHAMYQKSHLELKDTIIIMGPGPIGLYLLQIAKEIGAFVIMTGITKDAHRLALAKKLGADVIVDTMKEDLAKVVNEITDGYGVDKVYDASGAVPAVNASLPLIRKQGQFIQVGLFANKMVDLDTESIIQREIEYIGSRSQNPYDWPIAIHLLAKGAINIDEMITKKYPLTEWREAFDKVMEGNEIKVMIESNPEEF
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MAESETDCDTPGLDTLGSECVIAHTQVGDLHYGAETEIMTQEDKRLDLEAIHGDLGAVTCVDVVTETDHDYIKSEIHHDHHQYFSSAEIKGNEHLLGEVLLKTEIGGGDHIVKVESDHGGELTVESENGVIIHEAHGLQCSECGEIFGCMSDLHEHFEIHKATHPYICVHCGESFAIEASLRSHMRIHMKEKSYTTGLEMVGKGVIDAFSLKPHQMMHSPEKPHRCSECGKSFAAAITLREHMKMHSDDKPYKCTQCRKSFMRRRHLKKHQELHARDKPFTCLQCGKGFTTASNLKQHQKTHAGDKPHRCTQCGKCFAAAATLREHQRIHSGEKPYKCTQCRKSFVRKRHLKKHQLVHQGGKPYRCSQCDKGFNHSSSLSRHHKVHLEAKMYAQADKDFPFDTTLKRGMHTGEKPYSCNHCEKSFNHSSSLSRHQRTHSDGKSYTCAQCGKRFNHPSSLARHQRVHLEDKSTYSAIATGKGFPHTTILKQRILQSEKPYRCAQCGKGFNHSSSLSRHHRIHIDQ
The following text describes a protein:
Function:
Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular Localization:
Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasm, cytoskeleton.
Sequence:
MVREQYTTATEGICIERPENQYVYKIGIYGWRKRCLYLFVLLLLVILVVNLALTIWILKVMWFSPAGMGHLRVTKDGLRLEGESEFLFPLYAKEIHSRVDSSLLLQSTQNVTVNARNSEEEVTGRLKVGPKMVEVQNQQFQINSNDGKPLFTVDEKEVVVGTDKLRVTGPEGALFEHSVETPLVRADPFQDLRLESPTRSLSMDAPRGVHIQAHAGKIEALSQMDILFHSSDGMLVLDAETVCLPKLVQGTWGPSGSSQSLYEICVCPDGKLYLSVAGVSTTCQEHSHICL
The following text describes a protein:
Function:
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Sequence:
MTSMENDLYEAEQLPAAFVTGIRFNVSNDRDNEKMSVMEIAAPSEVSDPKLGFPNFSNHCTTCGAADMKHCEGHFGVINFPYAILHPYFLSEVVQILNKICPGCKSVRKDLRIKGANSVSKVNQRKGCKYCVGNSIDWYPPMNFKISSKDLFRKSAIIVEVSEKSSMKVRKRGKQALPSDYWDFIPKDEQQEESLIRPNRRVLSHSQVRYLLKDVDPEFIKKFVLSMDSIFLNCFPVTPNSHRVTEIMHASSNGQRLIFDQRTRVYKKLADFRGIANELSSHVLECLKISKLHLEKPSNEESALVLAQKRNKDSASNMSGLRYMKDVILGKRNDHCFRMVLTGNPNLKLSEISIPCHVAERLQIAEQLNNWNEERLKACCDLRLLEKGEIHVRREGRLVRIRHNEKLQVGDTIFRPLNNGDIILINRPPSIHQHSLIALSVKVLPVSSVVSINPLICSPFRGDFDGDCLHGYVPQSIKARVELIELVSLNRQLINGQSGRNLLSLSHDSLTAAYLVKEDGVLLNLFQMQQLEMFCPNHSPFPAIVKAPLLRSSVWTGKQLLSMLFPLEFDYDFTPNDVVIRNGELISSSEGSTWLRDADGNLFQSLIKHYQGKVLDFLYAAQEVLCEWLSMRGLSVSLSDLYLSSDSNSQKNMMDEIFCGLQEIEQTCNFKQLMVDSNHDFLVGHDEEVDSFMALDVEQMCYEKQRSAALSQASVDSFKQVFRDIQNLLYKYANKDNSLLTMFKAGSKGNLLKLVQHSLCLGLQHSLVPLSFRFPHQLSCAAWNNQKSHGLTQKVDDTAESAKNYIPYAVVESSFMTGLNPLESFVHSVTSRDSSFSDNADLPGTLSRRLMFFMRDLYTAYDGTVRNSYGDLVVQFCYDIDKDASSPTSCAHGLISESSTIPEGIGGQPVGSLSACAISEAAYSALDQPVSLLETSPLLNLKRVVECGSKRSNADQTMTLFLSNKLGRKRHGSEYAALEVKNHLERLTFSDIVTTVSIIFSPQMYRENHFTPWVCHFHVCKDTMKRRQLKVQSIIDSLHMHCTTAKTMWKISLPDMQITSNGRACSHIDMPNEDDTFCITVTIVEYSKSSHMELDVIRDMVIPYLLEAVIKGFPEIKKVDILWKDRLKVSKPHKSSCGELYLRVFVSGDFGITKLWGVLMNDCLQIMDMIDWTRSHPDNINQLCLAYGIDAGWKFFLNNLKSAISDTGKTILNEHLLVVANCLSATGEFVGLNSKGLRQQREHAYVSSPFMQACFSNPSASFVKAAKTGASDDLQGTIDALAWGRIPHIGTGGQFDIIYSVKDQRLAEPVDVYKLLGSSISSQKQDVEFEVPKALNFKSEKYGSLLIDALGDSASEELKKIETKRRSIWRELLTLDDIQRLSRALRNILHKYPIDHRLSEADWNTLMMALYFHPRRDEKIGSGAQEIKVGYHPEHANARCFSLVRTDGTIVDFSYHKCVLGALEIIAPHRAKSYKSKWLQSGSL