lhallee/plat_data huggingface dataset:
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; 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 and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MVQPFVSAPKKDATKQASPTLALDIFLDNQHQSYFEELYRLLPPVCRQIILHALWSHHPLRTVDVKLLLQMDVHAPLEECDEVMRPAIDRKVLHPMHYKKQRMQWSLNDSFKKGLRNALTGLGTSNSFGVPFERHQATDLDLPSEDELVAYGEDTFESILKYMVSSGLGTEFSGSRPQPEVLQLLHTSGLMTDSVDMNGRNPNINRLTITSKGFQFLLEKRQTQLWEILMYYLSAKEANSERSSEVLSMFFSLGCMQLGQDYSASNSFPGAQEALDDLAQYGFIYKSSPDSDQFWPTHLATSLCSGDASAIQSQSADDKRFLILETNYKIYAYTSNELEIAILNLFVDIRIRYPNLVVGKLDRQHVKAAMEKGISARQIIAYLSSHAHPQMYNSPPPLLHPTIVDQLYLWDRERNRLQTEETVMYEFFSKELFDDTVNEAKANAALQHAAISQKLLFIEPHTKPAITEFVKQRQNVLRGGY
The following text describes a protein:
Function:
After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MPLPPPSSSSSSSSASSSAVYHPLHPLQGHHHSQSPILSTGQSTDDQTEMGSFQRFIKYGGWRRNSLLVILIIITFSYSIIFRLRNSPPPSSSSSDLISLANDPNCRPPPGHPSHRYALMIDAGSTGSRIHVYRFSYCLPASSTSSSSSGSILPKLENELFFKTQPGLSSYAGRPIDAAESLRPLLQAALDGVPLEQRSCTPISVKATAGLRLLGDSQSKEILDEVSRWLRASWPFKLSPSGAVSIMDGADEGVYAWVTINYLLKTIGPIPAGQKRNTTAAVMDLGGASTQIVFEPERTKLESGGHVYELAFGGKTHALYQHSHLGYGLMEARRAVHQMVGYSELWRRKIEWSELASLGPLGNPCLQPHTSRKVSLVPSASPSSPESTLPQIVEFVGSAGGFAACRRVVELVIGKDAVCKLKPCAFAGVYQPSFAEAFADGPIYALSYFYDRLSPLGIKESFTLSELEQLIEPICSRTVSDGGRFEREIARLRTAARAKKGPSNLSDLDLQTILAELDDRPETCLDLSFIYAILDLGYQLDHHRPIIISKKITAIELGWALGATIDLLEKTPFDDCPKS
The following text describes a protein:
Function:
Binds to zinc finger protein TNFAIP3 and inhibits NF-kappa-B activation induced by tumor necrosis factor, Toll-like receptor 4 (TLR4), interleukin-1 and 12-O-tetradecanoylphorbol-13-acetate. Overexpression inhibits NF-kappa-B-dependent gene expression in response to lipopolysaccharide at a level downstream of TRAF6 and upstream of IKBKB. NF-kappa-B inhibition is independent of TNFAIP3 binding.
Sequence:
MAHFVQGTSRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMYCPPCNCGLVFHLQDPWVPTGPGAVQKQREHPPDYQWYALDQLPPDVQHKANGLSSVKKVHP
The following text describes a protein:
Function:
Freestanding tRNA editing subunit of threonine--tRNA ligase, the catalytic subunit is AC Q97VW8. Deacylates (edits) mischarged L-seryl-tRNA(Thr) in trans, removing L-serine, has no aminoacylation activity. In vitro when both subunits are present, or if the 2 subunits are fused, L-seryl-tRNA(Thr) is no longer produced. Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr). Editing is probably catalyzed by the 2'-OH of A76 of tRNA(Thr) (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MIILFIHASDFSFNVKERAIKEPEEAKLKSIELKNTLVCFTTVEKGDDEEILSKAIDDILDVYSKVKADSVVIYPYAHLSSNLANPDTAIKILESLENLLKDKVKVYRAPFGWYKAFSISCYGHPLSELSRRIRKTEELEKSEELKYCEKFGFPSSSESAFMRRATIGYLRNLFQPLFESENNENVRDGEMSILYQNVESGRILPCINENPRIVVVYGGVRELNFPKEINDSKNRIRVWWVNESKIYVDVGRLIYYFILESVKQQPPTLPDWLNPIQVRLLPVKKDFLDFSIQVAERLRKEGIRVNIDDLDDSLGNKIRRAGTDWIPFVIVIGEREVKTNTLTVKIRARNEQKSMTVEELVKEIKDEVKERQNLPLYYTLYRHKNN
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of Cox2 and heme A of Cox1 to the active site in Cox1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MFSRVALRAAPRQQPFSLVARRTFQTTRAQLSSPYHYPEGPRSNLPFNPKTRFFWFRYLMYCVVGFGSPVAIAVWQTYRPRS
The following text describes a protein:
Function:
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular Localization:
Nucleus.
Sequence:
MVKLTLRGRQLVGGFYGAEKRQSEKNYFPLQKLMIMSSYLMDSNYIDPKFPPCEEYSQNNYIPDHSPEYYSRTREPSFQHHHQELYPPPPPPPPPPPPPPPPPPPPRPSYPERQYSCASLQGPGNPSVHPRGHGPPPGGHHLPEKPPQPQLCDQTALPSAATSPSPAPPACNQQNPDHPSSTASKQPIVYPWMKKIHVSTVNPNYTGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRIEIAHSLCLSERQIKIWFQNRRMKWKKDHRLPNTKVRSTAPANSSTGSLPAAPSNASEDHSQSSSQEARAEDITRL
The following text describes a protein:
Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Sequence:
MVKAVAVLSSSEGVSGTIFFTQEGDGPTTVTGNISGLEPGLHGFHVHALGDTTNGCMSTGPHFNPAGKEHGAPEDENRHAGDLGNVTVGDDGCVSFSIIDKQIPLTGPLSIIGRAVVVHADPDDLGKGGHELSKTTGNAGGRVACGIIGLARGIGAQEKPVQYQKPSDCIDRCHGCTVNQCTAGLCVCGCALPLEELYAIKQEKPVQCRKPEECVSRCNGCTANKCTAGLCVCVC
The following text describes a protein:
Function:
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=N-terminal lies in the periplasmic space.
Sequence:
MNTIFSARIMKRLALTTALCTAFISAAHADDLNIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWFG
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MRWAYCYLLALHYTIGIQWLYMSRFADEGTKRSRITCPKSEKFLAKQQQEFCRQTQQHANLLAETSNDVVELCEQAFQFKRWNCSSVRLAPRFKRDLTKGTREQSFVYSLSSSVFLLNLERYCHLGQIIEGCRCAKRWHESDDTRIFNAKSNDVERCNSIRYVGKISRSFTDSSLKVIQHRIISSINSSNDSTNFASKIKLKSNSRKTLSAVEVQTRLHNTAVGRKIITKSLAKYCRCHGTSGSCNVKVCWMAFNMTRDRLLHVLVKKYYQAIRVRGSKNINSIMIKHKNGNNNNNNNNNNNNGRMISSSQESFSNNLIYSAISSDYCLPDKYLGSSGTYGRECHLEPKKQGHCDVMCCGRGFRNETRSRGVKCHCKYYWCCYVKCKTCVQDVLVHFCK
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 matrix. Nucleus speckle. Nucleus, nucleoplasm.
Sequence:
MPARALLPRRMGHRTLASAPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQPGRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLPWLQQLREASYEEAHKALCALPGVGTKVADCICLMALDKPQAVPVDVHIWQIAQRDYSWHPTTSQAKGPSPQSNKELGNFFRSLWGPHAGWAQAVLFSADLHQSHRAQEPPAKRRKGSKGLEV
The following text describes a protein:
Function:
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Sequence:
MNRITAYIRQSLQDIYPPEEVKALSMLICCDMLGVDALDIYMGKDIILSACKQRELENIIFRLQKNEPIQYIRGYAEFCGRNFRVAPGVLIPRPETAELVDLIVKENPDARRLLDIGTGSGCIAISLDKNLPDAKVDAWDISEEALAIARKNNEELDAQVTFRRQDVFSADGIQGTSYDIIVSNPPYVTETEKTEMEANVLDWEPELALFVPDEDPLRFYRRIAELGRELLRPGGKLYFEINQAYGQDMIRMIEMNQYRDVRVIKDIFGKDRILTANR
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MRVQGWDPAVAETSGGVLVGVQLAAPGSLLRVAAPQPSAGSRAGSREALEEASWPSCKEGRPAVREAVEGSAEPLGPTSQAPGRAQGPMEAAEAPMAPLQAPVTFKDVVVTFTREEWELLDLAQRTLYWKVMLDTCRLLASLGSPAPTRELTSLPEPAQEPQAVEGGLSQSTSSGGKAEFKTTQPTASQPALLEGCSLHRSLTQEDSRVSMLGQAREQEEPSEKQEEHLRTGLVPLKETPLGKMSPECDDLGTGDSVCSNDFQELASPGDTLHECESHGSRKDPLIHRGKNSYKCKDCGKGFTKNRLLLRHQRIHTKVKLYKCRKCGKAFLKKADLTEHYSIHIGEKPYECIECGRAFSRRSHLTEHQRIHSGEKPFECMECGKAFSRRSHLTEHQRIHSGEKPYVCSECGKAFAHPSDFIRHNRTHTGEKPFECKECGKAFCDSSSVTRHMRCHSKEKPYECSECGKTYSYSSTLTTHQKIHRGVKSYKCKRCGKAFYQKGGLSQHQRTHIGDRPF
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination of cd86 and MHC class II proteins, such as hla-dr alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies.
Subcellular Localization:
Cytoplasmic vesicle membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Sequence:
MPLQQISVVPAQESTGNGRSSLGKNKEKRKERENGKSPGCSASRSNNISKARSTATGTTPRSHSQSSVCPSTQDICRICHCEGDEENPLITPCLCTGTLRFVHQTCLHQWIKSSDTRCCELCKYDFVMETKLKPLRKWEKLQMTKSEKSKIVCSVTFHIIALTCVMWSLYVLIDRTAEEIKQGSENGVLEWPFWTKLMVVAIGFTGGLIFMYVQCKVYIQLWRRLKAYNRVIFVQNCPNKSKKLEDRDYTSNQNSNLKESVAVPVLQTSTIMQSCSAADAPESMAV
The following text describes a protein:
Function:
Involved in chlorophyll b degradation. Belongs to the chlorophyll catabolic enzymes (CCEs).
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MTTLTKIQVYPQVLEHRLFFRDPIRVGSRLTCRERSNRVYVHRCEKKVERKRKVEKFKGNGSWDSLKSGFLGFSKLGFLSKDEYNQKVENLEMVFSSVAVQIARYIVTMTSTGAILLIGFQLSGGDSSMNSLVWYSWLGGIIIGTMTGANMVLEDHYRAGPRNVVITGSTRGLGKALAREFLLSGDRVIVTSRSSESVDMTVKELEQNLKEIMSNASESARKKLSDAKVVGIACDVCKPEDVEKLSNFAVKELGSINIWINNAGTNKGFRPLLEFTEEDITQIVSTNLIGSILCTRGAMDVMSRQHSGGHIFNMDGAGSGGSSTPLTAVYGSTKCGLRQFHGSIVKESQKTNVGLHTASPGMVLTELLLSGSSIKNKQMFNIICELPETVARTLVPRMRVVKGSGKAVNYLTPPRILLAIVTSWLRRGRWFDDQGRALYAAEADRLRNWAENRTRLSLTDAMEMYTENTWVSVFSLSVVCAFIILQSTTPSSFPGT
The following text describes a protein:
Function:
May act as a carbohydrate transporter. Required for male fertility and seed yield.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MARRDQLVSFLCFFLIVSAVAGGLCVSATVLPMRVGKQYVVGGRSGWRTPPPASVDLYAKWAAGIRFYVADSIEFVYKNDSVVKVDKFGYYHCNATAAAANDGSVLFLLDAPGFAYFSSADADHCKKGQRLMINVDSAPSPSPSPSPAPQEAATASAATSSSAATAAHALLLAAMAMMGLILGEW
The following text describes a protein:
Function:
DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
Subcellular Localization:
Cytoplasm, nucleoid.
Sequence:
MEYQDYYKILGVSRDATADEIKKSYRKLARKYHPDVSSEPNAEEKFKQVKEAYEVLKDVEKRKAYDAIGSGWKQGQGFTPPPGWESRPGGEGVRPEFREGFSDFFESLFGGLGQEARWTRQEFKQRGQDQHSRVTVSLEEAFNGSTRLLTLQEPIVDYQTGQVTSKTRQLRIKIPAGVTEGQQIRLQGQGLPGIGGAPNGDLYLEIHLAPHSLFTVEGKDVYLNLPVTPWEAALGAKVSIPTLGGSVDLTLPPGSQTGQKLRLKGRGLPGGTPGDQYVLIKIYIPEPKNDQQKELYQQMAEQMPFDPRKELLG
The following text describes a protein:
Function:
Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids (By similarity).
Subcellular Localization:
Cytoplasm. Lysosome.
Sequence:
MDKQLADTFTQLSQQNGVVGYCCVDESGLCLKAHGNKQSSNAGFYKSLLDKSKFLTQSGEPANIVIETDTANIFIQQNDKITLSVSKLP
The following text describes a protein:
Function:
ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MSSNIFKRFKSAEESLDEDESVTPVYIPKAKRAKLEALKAKKSQIASRLSTHKQQSAPTTTTNTSTTASTTTTATTNNTNNSKPSIQTKKPTGKKFQFDWDVEEEDTASGFVPLIEMDEEIDDPLFSGQESTHWTNKNLEEMTDRDWRIFKEDYNITTKGKNIPNPLRYWNEGSINDKLVSIISQLGYEEPTSVQRASIPLALKKRDVVGVAETGSGKTLAFLIPVLNYILSIDENYLKYEKISNEPVGLILAPTRELALQITKEAEKFCKKLGYQVLPIIGGHHYQDTINKIDQTGVHLIVATPGRLVDSIERKIVDLSKCYCLVMDEADRMIDMGFEKDLNKVLDKLPTEKQLSSTIDGRIFHLEKRSTMMFTATISPTVEKLTKKYLIDPGYLYIGGAGEALDNISQSFEFLSSATTEATKFNKLIKIIRSHWRVTENPLIIIFANFKHVCDSLSQELSSNDINNVVIHGSKSQDMREQAITNFRNHESEVLIATDVAARGIDIPNVTLVINYQMVKKFDEYIHRIGRTGRAGNLGESFTFISDQDTEIFTPLKKFLKKGGKRLPDWLYKHQSQTVQE
The following text describes a protein:
Function:
May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides to prevent their incorporation into DNA, is unclear. Through the hydrolysis of thioguanosine triphosphates may participate in the catabolism of thiopurine drugs. May also have a role in DNA synthesis and cell cycle progression by stabilizing PCNA. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Sequence:
MTSGAEPRVRRPGVGIGVVVTSCRHPRCVLLGKRKGSFGAGSFQLPGGHLEFGPVGWAGGGWGTLEEAALHLKNVRFASVVNSFIEGENYHYVTVLMKGEVDTTHDSEPKNVEPEKNESWEWVPWEDFPPLDQLFWGLRCLKEQGYDPFKEDLDHLVGYKGNHLEVNKKIP
The following text describes a protein:
Function:
Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1. Enhances phosphorylation and proteolytic turnover of the NOTCH intracellular domain in the nucleus through interaction with CDK8. Binds to CREBBP/CBP which promotes nucleosome acetylation at NOTCH enhancers and activates transcription. Induces phosphorylation and localization of CREBBP to nuclear foci. Plays a role in hematopoietic development by regulating NOTCH-mediated lymphoid cell fate decisions.
Subcellular Localization:
Nucleus speckle. Note=Nuclear, in a punctate manner.
Domain:
The C-terminal region is required for transcriptional activation.
Sequence:
MVLPTCPMAEFALPRHSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQAKAKRAGKHRQPPAAATAPVAAPAPASAPAAARLDAADGPEHGRPVAHLHDTVKRSLDSAASPQNGDQPNGYGDLFPGHKKTRREAPLGVSVSANGLPPASPLGQPDKPSGGDTLQTAGKHSLGLDPINKKCLADSGIHLNGGSNSSEPFPLSLSKELKQEPVDDLPCMIAGAGGSVAQSNLMPDLNLNEQEWKELIEELNRSVPDEDMKDLFTEDFEEKKDPEPPGSATQTPLAQDINIKTEFSPAAFEQEQLGSPQVRAGSAGQTFLGASSAPVGTDSPSLGSSQTLFHTTSQPGVDNSSPNLMPASAQAQSAQRALTSVVLPSQGPGGASELSSAHQLQQIAAKQKREQMLQNPQQAAPAPGPGQLATWQQAGPSHSPLDVPYPMEKPASPSGYKQDFTNSKLLMMPGVNKSSPRPGGPYLQPSHSNLLSHQSPSNLNQNPVNNQGSVLDYGNTKPLSHYKADCGQGGPGSGQNKPALMAYLPQQLPHLSNEQNSLFLMKPKSGNMPFRSLVPPGQEQNPSSVPVAAPAASVGTQPTVSVASTHNSSPYLSSQQQAAVMKQHQLLLDQQKQREQQQQQLQQQQFLQRQHLLAEQEKQQFQRHLTRPPPQYQDPTQSTFPQQVGQFTGPSAAVPGMNNLGPSNSSCPRVFPQPGTLMSMGPGHAPVSSLPSSSGQQDRGVAQFTGSQSLPQNSLYGMASGLAQIVAQPPPQATSTHAHIPRQTNVGQNASTSAAYGQNSLGSASLSQQHSKGTLPPGLTKPQVPRVSAAMGSQNASWQHQGMPNLSSQTSGNSSVNPFTAAPSFHIQQAHLKLAGQQFSQAMPSRPMAPLSSAGAAGPMLPPVSAQQRNSAPASAPPQAAPQQGLPGLSPSGPELGAFGQSPTSQMSGRPGLHCAQAYPVRTMGQELPFAYSGQPGSSGLSSVAGHTDLIDSLLKNRTSEEWINELDDLLGSQ
The following text describes a protein:
Function:
Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways including fatty acid elongation.
Sequence:
MAEPYQMNGILNGMPNLRHPSSPSERSTNSVKRLMVTRQYTGVLVANNGMAAVKFMGSIRIWALETFGTEKAILLVAMETPEDLRINAEHIRIADQFVEVPGGTNNNNYANVRLIVEIAERTRVSAVWPGWGHASENPELPDALNEKGIIFLGPPSAAMAALGDKIGSSLIAQAAGVPTLPWSGSHVKVPPESCHSIPEEIYKNACVSTTEEAVASCQVVGYPAMIKASWGEERLVHNDDEVRALFKQVQGEVPGSPIFIMKVASQSRHLEVQLLCDKHGNVAALHSRDCSVQRRHQKIIEEGPITVAAPDTVKELEQAARWLAKCVQYAGAATVEYLYSMETGEYYFLELNPRLQVEHPVTEWIAQVNLPAAQVAVGMGIPLYNSRRFYGMDHGGGYHDWRKISAVATKFDLDKAQSVRPKGHCVAVRVTSEDPDDGFKPTSGRVESGGAIHEFSDSQFGHVFAFGESRSLAIANMVLGLKEVQIRGETVDLLNATEYRENKIHTGWLDSRIAMRVRAERPPWYLSVVGGALYEASSRSSSVVTDYVGYLSKGHIPPKHISLVNLSVTLNIEGNKYTIETVRGGPRSYKLRMNGSEIEAEIHSLRDGGLLMQLDGNSHVIYAETEAAGTRLLINGRTCLLQKEHDPSKLLADTPCKLLRFLVADGSHVDADTPYAEVEVMKMCMPLLLPASGVIHFANDLIARLDLDDPSSVRRAEPFHGSFPKLGPPTAISGKVHQKFAASVNSAHMILAGYEHNINDVVQDLLNCLDSPELPFLQWQELMSVLATRLPKDLRNELDGKYKEYELNPDFCKSKDFPAKQLRCVIEANLAYCSEKDRITNERLVEPLMSLVKSYEGGRESHARVVVKSLFEEYLSSDVIERLRLQHAKDLEKVVYIVFSHQGVRSKNKLILRLMEALVYPNPSAYRDQLIRFSALNHSSYSKLALKASQLLEHTKLSELRTSIARSLSELEMFTEEGERLSTPRRKMAINERMEDLVEDALVALFDHSDPTLQRRVVETYVRRLYQPYLVSGRIPGTNKWHRAGLIAVWEFSEEHLKQRIGQVENPIEKRWGIMVVIKSLQFLATAIDVALKETSQYRVGAGSVSDGNYVNSNQSNMLHIALVGIYNQMSTLQDSADEDQAQERVDKLSKILKDNTITSHLNGVSVKVVSCIIQRDEGRPPMRHYFQWSEKVNLEGYNEVKYTPSCDRQWHIYTLIKNKKDQRLNDQRMFLRTIVRQPSATNGFLSGNIDNEVGRAQASSSFTSNSILRSLMGALEEIELHAHSETVRSGHSHMYLCLLREQQLHELIPFSRMTEEIDQDEGTACTLLKHMVLNLYEHVGGRTHRLSVCQWEVKLWLVCDGQASGAWRVVVTNVTGHTCTIDKMLCMLSSFDHLLLEVEDPSTHQLLYHSATATAGPLHGVALNEPYKPLDAIDLAFETALKRSWKSSSYAVSEANEHNQLYAEVKELIFVDSDGAWGTHWFHLNVLQLSTLEFPSGREIIVVANDVTFKAGSFGPREDAFFDAVTNLACDRKLPLIYLAATAGARLGVAEEIKSCFHVGWSDDESPERGFQYIYLTTQDYSRLSSSIIAHELQLENGETRWVVDTIVARRDLNREELPLFILANWRGFSGGQRDLFEGILQPGSTIVENLRTYKQPAFVYIPMGGELRGGAWVVVDSKINPDHIEMYMKKQNASILEMETTRRSMTIRMKQLMPIYTQVATRFAELHDTSARMAAKGVIGKVVDWEESRAFFYKRLLRRVAEGALAKEVKEAASEQLSHRSALDSIKKWYLVSKGTEGGSEMWNDDESFFAWKDDPKNYENYLDELNAERVSNWFSHLAESSDVKALPNGLSLLLNKMDPLKRKQVIDGLRQLLG
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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 turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MFRQASRLVSRSITAKSTTNRAFSTEVPSTIDSSFVEAWKKVAPNMDPPQTPSSFMKPRPSTASSIPTKLTVNFVLPYASELSGKEVDMVIIPATTGQMGVLPGHVPTIAELKPGIMSVHEGTDIKKYFVSSGFAFLHANSVADIIAVEAVPLENIDASQVQKGLAEFTQKLASATTDLEKAEAQIGVEVHSAMNAALSG
The following text describes a protein:
Function:
Required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. Acts as a positive regulator of PS1 in male sporogenesis. Not involved in female meiosis.
Miscellaneous:
MISCELLANEOUS: Diploid male spores in jason mutants give rise to viable diploid pollen grains and spontaneous triploid plants in the next generation.
Sequence:
MRRLLMNRNLSPLCRSVLRFIDLSVCRAMACFLDCFRARDNRSTSNLVSHSSLANSRKAQDSQNDLSALFLSEEKSASSPCLDKERFDLDSIHIDKGLRDEARFLKACGTIPETPIEIRKASQKLSPQHSGSSHFHSWISSSSSMGSRLAESSTPMKACEEVGRPSFTSEQTASSCVIDVRDNARISSASSDGTEVESVGTAIKGELDRTARPTFTAGKNKSVRFECDLDQSNSSNSSENGSSRKPEMGGKICFTVSSPNPTPLKLSDEMQTPGTIYPANMESGGRGRPRIRSQFVHSVSNIMENASLYKVYKDSHEGLDYEEQIEAETPSSETYGEKVEESSDEKLSKFEASFSPWLNQINENIAALNERTPGVGVITPGDRPIIGLVAAQWIENEQTEISPKMWDGNGIPNSTTKYKEDQKVSWHATPFEVRLEKALSEEGGQSLFPQRKLEVMMEEVEGDTDISQLHHSVQPNSVVSF
The following text describes a protein:
Function:
Parathyroid hormone elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Acts by binding to its receptor, PTH1R, activating G protein-coupled receptor signaling. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.
Subcellular Localization:
Secreted.
Sequence:
MTSTKNLAKAIVILYAICFFTNSDGRPMMKRSVSEMQLMHNLGEHRHTVERQDWLQMKLQDVHSALEDARTQRPRNKEDIVLGEIRNRRLLPEHLRAAVQKKSIDLDKAYMNVLFKTKP
The following text describes a protein:
Function:
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Sequence:
MLENRVKTKQIFIGGVAIGGDAPISTQSMTFSKTADIESTKNQIDRLKLAGADLVRVAVSNEKDALALKELKKVSPLPLIADIHFHYKFALIAAQSVDAIRINPGNIGSKEKIKAVVDACKEKNIPIRIGVNAGSLEKQFDQKYGPTPKGMVESALYNAKLLEDLDFTNFKISLKASDVIRTIEAYRMLRPLVIYPFHLGVTEAGNLFSSSIKSAMALGGLLMEGIGDTMRVSITGELENEIKVARAILRHSGRLKEGINWISCPTCGRIEANLVDMAIKVEKRLSHIKTPLDISVMGCVVNALGEAKHADMAIAFGNRSGLIIKEGKVIHKLAEKDLFETFVIEVENLAKEREKSLKD
The following text describes a protein:
Function:
Putative gamma-glutamylcyclotransferase.
Sequence:
MQHLVFVYGTLRHGESNHTYLQHSQLLGQFETKPEYALYDLGAYPGLVEGHQSVHGEVYLVDEHTLAQLDILEDVPVEYRRDTIETPFGTAWIYIYQETHRLHSLIDSGDWCQRV
The following text describes a protein:
Function:
Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway.
Sequence:
MNLDEYVRSLRGEVMGHHHGGPGRYEQKFKAFPISFLPKEKHSLESGGKILLPPSALNALSRLNIQYPMLFEISNPISGKKSHCGVLEFIAEEGICYLPLWMMQNLQLKEGEFIDIKNATLAKGTFVKIQPRTSNFIDISNPKAVLENSLRKFATLTKDDEIMIDYNNTKYYLKVVELKPANAISIIEADVSVDFAPPMDSKEATSPSTSSPGSHVSGPSKGLTFGPASTSAKPIPGGKKKKDESDSDSDSDDEPKFKAFAGTGARLDGKVGTPLGTSPKTLNTNNNNNNNNNNNNNNNNNNNNNSNNNNTKNEDTKFKSFSGKGHSLKD
The following text describes a protein:
Function:
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence:
ITGPSRPQRDGSRESPSSVAYQKLLDDCILKNRSRILAFKTAPEAPASKLPQFDEPIRPQKKQQRRIPKEPERVLVIHGLLDDNVLNLLDWGSNNVLAIGLKDAVYLWHAANESTKLLQPVEDRGPITCIRWSPDCAVLAVAFGNSDLDLIDPATGHVVDGMEDENQAPVLSLAWRSNSILTVGRFDGRYLASGGQDKLVHIWDACMPVSHHHSRQRQWLHRISSHTSTVKAVDWCPTRSNLLASGGGCNDHCVKFWNTVNGACLNSIDAGSEVCALLWDKNKSELLTSHGSPNNQLTLWNYPSMTRVAEVSGHSSRILSLAGSPLGGVVASAAADETVKFWNIFETPKITKPELPFAQFNVIR