lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular Localization:
Nucleus.
Sequence:
MWRNGNKVTGTNDAPLGAPRRWGGSQSDSKDSGAFGGLGAPTSYTSAPTTNRDDAPPPPPPPASTAPEPPPTERKRKSRWGAESEKVNVAGLPVAINGTIDAADLDRYAATLRLEQVNNKLRNGDVVPPEKERSPSPPPTYDGQGRRTNTREFRYRRKLEDERTKLIERSGRPSEKVYIPIKEFPEIKFFGLLVGPRGNSLKKMEGESGAKISIRGRGSVKEGKGRKEEFAGDDDDEMHCLVTADTQDKVDKCVRLINKVIETACSVPESQNEQKLNQLRELAQLNGTFRDFENQVCQNCGNPGHRKYDCPEQRNFSAGIICRICGGAGHMARDCTQRRGFNSGSSAAGGGVAQAFDSEYASLMAELGETSKVAPISEEGQNGQSDTPKHQSNWAGPPGSSTPARNGDSGAPSNTVPPWRVASNWHPPQPPQHHGGPYGQRNAYVFNAAQHGHHNHNHHNHHGHPHQHHYHGQHAHHHPQQHQQHIHQHQPAQPIMPTGAPGTEAGLASAAPSFVPQGAYAGYYGQ
The following text describes a protein:
Function:
Odorant receptor.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
LNWSTQSGMGNFSVITEFLLMEFSRIWELQVLHAVMFLLIYLATMMGNLLTIAAILIDPHLHSPMYFFLSNLSFLDICNISVTLPKFIIDSLIGSQTITLLGCTAQVFFFLFFATTEFALLVAMSYDRFVAICHPLHYGLIMMPSRCLWAAAGSWLSGLIYSAVHTGNMFRLPFSGSNVIHQFFCDIPHILKVSSSGVYQTEFALVIASSCFLLSCFAFLIASYIRIFSNVLKIPSVEGRYKAISTCSPQLMILILLLISVMTAVLGDTSDTSPIQNLFVAMFYAILPPLINPIIYSLRNKKVIAAMGKMLRKIFSLSMKYPSLKASKS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of pseudosubstrates such as p-nitrocatechol sulfate and p-nitrophenyl sulfate. Catalyzes the hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate. Acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate.
Subcellular Localization:
Lysosome. Secreted.
Sequence:
MALLGLLVLVLALASRGAVAGSAAESCSQVSSNACIHNAQRSMGVVAVEDAGACCQLCLNTSGCRAYTAWQQPNGTMSCNRFTTSDPTKIASGNCTSGLGKKVPNFIFVFPDTLRAESFGAYGNPFPNVSPNLDKFAEEGVRFNQAHVMHTQCSPSRCTMVTGRYMHLQGHRTQTHLVQDYEANYFRILKEHGYHVQYFGKNDMFSAMAFNLSVSAWAGNIGYASGSNPFPFGETGYYSFLRTGAGAVNASDLSNGDTLGVHNAINFLNSKPPEPFLLFLPSRGAHPPYGAPAPFHNLFTADKVKEKIKLRPRNIASKPTYMQNSNGIPHFRNLTYLNDDFFYQIQANYLNMIAYTDWLFGNLLEGLDQSGLRNNTAIFFSSDHGDFGGDFGLVEKWPGSMSDVLTRVPLLAQVPGGAKNHVVEAPVQTADILETMLALAEIDVDFVRFGQNLAPQLAGSEGQLNRTVYSEGGFYFSNEQMIEANECLSGGPKADYYPRGLEEAQPNGSPRAVMLRNLTAKLVYRPTGISELYNLTADPLELSNVFEDAAHASLRAAMMQQLTDWMVLTSDVTPVVTDSRGAPGYPYPIAAECAVEPLPDEAVTAIDPLDYLAINGVRE
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MRRERFEIDQYVRVRVTDTRYSIGVVTDIDEDQDRATVETRNGYEVTVPTSALRRAFLLVLDLNGVLVARGRGSFILRPNVSDFLKFVFSNFVVAVWTSGLQRSSNPIIDHVFGNYRDLLLFMLFRDACVPKPSAENPYGTEKNLQVIFDRYPHSFHSVNTIIIDDSPDKCSHPDIALCPIPFKDPVAQMQDEGLLQTMEVLKEVLLLDSGVPLILAAERRLEQLAKQQQQQDHPSGEEKTQEQAPSKVSTPTAAASASATASAGPVVRASVFGSHEAPSDMEEVELWKTRLCCDQLQGKCLRGDQCPFSHDADDGRPCSRKSGCRQHGSRWPKTREEVQLEEQRREARNAMRQRYEKTQQQREAHIRQPQKPPRQSNRANNRRRGGADDGAEWATETIGCSHTGDPMYDNMIDQQRRQSAPAAKATAATLPMGASGAALRNARGGSSATNAAAPPQAQPHSSQASSSMLLFFQTAASSSAAAPPLVPFSTRPIAPVVSVTDMNTLPRQQQQQPTSTDSARDNASSRRANNSNDHQHQRGGGARQQQQRRQAARPSQQPIHITGEQGDSTAVVNQLQALMGQR
The following text describes a protein:
Function:
Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MLPRWKVFVLFVTIGLLVVPCHCNLPPVFTQDMNNLALSEQTPVGAVVYKLEGYDPEGGNVSFGLIGSDNFIADPISGDVQVIKELDREAQDTLSFSVSIRDRVSATGIESENDNIVNVPITIIVLDENDNPPEFQNVPYETEVLENALPGTTIFDGILVTDRDTVGENLDVSCIPQPQNPDACEKFAIEVTDSQQDRLTAAVVLKQPLDYNERMIYQVLLDASDGLYNASAGLEIHVRDVQNAPPVFQGSLAAVINEDSPIGTLVMVIQARDGDRGQPRKIVYELVTNPMDYFLLDKHTGELRTAKPLDKEALPDDTGLIILTVKAREVVDGVPGNDNLTVASTQASITIRDVNDSPPMFNKTEYFVSLSENTAPGTPLPLEISVRDPDVGENAEFALRLNDVSNVFDVEPKLVTGSSQISIRVANGTLDYENPNQRKFIVLLIAEETKTNPKLSSTATLTVAITDANDNRPTFEQDSYSTTVSETAHPGQLITTITAKDLDSGLYGDQGIRYSLSGTGSELFSVDAITGAISVADCPGSGVERTAGEIQRVAGQLVRRRRRQIPTRSDLQHEQHQNASARGIEYMTYRIVNSGESNEYHDVNVIAPPTISTLYDSFETTTLEQQQQLVEELALPTTVRIEPLLTNDIQHPRQSDGPGKAPCLDYETQSVYYLSYRATDDEGRGQTSVVSVRISLLDANDSPPVCESPLYRASVDEGATAFEPPLIIRARDPDVVSEINYRIIGNEAVTRHFEIDKRTGQLTISKTVALDVNHLRSENVFFGVEATDGLYTTLCNVNITIRDVNNHAPQFARENYLTSIEENFPIGTVVDRLQALDLDTGINAEIRYRIQQGSFDDFAIDNRTGVVSIARKLDYDRRNTYQMEIVASDSGTPSLSGTTMLTVSIINSNDKAPYFTPTTQRAEVSEDAPIGTLVHTLVAVDPDVASSESLDYAATEPITAVDKNGKEVGEMEDFKDMFMIDRSGKVFVNRRLLRDSFAVIRITVLVTDTTAPSIQQGEGLLIITITDVNEEPPLFAPPWTPENPHYHYQVVEEQPIGTILTTVQATDADSTIAEYRMTESSFFEIHNTTGLVRSIARIDYEATPVIKFNVSVIDTGVPQLTSTAQITVEVVNTNDNDPEFEQPEYTLQVRENSPVGTLVGMVRARDADAGLYGQLTYTIVGDHSGNFVIDPDTGAITVHNASALDRETEQEASLTAIATDRAPEGMRRSTTVPVQIRVLDENDNGPTFTQQIYHATVAENAALHPPAAILQVMATDPDEGAAGDVKYAILSDNVGGIFRLDANSGILYPGASLIGKSGQYRIDIEARDGLGSGPHNDAATIVIEIQSINQHRPVFIMPALYNATVEIPENLASPDYLVMTVKATDNDSGSNGKVLYYLQVNSVNVQETDEFSINEMSGELRIRRQLDRKRQSRYELILVARDQGTPAWFETLRFLTVLLVDVNENYPEFPDASNPYKFFITENGARDVRIGKIQAFLDSPNPSIFYYMLVGNEDGAFYVDKTSGDLYTNRSVDREENDLYVLYVLASKQSDLYVSEHERALLSMDQLERNATIAKVWVHVLDVNDNAPVFKRDVYYAGISSKASINELVTIVNATDRDLGVNATLDLFIRGSYLYKYGATKTTGSIVPSPFAISKDGRVVTANYMAEYNQDRFVLEIVAKEIESPEREAVTRVHVWIFNPEQLVRMILSRPPSEVHQDRDEIVSELGNATQRLIIVDEIRYHVDSLGRIRMDWCDMYFHAVDMTTQMIVPVEEILREIDAKYDFLQDYNAGFSIMNVVPAYATTVQDEFDLALAALIALLIVLFVGAVSFIVLCCCLKHWSITIPSETRRKDALIKKQIIEDLNTTENPLWIEQKLKLYEEQELTMQVFSEPEMSQQQSMNNSNSTNSSQDPPSQLSLTLGLDHHHQLHHHQQSAAHQQRRDSYDLSQAGDNTYATIQPRNYGTSNLSTVLGSSLAPPGALSSSGVTSPSATSSSEVADYATLRNSRAPSLFEFRGSTFQVQQPGGTDQPDYVTELM
The following text describes a protein:
Function:
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
Miscellaneous:
MISCELLANEOUS: This protein binds one calcium ion.
Sequence:
MPVVISEKQFNDAHQAFKLHDKKDEGAVSNKELTNLFKSLALHVSDDKLQQWVDEMDEDATGVIRWEKFKILFERKVQEDEDERELRSAFRVLDKNNQGVIDVEDLRWILKSLGDDLNDDEIQDMINETDTDGSGTVDYEEFSALMLG
The following text describes a protein:
Function:
ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Also required for efficient mitochondrial translation (By similarity).
Subcellular Localization:
Mitochondrion matrix.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence:
MNISLKGAIFSTVGRFNLPKVQGFIRWNSTMKSQQPTLFSEVASLSSTFKNSLSRAGFEKMTPVQQRVLNEVFPNEENAVVQAKTGTGKTLAFLLVAFKDVLKGKPRLNSSKIHSVILSPTRELALQIFEEARKLTYGTGIRVSYAIGGNSKMREENAIRRGNANLLIATPGRLEDHLQNPRILESLSTDSFILDEADRLMDMGFAESILNIHEAVTTTKTRKLCFSATMPPKVSNVFRGILGTDFKLINCLDPNEPPTHERVPQFVIETKLDKVFSSSLSLLQQLTSSNPSSRIIVFLPTISMVDFVGGVLENHLKIPCFILHSGLTTAQRRSITESFRKCQSGILFATDVVARGMDFPNITQVVQITGPSNTDDYIHRIGRTGRAGKTGEAYLILLEQEKPFLNSIKHLPLKRATIEPLSDQALSTLRSDIEKSSKFSRTNALKTLYGSKPHVFSGSSQRRATGKNIHESAIALFSLHDVPGLMEELIYKSRGRGSPKGFRGSQLKYPSSSSSSFQRRPRSLPSRGRYQQSRR
The following text describes a protein:
Function:
Required for 27S rRNA processing to 25S and 5.8S.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSAPSPFIKKLAANDRKTRDKALESLQRFLSQKKKFERLDFLKLWKGLFYCMWMADKPLYQQKLSDNLAALVPIVWIDNRILFQSTFWETMGREWTGIDILRTDKFYLLMRRFCAAAFRDIQTRSKTALLDKVVAEYNQMWMDGPFNTENLAFPNGILFHLADIWTEELRKVYPEDVPKADWYLPFDSTIKSSHNVVLRKTLPKRLDRVSEYTKDSQ
The following text describes a protein:
Function:
Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates (By similarity). Confers salinity and drought stress tolerances by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormones levels such as gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-acetic acid (IAA) (By similarity).
Subcellular Localization:
Nucleus. Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.
Sequence:
MAAAAAIAAALLRRSTSSQHHRRILLLPLLSHLQRAAPRSPSPWDPPPHHRFFFSSDVTAEGDSKPRPPLDGKQLWREVSTSEPATGASRLPKATWDAVVALLRRFGKDPAMSDQALALYIPASAFPTYARRFRHFLPARLSLESAEHLLSLPADDAHALLLPAFAEFCVTHLADELRKHESVMAAADLTAPHAWYPFARAMRRRVVYHCGPTNSGKTHNALTRFAAAKSGVYCSPLRLLAMEVFDKVNALGVYCSLRTGQEIKEVPFSNHVACTIEMLSTEEPYEVAVVDEIQMMADPVRGYAWTRAVLGLKADEIHLCGDPSVLKIVRKICADTGDDLEVHQYERFKPLVVEAKTLLGDLKNVRSGDCIVAFSRREIFEVKLAIEKFTKHKCCVIYGALPPETRRQQAKLFNEQDNEYDVLVASDAVGMGLNLNIRRVVFYSLAKYNGDRMVPVAASQVKQIAGRAGRRGSIYPDGLTTTFLLDDLDYLIQCLQQPFEEAKKVGLFPCFEQVESFAIQFPDLTFNELLDKFRENCRVDSTYFMCHQESIKKVANMLERIQGLSLKDRYNFCFAPVNIRDPKAMYHLLRFATNYSQSRRVSIAMGMPKGSAKNDTELLDLETKHQVLSMYLWLSHHFEEDHFPHVQKAEEMSINIADLLAKSLAKASWKPTSRQQAKPRRENEEDNDVEQASDDNAKNDSEDGYERSISRIKPFMRKRLDRPSQDPSSLNFVA
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its conjugates. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Acts as an omega and omega-1 hydroxylase for arachidonic acid and possibly for other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes. May down-regulate the biological activities of N-arachidonoyl-serotonin, an endocannabinoid that has anti-nociceptive effects through inhibition of fatty acid amide hydrolase FAAH, TRPV1 receptor and T-type calcium channels. Catalyzes C-2 oxidation of the indole ring of N-arachidonoyl-serotonin forming a less active product 2-oxo-N-arachidonoyl-serotonin.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Microsome membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MYPAFGSLQVILLAVLCVIATLVLCGRPRNLPPGPRGLPIVGNAISLLKGALPLVYTDWSKKYGDVFTVYFGPRLTIVLNGYAAIHEALVKNAENFSSRSPSHAMRTPDGKTLGIAAEPYGPKLKEHRKFAMMSLRDFGVGKRSLEGKILEEARGLGDEICKTEGRPFCISQMMQNAVSNVICSIVFGRRYEYDDMAFKDLLNAINGVFSRSFAVIFAQVFRPMRILPGVRKPFQKLKRNQAKLINHIRDRIKEHEDTFDPKDIRDFIDAFLLESKKRQGDENSTFTEQEHAAIVYQLFVAGTDTTSTTLRWALLYMILHPDIQEKVQQEIDSVLGPNQEPAMAHRSQMPFTEATLAEVSRLASVTPMTIPHGTSNDTAFRGYNIPKNTSVTVNIWSVHHDPNLWPEPDKFDPTRFLNDEGKYVKRNEVLAFSIGRRVCLGEQLARMELFLFFTSLLQRFTFKLPEGAPKPSEKGIHAALHHPVPFKLIAEPRD
The following text describes a protein:
Function:
Involved in the development of the fruiting body. Overexpression phenocopies the spnA null phenotype.
Subcellular Localization:
Cytoplasm, cytoskeleton. Membrane. Nucleus. Note=Localized in the subcortical region of the cell with some enrichment in cell protrusions. In developed cells, colocalized with spnA. May translocate to the nucleus in response to a regulatory signal.
Sequence:
MSIKLPLSNINSGGNSNNSSSSNSTSNNNININIGNGIPTNIEKMTFEDSETQKLNIKQQSNNNTSTSVCVSSIHSSSPISSPTSHQVNKSSGSLPPVIKRSPTTTHHHNSSGSNSSSSSSGSNNNNNQIKTSNGMNKPNPTGFLFGSKPRENSQNKIDDNKGVNLAVSTSNSSNNFHKSHSESNIININAPPVETVNMEEIYNNIPSSISMENIRENENNNNSSNNNSNNNNNNNNNNNNSNNINNVNGNKSSLASSTSSISSLSSVSTLSTSNAATNTNTNANTTSTTKTTSTVRSTSPTQFKPRVEFDENNPNAIILSRQRCKSISSPSDFRLNPPSNVHMPTSSLSTSTSTTNVNGLLLPNGVGGVSMSFTPSGLPMTPPTNSSQVDTLQMSTESITIQPSSLDSSSESVSDGLQSVSGSPVTASPSPTISNNTNATTTNNNNNTNTNNNNNNNNNQHNHHHHQHSHSQQHDVYQIKKENFPSSPTSPTLLPSETHDFSSEYSSNPGGKCAICRKPLWSFPISDKSRRCRDCSLVVHRACVPLATECPSAKKSPSKLSVPNGNQSNSSSSSSSSSSSSSSSNSSSSNTKGHSRTPSSPSVSSIPGFQLTSNASQNLHVNSHTLSLLVNGATIDSNHYKRNKKSLEAGARDFHFIFRGCGIPLDEFPLDSYVCGLYSYFAHGRLYLTESYVCFYDGFVFDRTKERTKIIKVSNIASIEKRSSGLNPSAIKIKTFDDQSFIFTHFMHREVAFDDLEGLLIHQESLHFAHSIVANNFPGMNEAIRGQTKRLLSRARLDGHYQIHSKIRCPMPSKEILLMSAIKNNNLDMVVTLLNYYCQVNSDEINSVDSKGYTPLHNAVFSECSDQIFMHLLNQKEVRVRERNMDGNTPLHYFCQKFKSPECQRIVQAMIEKGANINEQNYNGETPLHKAIFNHSVRLLMVYILLKNNANVNIVNNAGESPLHYAVRLGRLDVAKMLLAAGADPTIISLRDRKTALALAVDYDVCPEISDLLRRLDTITTSLEMYELEKFQASLVVEELQKENVVARLDEKLLDKIGCTDKEERRKFLSLKSNRLLIHHPARTQGAKIILKEMETMDIKNGKLIISETELEYTEKIGSGASGKVFKGIYRGRVVAIKVLKSADDEMTREDFLKEFGVLASLESHTIVGLYGVVLEPKICLVMEYCSNGSIYHSIRKNPPSWERFFSFVQQMLAGINALHQSTPQVLHRDIKTLNFLVNHNNKVKVADFGLSRFNTESNQETLNKTRGTSVYCAPEVFEGKEYNERSDMYSMGIVMWEIVYCVVYGCYMIPYQEYNKMFNAFQVALLVNSSKRVLRPTIPIGVPQVLKDLIYCLWDHDVSSRPTATEAMTALAVCEKEYKQNKAQWELVITKKEPTPLPRVAPLPAFPGYRQFYEQNLDIKPIPEEEQIYQEAMEKQRRNQEASANRNQKNKELLNNNN
The following text describes a protein:
Function:
Deubiquitinating enzyme that functions as a negative regulator of the innate immune system. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Controls neuroectodermal differentiation through cleaving 'Lys-48'-linked ubiquitin chains to counteract degradation of select chromatin regulators such as ARID1A, HDAC2 and HCF1. Acts as a positive regulator of mTORC1 and mTORC2 signaling following phosphorylation by MTOR: acts by mediating deubiquitination of BTRC, leading to its stability.
Sequence:
MTILPKKKPPPPDADPANEPPPPGPLPPAPRRGGGVGVGGGGTGVGGGDRDRDSGVVGARPRASPPPQGPLPGPPGALHRWALAVPPGAVAGPRPQQASPPPCGGPGGPGGGPGDALGAAAAGVGAAGVVVGVGGAVGVGGCCSGPGHSKRRRQAPGVGAVGGGSPEREEVGAGYNSEDEYEAAAARIEAMDPATVEQQEHWFEKALRDKKGFIIKQMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQYSTEPINTFHGIHQNEDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPSFKPGFAEQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQVRGPSQPRKASATCSSATAAASSGLEEWTSRSPRQRSSASSPEHPELHAELGIKPPSPGTVLALAKPPSPCAPGTSSQFSAGADRATSPLVSLYPALECRALIQQMSPSAFGLNDWDDDEILASVLAVSQQEYLDSMKKNKVHRDPPPDKS
The following text describes a protein:
Function:
Involved in the anaerobic metabolism of phenylalanine and phenylacetate. Catalyzes the oxidative decarboxylation of phenylglyoxylate to benzoyl-CoA and CO(2). It can also react slowly with 2-oxo-3-methylbutanoate and use different electron acceptors such as benzyl viologen, methyl viologen, FAD or FMN, but NAD seems to be the physiological electron acceptor. Also catalyzes an isotope exchange between CO(2) and the carboxyl group which proves partial or complete reversibility of the oxidative decarboxylation reaction.
Sequence:
MYEVRFHGRGGQGSVMASGMLAAAMVEEGKYAVSIPSFGFERRGAPVVSFLRMSDREIRQLTNIYQPDCIVCVDPTLTKSVDIFAGMKAGGTLVQATHHPLSELALPDCVSTVGLLDAVKIALEIFKRPITNTLMLGAFAKTTGVVSLESLKRALEDSEFRDAGLAQNMTALERGYAEVAVHHIERRAAA
The following text describes a protein:
Function:
Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MRPLDETETDAVFRKLYSFTGHNLKNIVENPSHEGPDPNPGRYCFRLHKNKVYYVSESLVKRATNISRKNLASLGTCIGKFTHGGNFHLTIQALNLLAANAKHKVWLKPTSEMSFLYGNHVLKGGLGRITDSISKNDGVVVFSMSDVPLGFGSAARSTQDCRKLDPNGIVVHHQADIGEYLRMEDEL
The following text describes a protein:
Function:
Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
RLLPQEDGVLYVDSDAVFFLSVEDLWNYFGQMNDQQLAVVFSDVEDEALTIYNEWEMPHYKRYGINAGVMLMNLTRMRNSGLDALLLSWMDKYHHKVLDFHDQDIINTVFHHHPEKVFHGPCKWNFVHLVCLSNISCRGETPALVHGTNETFSDPYRVPAYRAIGKAIQQYRLGTSLERGFIDVLEENLRSTKSSVCADKIQGFVVHWRRLARQLDIERGWSTTEAATATS
The following text describes a protein:
Function:
A maternally expressed membrane and cytoskeletal linker protein, which is essential for attachment of the centrosome to the male pronucleus. Promotes male and female pronucleus congression and subsequent fusion after fertilization. Congression is mediated by the sperm aster microtubules.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Chromosome. Note=Localized at both male and female pronuclear membranes during pronuclear congression and fusion. Colocalized with tubulin at the centrosome adjacent to the nuclear membrane. At prophase is localized at the centrosome on opposite sides of the zygotic nucleus and at the reforming nuclear membrane. At metaphase is juxtaposed with the centrosomes at the mitotic spindle poles. During chromosome segregation is localized with the chromatin. Undetectable at the centrosome at the onset of anaphase, but becomes again apparent by late mitosis.
Sequence:
MDVGVTPRRHNPVDSICRKLQTIQRRDQEINSPFQIPKFQTNSYDSPHSGLRFNLEAILKKHTVRPDDSDSASSAGMLTPTASPGPGSSCNTPRAPITPVNATYSITSTLGTLGTIGDRRTSGTYSRPFRRNCSTPSAQTGDNYFNFTPRYSTQSQGPDTDVRTSKIPTPGLFSYNLNFSSDISNMDSELAYPALVVKRLSLGEGSLFTSEPKKESMAEVSLICEEDLLDTIFQACDTQCRGKVYVSHIVDFLRHTTCRSSEDSGLEELCNMLDPERKDISIDLDTYHAIMKEWIEDCRNQGKDLKNDTQQESSKLRDSLSAKRSALLNMTSGSLEAFGGEASRADLETSDLVFCVADLQLNNQKLQEEVRKLKQAVENMEDTNQKLIEENEELKTQAKMGQQLLQKEKMLKEEVEEMKLSLTSSEESRAQAAAQRKQMERENQSLISKIAALQEENMKVTLEAEELQKKMNDLCDLNADLQVQIHSFDAILADKESLIQEKNKQMDELKVAVVEYSSVTELLRADKNKLESQMQMMQPDVTIPGLSLSVAYRLNQTSSGSLQTELALAQNPLEGLEHLSTSVCFASSLDETLDREVLLLLQGPTPEQLSLEFKSLISRLKREFKEDGLTFLTAIRSLTENSETQEANTDLKMQGLEVQLEQRRTDWIRSLEQLDQYRDSLERELLKMASNMRRSRTEILHLSVKVQEQENQKQQLREEVDRLKTPLDNREASSQTPDHLQQVVEELDGPSLEWDEEYVLSESPPLQELGPDQQMLEELCCDEEVLQALKQEEEEPTETVSDKEKITAKSEGEGEATYDSGVENEEPQRDFTLSHMCLPDKKSERESNEAPFVGEGGEQRPCMSLKEEDRLPECTGPEDAHEQAAPLPHTHCECAGDQPLTYDNLEVTSVKDHILSTEPSSLMTCELVSPSTGHPEVGNSITGRTEQLVGTNGEPEEERLTTGADMSDLQRLGEGQLSKVSAKSDKSLLLPVAEEEEAMPEAVEVTSAGVNSPDKHKTGSKKTVVTSDSNSTGSADSLKDPSEKVKDMTFDPAASEDNIPTVPATQSPKKDPLASRNKLKKEMSSMEVIEEQKAQEDGEPTVVTEKEGDTSVSSENASDSTKDDKNSLSPSDKEIEAEFHRLSLGFKCDMFTLEKRLRLEERSRDLAEENVRKEVISCKALLQALIPRCEEDNQSMEIIHRVQKNLEILVQSMTRVSSRSEMLGAIHQETRVGKTVEVMIQHVENLRRMYTKEHAELLELRENLTPNERSFGSHSERDDFRNKKQTTSNIFKTTSRRISIATIPRSIGGQTHFDMPKDMAETEVERLSRRSPWNMAAKRPPLKRFVSSGTWADIDEPTLMNSPTPSPTDNAPPSLMEGRPAVSRGARGIWIWVALFVVLAVLLALLASLMLQPAVDAAPVGTGDSWMTIQQLLWPYTGLRHNGQPPV
The following text describes a protein:
Function:
Probably involved in the processes of spore formation and contributes to ascospore thermoresistance by participating in the morphogenesis of ascospore walls. The enzyme may do this by modifying glucan linkages in the developing ascospore wall, thus strengthening it or lending it plasticity.
Subcellular Localization:
Secreted.
Sequence:
MVSFRGLTTLTLLFTKLVNCNPVSTKNRDSIQFIYKEKDSIYSAINNQAINEKIHGVNLGGWLVLEPYITPSLFETFRTNPYNDDGIPVDEYHFCEKLGYEKAKERLYSHWSTFYKEEDFAKIASQGFNLVRIPIGYWAFTTLSHDPYVTAEQEYFLDRAIDWARKYGLKVWIDLHGAAGSQNGFDNSGLRDSYKFLEDENLSATMKALTYILSKYSTDVYLDTVIGIELLNEPLGPVIDMERLKNLLLKPAYDYLRNKINSNQIIVIHDAFQPYHYWDGFLNDEKNEYGVIIDHHHYQVFSQVELTRKMNERIKIACQWGKDAVSEKHWSVAGEFSAALTDCTKWLNGVGLGARYDGSWTKDNEKSHYINTCANNENIALWPEERKQNTRKFIEAQLDAFEMTGGWIMWCYKTENSIEWDVEKLIQLNIFPQPINDRKYPNQCH
The following text describes a protein:
Function:
Transcription factor (By similarity). Plays a role in the unfolded protein response (UPR), perhaps mainly during constitutive endoplasmic reticulum (ER) stress, by activating transcription of genes involved in the UPR. Plays a role in modulating lifespan, acting by positively regulating expression of calcium-binding chaperone crt-1, thereby influencing ER calcium homeostasis. By activating the UPR pathway, confers adaptive protection to subsequent exposure to hypoxia. Involved in protection against proteotoxicity, probably acting via the UPR. Probably acts in the UPR in parallel with the ire-1-xbp-1 and pek-1 pathways. May be regulated by endopeptidase S2P-mediated proteolytic cleavage.
Subcellular Localization:
Nucleus. Membrane; Single-pass membrane protein.
Sequence:
MNFDNTVHESNFDDLLHNPNFPPQFDQLELDSLLYGTDESQESTSSSSFGFSDQNAGFRSRDGGSLGDSSSDSSPPLSCANFTENDQEMWDFGFQSRSPFENFEQQFGSPYQDDEVIAEPTNEFMNARYLREEPAKHLPMQQKRIITILPKQSQPVKRIVSRPIQKVYRVKESPGSQQQTYRVVQPLMPSPSQATQRQIKQMYYNEPVQEIHMQPKSGPLVRQVSEEPRYVPIAPTVDIKAEPQVFTSEQNRKIRNRMYAQASRMRKKEADEHMKMNLQELLQENEILRTENAALKQRLAFFEHEEPVVEVPQPFGRNQKKKRIIAAGSVLMMFGLFAVISPFNVDNNLNINNQIMAISNETSMVARHGRVITYEDSAPVAKIPTQQPIHNYPNSTQNDCDMYKLNATETIRVNNDIERWVQVHSFDNVPMKFSGGLLNKEAMRKFNYAQKVKPASVYGPQTLAVQKKSEQAALRSRERTWKQLDLLKTGNNIQLDNEKIQRKRQDIDKIASIVRQKGDTLYIMTLQDYVLLPSLIKGANSVPKLSLLLPSVPMNGTLQDQYTLLRVDCEVTGTGQLTLSNKQLSYLMP
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MGEVSAIVLAASQAAEEGGESSNFLIPNGTFFVVLAIFLVVLAVIGTFVVPPILKVLRERDAMVAKTLADNKKSDEQFAAAQADYDEAMTEARVQASSLRDNARADGRKVIEDARVRAEQQVASTLQTAHEQLKRERDAVELDLRAHVGTMSATLASRILGVDLTASAATR
The following text describes a protein:
Function:
Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism.
Subcellular Localization:
Cytoplasm, cytosol. Note=May also localize to mitochondrion and nucleus.
Sequence:
MSQAGTGVCGNGGQEDSAAAGPFSFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKSDAEPGPQAWQPKERAALQEELSDVLIYLVALAARCHVDLPRAVISKMDTNRQRYPVHLSRGSACKYTDLPRGTLSENEAVGSGDPASELGNQAST
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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; Multi-pass membrane protein.
Sequence:
MYNAISLIIILPCISWLFPLFFGRQLGYVFVTRMTSTLIIITTLITYYYFYQLLGNNNPINLELFNYLNIDYLDINYNFEIDALTITMLLAITTISSMVHIYSIGYMETDPHQVRFFSLLSMFTFWMIILVTGSNYFVLFVGWEFIGVTSYLLISFWVTRLQAMKSALSAVLMNRFGDAFFVLGLCVIAYVFGTLNYSTIFATAYLINTDLLVLIMLALFIAAMAKSAQFGLHNWLTLAMEGPTPVSSLLHAATLVTAGIYLLLRSANILEYTPTVLFIILWIGALTTLSAGLIAICSNDLKRIIALSTMSQLGMMTIAIGLSAYNLALFHLLGHAFFKALLFMSAGSIIHSILNESQDIRTYGGLLSYLPYTYICITIASLSLMAMPGLTGYYTKDIIIESTYGSYSISNYVVYWIAYLSAVLTCVYSMKILYLTFYSNPNNNTITYYNAHESNIYITLPMFILAIFAMFAGWILKDIYLGVGTDFVGTHILPNNFSYFDTEFSITQFYKLLPLISAILVSILIVVLNEFFAIVFNLNNKYINTVYSIFNQKLVSDQILNHFIIFKGLVTSGNIAHHVDKGSLYRLGPVGINRLLNKASYNVINLSSNTRSSLSMNSMLILITIVSLLLLVLVMNVNFIIVIPVLISILYILFS
The following text describes a protein:
Function:
Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late stages of complex I assembly.
Sequence:
MASLSLSISPNPDRLIDGIFVSPRRQLLRRVAINSSPSGFNFLTKLTSAEKHRRNKVAAVRMSSISPASHSYDVVVVGAGIIGLSIARQLLIGSHLSVAVVDAAVPCSGATGAGQGYIWMVHKVPGSEKWELAMRSRELWEKFAEDIKYQGMDPQEVLGWKKTGSLLVGKTSDEMAVLKEKVDKLSKAGLKAELLSIIDLKEIEPVLVVGEEGGAAFLPNDYQLDARRSVAYIEKENRKYASEGRYGEYYNQPVTGLLRSGNGEVEAVQTPKYSLYSKKAIVISTGCWTGSLMQDLIRDSDIKLNIPVKPRKGHLLVIENFNSFKLNHGLMEVGYIGHQDAILQPNNLDSGAETSSISMTATMDTLGNLVLGSSRQFVGFNTEINEEIINKIWERAKEFFPSLRELLLKDLEKNREVRVGLRPYMPGGKPMIGPVPGLSNVFLAAGHEGEGLTLALGTAEMVADMVLGNPSKVDNAPYALHAHCS
The following text describes a protein:
Function:
Involved in the archaeal biosynthesis of heme. Catalyzes the methylation of carbons 2 and 7 of uroporphyrinogen-III (UROGEN) to yield precorrin-2. It does not catalyze the overmethylation of precorrin-2 to trimethylpyrrocorphin.
Sequence:
MSGNYGKVYLVGSGPGDPELLTLKARRLIDSAEVIVYDQLPGKAILDSMPASAEKINVGKYAGSHTMTQAEINEVLVQKAKEGKMVVRLKGGDPYVFGRGGEEAEVLVAEEIEFEVVPGITSAIAVPAYAGIPVTHRESTSMVTFITGHEDPTKEESGLDWETLAKFGGTIVILMGVKMLGRNAEELMKHGKAPDTPVAVIERGTRADQRVTVGTLANIASLAEERKVKAPAITVVGDVVHLHDILGEQRTGVDF