lhallee/plat_data huggingface dataset:
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:
MQVEVFKVKLSDLLCLTKPKQTFLLLLTSIFTYVGAGGMRLDALLLLTAAMLLSISGTTSVNMALDADIDAMMPRTKDRPVPSGRVSRVEALSFGLLLFIVGLGLSYLINPWTAFATSLGMAFDILVYTMWTKRRTPLSIIFGGVAGAAPSLAGWAAARGSIELQAIMIALITILWIPSHIWYISIYYLDDYAAARVPMAPVVWGIERTSKLIVASNVLMIILQLLLFLMGPLGPIFLVLSLPITLRFLIHSIRYARSPSRGEARRMYKVASPVEGVIFLAIALDGIFRILWSS
The following text describes a protein:
Function:
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Sequence:
MAYAKSSKAISLAWTGASGAPYGLKLLECLLASGYQVFLMISSAARVVLATEHGLQLSANSDKAKAQLLDVLAQKNIPLSGELVVLGKDEWFSPPASGSAAPKQMVICPCSTGTLAAVATGMSNNLLERAADVVLKERGQLILVPRETPFNAIHLEHMLNLSRLGATIMPAAPGFYHNPKSVEDLIDFMVARILDHLGVDHALTSRWGYDKHSPNDIDN
The following text describes a protein:
Function:
Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Golgi apparatus. Early endosome. Late endosome. Lysosome. Note=Rapidly endocytosed upon ligand binding.
Domain:
The NPXY motif mediates the interaction with the clathrin adapter DAB2 and with LDLRAP1 which are involved in receptor internalization. A few residues outside the motif also play a role in the interaction.
Sequence:
MRLAGWGLRWAIALLIAVGEAAVEDNCGRNEFQCQDGKCISYKWVCDGTAECQDGSDESQETCKSVTCKMGDFSCGGRVNRCISGSWRCDGQVDCENGSDEEGCSPKTCSQDEFRCNDGKCIAPKFVCDLDLDCLDGSDEASCPMPTCGPANFQCNSSMCIPQLWACDGDPDCDDGSDEWPKHCGTPHPSGPLQDNNPCSALEFHCGSGECIHSSWHCDHDPDCKDKSDEENCAVATCRPDEFQCSDGTCIHGSRQCDREPDCKDLSDELGCVNVTLCEGPNKFKCQSGECISLDKVCNSVRDCRDWSDEPLKDCGTNECLDNKGGCSHICNDLKIGYECLCPEGFQLVGKHRCEDIDECQNPDTCSQLCVNLEGSYKCECEEGFRLEPLTKACKAVGTIAYLFFTNRHEVRKMTLDRSEYTSLIPNLKNVVALDTEVASNRIYWSDLSQRKIYSAQIDGAPGFSSYDTVIGEDLQAPDGLAVDWIHSNIYWTDSILGTVSVADTKGVKRKTLFQEEGSKPRAIVVDPVHGFMYWTDWGAPAEIKKGGLNGVDVYSLVTEDIQWPNGITLDLSGGRLYWVDSKLHSISSIDVNGGNRKTVLEDKKKLAHPFSLAIFEDKVFWTDVINEAIFSANRLTGSDISLMAENLLSPEDIVLFHNLTQPRGVNWCERTALRNGGCQYLCLPAPQINPRSPKFTCACPDGMLLAKDMRSCLTESESAVTTRGPSTVSSTAVGPKRTASPELTTAESVTMSQQGQGDIASQADTERPGSVGALYIVLPIALLILLAFGTFLLWKNWRLKSINSINFDNPVYQKTTEDEVHICRSQDGYTYPSRQMVSLEDDVA
The following text describes a protein:
Function:
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Sequence:
MDVQMERLRAGLGPPAPKFPFGSAWIPSTAPILSENVETVQRRAGSGRSDELHHPHNKYKHARFEDFTNKREIGKGRNTVIYSAVCTRTNERVAIKTHTRKALSAIDLHRIKRECKLLRMLRHEHIIKWLGIFEDADCIYLVQEHAPGGDLFEHLKKWGGRMPEKWVITQVLIPLMKAMREMHNKGVVHRDIKPENILVAADETIKLCDFGLAINARAERPASRLGTLQYMAPEVVKRPFQRPKDMSKVEAYDEKVDMWACGVLVYELIVGYPPFDGDDDDIVTADIMHRDVKEMPDCLSPECRNLVLGLLQKRPSDRLSLDQLWQHPLVLRHSKPEDLKPARSARVASSKPRPGPDRAVDRSRISDADSSKTLNSPPSVLQAARASADEIAQPPQPPFEDPNPPAAVAAAPGVTDLMARLTLSLKTHLHASLTQDAQMNAQMSEAAPETAAAEAAAEPPSPVTSPDIISRSPGNTATNLQAWQFLRSISTQPGGSGTTQARRPQVHAPGTSWAWLREPARKAAPRAEPDCPRTWYMYRILPGGRRKSHQAVRIRSRSWGQRERPRKGGRRALAYGRGLVSSSAVLDRRNTSWSGTESDPETSVSPVGKRPERRGDSPDRGGPVEEAVGCGDRDGITIAGLRLSAERDDGLAEARADALKDARADGTGEETMEVEEEQTAPGLPSPGFLRPFQTWFNFF
The following text describes a protein:
Function:
Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity.
Subcellular Localization:
Nucleus.
Sequence:
MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQEDEEKASEYRGSEIDQVVPAAQSSPVSCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKAGVKHLFNIISRKKEALKDDSIQKDKGSCKEDPLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEIKNLTEFSSKVEEKSLQKEETGGISSTETDSTRNLDDLKEQLPKGNWKRKSDGESGNMKKKVKLSRESQPLEENQRQTRSKRKATGDTLEASPKIIPKCVSENESAKPSQKKSKVKINWLKPATKQPSILSKFCSLGKITTNQRSKGQPKVNEGDLEEDLEKDGRDNTVNGSGPASPGSSVTPVDSSEAKSINKGAEQIGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKVTDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGTAENYDDEVSIRVGGNAQPSKVLNKKNVEGIGLLGGQKSKADYELCSKASNPEKVVGTPFTDSRNSETNDTNGTQESDRSKESSDQTGINVSGLENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLLFYKKL
The following text describes a protein:
Function:
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Sequence:
MSLPNPDNRPLLIGPPTGPEAPFPFRMEGEVISGFGRGSKELGIPTANLPVDDENAWIKNIDSGIYFGWASLKLPASHPNSVLYQKPPTSEPVMMDPVQQQQQQQQQQRNQQQQQEGGVGSAQQEKLVDQETGQWQIYPMVMSIGYNPFYKNTVRSAEVHVLGEFAADFYGVGMRLLITGFIRNEKDYSGLEALIADIHFDCEVARHSLARKGWRVRELGVKEGEEEGELDGSWLVR
The following text describes a protein:
Function:
Acts as a negative regulator of hedgehog signaling.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MALGKVLATALALALAVLGSLSPGARAGDCKGQRQVLREAPGFVTDGAGNYSVNGNCEWLIEAPSPQHRILLDFLFLDTECTYDYLFVYDGDSPRGPLLASLSGSTRPPPIEASSGKMLLHLFSDANYNLLGFNASFRFSLCPGGCQSHGQCQPPGVCACEPGWGGPDCGLQECSAYCGSHGTCTSPLGPCRCEPGFLGRACDLHLWENQGAGWWHNVSARDPAFSARIGAAGAFLSPPGLLAVFGGQDLNNALGDLVLYNFSANTWDSWDLSPAPAARHSHVAVAWAGSLVLMGGELADGSLTNDVWAFSPLGRGHWELLAPPASSSSGPPGLAGHAAALVDDVWLYVSGGRTQHDLFSSGLFRFRLDSTSRGYWEQVIPAGGRPPAATGHSMVFHAPSRALLVHGGHRPSTARFSVRVNSTELFHVDRHVWTTLKGRDGLQGPRERAFHTASVLGNYMVVYGGNVHTHYQEEKCYEDGIFFYHLGCHQWVSGAELAPPGTPEGRAAPPSGRYSHVAAVLGGSVLLVAGGYSGRPRGDLMAYKVPPFVFQAPAPDYHLDYCSMYTDHSVCSRDPECSWCQGACQAAPPPGTPLGACPAASCLGLGRLLGDCQACLAFSSPTAPPRGPGTLGWCVHNESCLPRPEQARCRGEQISGTVGWWGPAPVFVTSLEACVTQSFLPGLHLLTFQQPPNTSQPDKVSIVRSTTITLTPSAETDVSLVYRGFIYPMLPGGPGGPGAEDVAVWTRAQRLHVLARMARGPDTENMEEVGRWVAHQEKETRRLQRPGSARLFPLPGRDHKYAVEIQGQLNGSAGPGHSELTLLWDRTGVPGGSEISFFFLEPYRSSSCTSYSSCLGCLADQGCGWCLTSATCHLRQGGAHCGDDGAGGSLLVLVPTLCPLCEEHRDCHACTQDPFCEWHQSTSRKGDAACSRRGRGRGALKSPEECPPLCSQRLTCEDCLANSSQCAWCQSTHTCFLFAAYLARYPHGGCRGWDDSVHSEPRCRSCDGFLTCHECLQSHECGWCGNEDNPTLGRCLQGDFSGPLGGGNCSLWVGEGLGLPVALPARWAYARCPDVDECRLGLARCHPRATCLNTPLSYECHCQRGYQGDGISHCNRTCLEDCGHGVCSGPPDFTCVCDLGWTSDLPPPTPAPGPPAPRCSRDCGCSFHSHCRKRGPGFCDECQDWTWGEHCERCRPGSFGNATGSRGCRPCQCNGHGDPRRGHCDNLSGLCFCQDHTEGAHCQLCSPGYYGDPRAGGSCFRECGGRALLTNVSSVALGSRRVGGLLPPGGGAARAGPGLSYCVWVVSATEELQPCAPGTLCPPLTLTFSPDSSTPCTLSYVLAFDGFPRFLDTGVVQSDRSLIAAFCGQRRDRPLTVQALSGLLVLHWEANGSSSWGFNASVGSARCGSGGPGSCPVPQECVPQDGAAGAGLCRCPQGWAGPHCRMALCPENCNAHTGAGTCNQSLGVCICAEGFGGPDCATKLDGGQLVWETLMDSRLSADTASRFLHRLGHTMVDGPDATLWMFGGLGLPQGLLGNLYRYSVSERRWTQMLAGAEDGGPGPSPRSFHAAAYVPAGRGAMYLLGGLTAGGVTRDFWVLNLTTLQWRQEKAPQTVELPAVAGHTLTARRGLSLLLVGGYSPENGFNQQLLEYQLATGTWVSGAQSGTPPTGLYGHSAVYHEATDSLYVFGGFRFHVELAAPSPELYSLHCPDRTWSLLAPSQGAKPRPRLFHASALLGDTMVVLGGRSDPDEFSSDVLLYQVNCNAWLLPDLTRPASVGPPMEESVAHAVAAVGSRLYISGGFGGVALGRLLALTLPPDPCRLLSSPEACNQSGACTWCHGACLSGDQAHRLGCGGSPCSPMPRSPEECRRLRTCSECLARHPRTLQPGDGEASTPRCKWCTNCPEGACIGRNGSCTSENDCRINQREVFWAGNCSEAACGAADCEQCTREGKCMWTRQFKRTGETRRILSVQPTYDWTCFSHSLLNVSPMPVESSPPLPCPTPCHLLPNCTSCLDSKGADGGWQHCVWSSSLQQCLSPSYLPLRCMAGGCGRLLRGPESCSLGCAQATQCALCLRRPHCGWCAWGGQDGGGRCMEGGLSGPRDGLTCGRPGASWAFLSCPPEDECANGHHDCNETQNCHDQPHGYECSCKTGYTMDNMTGLCRPVCAQGCVNGSCVEPDHCRCHFGFVGRNCSTECRCNRHSECAGVGARDHCLLCRNHTKGSHCEQCLPLFVGSAVGGGTCRPCHAFCRGNSHICISRKELQMSKGEPKKYSLDPEEIENWVTEGPSEDEAVCVNCQNNSYGEKCESCLQGYFLLDGKCTKCQCNGHADTCNEQDGTGCPCQNNTETGTCQGSSPSDRRDCYKYQCAKCRESFHGSPLGGQQCYRLISVEQECCLDPTSQTNCFHEPKRRALGPGRTVLFGVQPKFTNVDIRLTLDVTFGAVDLYVSTSYDTFVVRVAPDTGVHTVHIQPPPAPPPPPPPADGGPRGAGDPGGAGASSGPGTPAEPRVREVWPRGLITYVTVTEPSAVLVVRSVRDRLVITYPHEHHALKSSRFYLLLLGVGDPSGPGTNGSADSQGLLFFRQDQAHIDLFVFFSVFFSCFFLFLSLCVLLWKAKQALDQRQEQRRHLQEMTKMASRPFAKVTVCFPPDPTAPASAWKPAGLPPPAFRRSEPFLAPLLLTGTGGPWGPMGGGCCPPAIPATTAGLRAGPITLEPTEDGMAGVATLLLQLPGGPHAPNGACLGSALVTLRHRLHEYCGGGGGAGGSGHGTGAGRKGLLSQDNLTSMSL
The following text describes a protein:
Function:
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Subcellular Localization:
Cytoplasm.
Sequence:
MAADPTPEVTELPANQEKNEEEAKQSQNDTTPADPEPAGFQLSIFIPRPNFCSEVNLTPSQPNADPEPESEYIELILPAHGPETIRELQQSVIESAEGWWLGSIGLASVELDPNGKPDPQQLSVRTVYGEFAELSSAFQSDKFKDPDAKRALLAINIDYTEYSARLHVIRLRDVLYSQAPGLLVGNPTPFPPYDPSQIGISGAVSLFPFVRGDQGTTGADSPACEQNLTDQPGTGPSKNKKKKKSSQPTSSIVNMPQAAPEPAAQESAIESLGNYRFNSSNPFGVFSSLMGEQSEPREPNLSARYLKSFALSTWNSPPHHYRLRGHYLYLAITTFENVSYEITCHTKGFYVNKSTKTQFDPSPSSDSSPDSVYFHTLTQLICTLSPAFVKQVTQTWNRALNPAFPDFFTSISITNCLPAFPWLVNPEKPSPDAIRSQLAYLITGSTTAETLPPARDWADEFAQARELPRKSLAERILRERIWSRLQSDFSMAATRGVISCSRGEVPALNPQEPESAWTYVLNNILFSRAEDPIGAYEHLGGTAAARAIASKDLHSIKYLNQLDVPGIYTMGSAVVDYHGKRWIAQGMIPGIFRPPDLEAEKAQQDLAAQQSQINGHSTPDDKDEGDWEKVNRSLPVTPQLGTVAVPEEVSPPTTYDILYGSADIEKPEMGLRSDPKFHRLAAQVAAGFNLSEHDVIDVNGRTHRLWLSADVHGIRATDGRCYLIDLYRMAPLDVSFIENDIDGPILDGKTPISEPAVSKTSAKPTQDTFPHRFTVVRTEAINAFKQHKFRQFALNHIKKHKQQQQASQATADSKTDGKPIEASTEGLGEDVVVDPDMSTDDGSDASVKENFEFGLNPDAFVDRKDQPWTLPQDKEDQGMALVKELSKYVREQLLVTVVQDLSEVKGLPADGRRLSDFLHSRGVNIRYLGHITHRLQLLATALSASPDNKTDQNVILNASIGLLQSEMVFRACKHILNEMLLNTSENEACHCISHFLNCLLGQSAAVPSSEQHLDSSSTWRTCTRHSLRSLITSSIRRRFRYALPNSYFTQRLPRTKIQLLREICTRMGIQLCLRDYNLCSPLPEAITNGHAQVVNEQVQKNAETVQATEEPVPATNGHTNCTDDENSTEGATPNESAAPSAPKQLKKKKKSKSKKGTASSSGSADGQTFSPSDILNILPIVRDSTCRSSVADELYAEGRKAFSNGDIALGQELCTDALTTYEQVFGSVHPEMCRHWHSLAILYHQLSQRTLVELSEYNDRLLELSAIYHSASNEEDREKVKERIESYQRDREPEALKNEIDTYIQLAANNLRRVSSWLNVL
The following text describes a protein:
Function:
Required for correct functioning of the GINS complex, a complex that plays an essential role in the initiation of DNA replication, and progression of DNA replication forks. GINS complex is a core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built; The GINS complex plays an essential role in the initiation of DNA replication.
Subcellular Localization:
Nucleus.
Sequence:
MPLQTSYFPDYFSVDDILATQEKIPCKFIQNVPKLGKLNPATEDPDLQSGTVLEMPLWLVLEASLMRQPIVTADLPKVYKDAYLEILKADPCAVDLHKFGVYFYELGSYMKQFGQNDDIAKTLLHTFTLRFRQIMDLSDNVISDPNVIQKLDALEKSLYESGHDAKMKLFSWLKMSEIPLEAATMVTNHKKRKRVDEDLF
The following text describes a protein:
Function:
Possesses 5'->3' exoribonuclease activity. May promote termination of transcription by RNA polymerase II.
Subcellular Localization:
Nucleus.
Sequence:
MGVPSFFRWLQRKYPLVVSRVLESDVDVDPLESNPNTIGSQEFDNLYIDMNGLIHSCFHPADREQPKNIEEVYENIKLYLKRIFNIVRPRKLLYLAIDGVAPRAKMNQQRSRRFRAAKDSEYNRNKNFQELITLGKQKEAEKIMKEQYIQDHDSNIITPGTKFMCDLSQILRSFISEMQNTSPAWSNIAIILSDASVPGEGEHKIMEFIRIQRLTDGYNPNTRHVMYGLDADLIFLALASHEVYFSILRENIFDKKENDKPIGPSSFIFANIFVLRQYLDRELQIDVKFGWDLERVIDDIVFLCFAAGNDFLPQIPGFEIPRGFVDQLFERYKKLLPQLSSYITNTGDVEMKNLLPFMLGFDYLEPESVHNIVSPSERSISVSEYVNNLCNDVKTEYKPENDKKLVTAKFQKNQNNLEIYDTKRDKKFYYQSKFGFEDEENIKNVVHEYCKGMEWVLKYYTKGVASWSWFYPYHSAPLVSDFVLLDCDVKNEFVLGHPFTPLQQLMAVLPPQSSWCLPKMMCDLMNSDDSPILDFYPKKFKVDLEGGTTAWKGHVLIPFIDAHKLKKCLRNVNDSLNEEEKQRNSFGVTFLYNKLQKVTILGTITEYSEGYENECIYELPPYDSNDPRINQILEGAEIPLINLDSQKIIEGKRVKTLKQMFNQTKKEENLLVVPGIPFDQPEDFRIREMQKTNSVSHKKSSKQGKSIFNF
The following text describes a protein:
Function:
Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5-bisphosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Miscellaneous:
MISCELLANEOUS: It is proposed that Thermoplasmatales adapted the classical archaeal mevalonate pathway by replacing mevalonate 5-phosphate decarboxylase (MMD) with two specialized enzymes (mevalonate-3-phosphate 5-kinase and mevalonate 3,5-bisphosphate decarboxylase) in order to produce isoprenoids in extremely acidic environments. It was found that at low pH, the dual function enzyme MMD is unable to carry out the first phosphorylation step, yet retains its ability to perform decarboxylation.
Sequence:
MNSRIMFIGGVPGVGKTSISGYIARNTDIDIVLSSDYLREFLRPFAPQESHLETSVYDAWKFYGDMSDDNIIRGYLDQARPIMGGINRVIARALANGEDLIIESLYFVPDMMDEMVLKNAFLAYVYIDDPDLHRSRLEDRINYTHRNSPGSRLAAHLKEYRTIMDYSMDMARGRGIGLYSTDDYALARQRLLDDFRKFVDRR
The following text describes a protein:
Function:
May be involved in a process influencing telomere capping.
Subcellular Localization:
Vacuole.
Sequence:
MSQSNSHGQSNLAKFAFNIYGTLSTNSSTPQSHEISPSSSLSSSRSKKQTSQYNTQDTNNNRLSYYCDKEIISLSQLNCSLSIGGYSGDLQHHVVIGGKNYLRLLCVSESQQRIISGINLLESKSIYNSRAPNKLINVNTIKTFADTIATGLSNGVVSIYKISPNGQSKVTGKYSDHNRTINSLDFIESENQLLSGSQDGTIKLWDLRSSSTKPVMTVQANLHSDPIRACQYSPHSAVRNKICVLSVHDSGALCKFDLRTKSGGKVYSPEKKWNLHTGPALSLHIHPEKELVVTGGRDKRISIFNYGERQSRNTPQNLINTYGPVVKVRWSTYTNTEETAEEFEENKQAKPNTLYNYDIACSYLNDDPTITIYNLGRKFIPKQIIHSKKPIQNFIWARNETRSRKIWTISKSSTFSSYNLDRLEDSDVSRPIEDLNNIAMTWDNNNDFCAVSQARYDYDLETYENGINETTEENFDAERNYSLGNEELIHSQANSLTASPVDKPQLTRSLTFNPASSFSTFSPVLVARAATGFLQNDSATSSSSIPNMQVSSSRPKLTRNTSQTTQDSSSSQFASVLPPPSASQTYSSPQYKKNNPPRFMNNPAYVIPVSIPIPANDEYVFRKLSSESLVSTPDGFTLVDVCLLNASVAASVGNNRTSQIWRLLAVSIQEEFESGIEPRRIYAFQPEAINKLPQDVQETSTNANDTLHAETTNSNFVESFKSTSTSGSQFGKQSDKDERKLQSKNSSGNLMDMINKANRTNSFSATSFKFKEQERKEDESQKAQSIKDENERASIHSKSAPISISSHPEDLDDENMGSNNSAALKFSPPSVGVSIPSTRIISSSLASSPKSVRGPSGVKSHISRSRPSPPVQTWLKQKNLEVSNGSAMASTSGLSLTLKRNKTNEEGDQLTKAWKFKSLLRKSLDYATLQGDIIFCSTAALLFYDIVPEIISQFECLEWLGIYIEVLQRKRLFVNAINVIKCATADIQEKLQKLYCQDLSLRFYCSNCQALLVNEKSKFSGKGEFGYWYCDECSKLQSQCVYCNEPCKGLAVTVGLKCGHHGHFGCLKEWFIEDQNTECPGGCGYQII
The following text describes a protein:
Function:
Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation. Contributes to proper membrane localization and stabilization of caveolin-3 (CAV3) in cardiomyocytes. Induces RHOA activation and activates NPPA transcription and myofibrillar organization through the Rho/ROCK signaling pathway.
Subcellular Localization:
Cytoplasm, myofibril, sarcomere. Cytoplasm. Cytoplasm, cytosol. Cell membrane, sarcolemma. Membrane, caveola. Note=In cardiomyocytes, accumulates in the Z-line of the sarcomere. In vascular smooth muscle cells, detected diffusely throughout the cytoplasm. Localizes in the caveolae in a caveolin-dependent manner.
Sequence:
MEHNGSASNADKIHQNRLSNVTEDEDQDAALTIVTVLDKVAAIVDSVQASQKRIEERHRVMENAIKSVQIDLLKFSQSHSNTGYVINKLFEKTRKVSAHIKDVKARVEKQQTHVKKVEAKQEEIMKKNKFRVVIFQEEVQCPTSLSVVKDRSLTESPEEVDEIFDTPVDLSSDEEYFVEESRSARLKKSGKERIDNIKKAFSKENMQKTRQNFDKKVNRIRTRIVTPERRERLRQSGERLRQSGERLKQSGERFKKSISNAAPSREAFKMRSLRKTKDRAVAEGPEEVREMGVDIIARGEALGPISELYPEALSETDPEEASATHPPQEGGEVSTPEPLKVTFKPQVKVEDDESLLLDLKQ
The following text describes a protein:
Function:
Exhibits strong arylesterase activity with beta-naphthyl acetate and phenyl acetate. May play a role in adipocyte differentiation.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSEADGLRQRRPLRPQVVTDDDGQAPEAKDGSSFSGRVFRVTFLMLAVSLTVPLLGAMMLLESPIDPQPLSFKEPPLLLGVLHPNTKLRQAERLFENQLIGPESIAHIGDVMFTGTADGRVVKLENGEIETIARFGSGPCKTRDDEPVCGRPLGIRAGPNRTLFVADAYKGLFEVNPWKREVKLLLSSETPIEGKKMSFVNDLTVTQDGRKIYFTDSSSKWQRRDYLLLVMEGTDDGRLLEYDTVTREVKVLLDQLRFPNGVQLSPAEDFVLVAETTMARIRRVYVSGLMKGGADLFVENMPGFPDNIRPSSSGGYWVGMSTIRPNPGFSMLDFLSERPWIKRMIFKLFSQETVMKFVPRYSLVLELSDSGAFRRSLHDPDGLVATYISEVHEHDGHLYLGSFRSPFLCRLSLQAV
The following text describes a protein:
Function:
Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.
Domain:
Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity.
Sequence:
MVHSESSILSSLRGGDGGGIPCSKDELAINGSYTDPMGRRKSKRFKVAAESEFSPDFGSITRQLRSRRMQKEFTVETYETRNVSDVCVLSSQADVELIPGEIVAERDSFKSVDCNDMSVGLTEGAESLGVNMQEPMKDRNMPENTSEQNMVEVHPPSISLPEEDMMGSVCRKSITGTKELHGRTISVGRDLSPNMGSKFSKNGKTAKRSISVEEENLVLEKSDSGDHLGPSPEVLELEKSEVWIITDKGVVMPSPVKPSEKRNGDYGEGSMRKNSERVALDKKRLASKFRLSNGGLPSCSSSGDSARYKVKETMRLFHETCKKIMQEEEARPRKRDGGNFKVVCEASKILKSKGKNLYSGTQIIGTVPGVEVGDEFQYRMELNLLGIHRPSQSGIDYMKDDGGELVATSIVSSGGYNDVLDNSDVLIYTGQGGNVGKKKNNEPPKDQQLVTGNLALKNSINKKNPVRVIRGIKNTTLQSSVVAKNYVYDGLYLVEEYWEETGSHGKLVFKFKLRRIPGQPELPWKEVAKSKKSEFRDGLCNVDITEGKETLPICAVNNLDDEKPPPFIYTAKMIYPDWCRPIPPKSCGCTNGCSKSKNCACIVKNGGKIPYYDGAIVEIKPLVYECGPHCKCPPSCNMRVSQHGIKIKLEIFKTESRGWGVRSLESIPIGSFICEYAGELLEDKQAESLTGKDEYLFDLGDEDDPFTINAAQKGNIGRFINHSCSPNLYAQDVLYDHEEIRIPHIMFFALDNIPPLQELSYDYNYKIDQVYDSNGNIKKKFCYCGSAECSGRLY
The following text describes a protein:
Function:
Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis. Involved in stress granule disassembly: associates with ubiquitinated G3BP1 in response to heat shock, thereby promoting interaction between ubiquitinated G3BP1 and VCP, followed by G3BP1 extraction from stress granules and stress granule disassembly.
Subcellular Localization:
Cytoplasm. Lipid droplet. Endoplasmic reticulum.
Sequence:
MLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALSDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREERERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPDSVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE
The following text describes a protein:
Function:
High-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTGKDSVVLVDKDTVPQIMATGEKKGAMVTLATVESQPNKAAERGKAMRQVIAAFVANIGTINTGLIFGFSAVVIPQLQAADSLIPVDESQSSWVASLSAIGTPIGCLLSGYVMDNFGRKKALIATQIPTIIGWIVIACASNVGMIYAGRVLTGFGSGMVGAPARVYTSEVTQPHLRGMLCALASTGISLGVLIQYTLGAFTTWKFLSGVSIIVPVAALILMLLMPETPNYLVSKQKPEKARRSLARLRGSSYNIDREVEQLQSFAAKTNASGKKSLSLRETVQALVHPSCLKPFAILTIYFMMYQFSGVNTITFYAVEIFRDSGTTMDKNTCTILLGVVRLIFTIVGAILLRRCGRRPLTFISGIGCGFTMVGLGVYLYFKHQWDTAVPPIEPTATWFPVACIFIFITTCTVGFLVVPWVMIGELYPMKVRGLVGGFTTCMAHSFVFIVVKTYPFLTHVLERHGTFILYGCFSFVGTIFFYLCLPETKGKTLQEIEDYFSGRTKTLKKPKAGTNGQQNDENDGQQMLLANGTKPAVLSPEKNKLLP
The following text describes a protein:
Function:
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Involved in the mating pathway.
Sequence:
MGGCMSTPEAPKKTAETKQVPSTSTSSRPPQASTSATATAAGAGTSAANGTANGIKGDTTATNRVGTSGGQGLAAALASTEPPGAQDSKGNKDRSNQIDRQLEDDQKKFRKECKILLLGSGESGKSTIVKQMKIIHQNGYSKDELLSFRGVIYKNVLDSAQALIMAMRKIGVDPEDANNRSYADRILEYRMDAGLDAVIPSEILYNIESLWHDPVIPSVMDRSSEFYLMDSATYFFANIRKIAGPDYVPDEADVLRARTKTTGISETRFNMGQLSIHMFDVGGQRSERKKWIHCFEAVTSIIFCVALSEYDQVLLEESGQNRMQESLVLFESVINSRWFLRTSVILFLNKIDLFKQKLPKVPLVQYFPEYTGGADINKAAKYILWRFTQTNRARLSVYPHLTQATDTSNIRLVFAAVKETILQNALRDSGIL
The following text describes a protein:
Function:
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Together with FL/APO2, involved in the temporal regulation of meristem identity during both vegetative and reproductive developments in an APO2-dependent manner (By similarity). Promotes spikelet formation by suppressing the precocious conversion of inflorescence meristems to spikelet meristems, probably via a positive regulation of class-C floral homeotic genes, but not of class-B genes, and through the control of cell proliferation in meristems. Mediates culm development and strength/diameter enhancement at internodes. Required for the regulation of the plastochron, floral organ identity, and floral determinacy (By similarity). Controls the number of primary rachis branches (PRBs). May trigger the formation of vascular bundle systems which, consequently, promote carbohydrate translocation to panicles. Involved in ozone-induced grain yield regulation.
Miscellaneous:
MISCELLANEOUS: Ozone has various impact on different cultivars; O.sativa subsp. japonica cv. Sasanishiki exhibits ozone-induced leaf injury, but no grain yield loss, and, by contrast, O.sativa subsp. indica cv. Habataki has grain yield loss with minimal leaf injury upon ozone treatment; MISCELLANEOUS: Plants harboring the PBN6 quantitative trait locus (QTL) (e.g. HI1 allele in O.sativa subsp. indica cv. Habataki) exhibit bigger peduncle diameter due to larger vascular bundles and an increased number of primary rachis branches (PRBs) and of the number of grains per panicle, thus leading to increased grain yield; MISCELLANEOUS: Plants harboring the SCM2 quantitative trait locus (QTL) exhibit both an enhancement of culm strength at internodes and an increased spikelet number leading to higher crop productivity and better grain yield.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The F-box is necessary for the interaction with ASK proteins.
Sequence:
MMNPRRLPPLPSSTSSASAADDMDPRVWRRLPQPLVDRVLACLPTPSFLRLRAACRRFYHLLFSSPFLHSHLLLSPHLPFFAFVVPAAGHLLLLDPTATASWSRLPLPLPPVAGGPAAFSPAAASAGLLAFLSDASGHKTLLLANPITRLLAALPISPTPRLSPTVGLAAGPTSIIAVVAGDDLVSPFAVKNISADTFVADAASVPPSGFWAPSSLLPRLSSLDPGAGMAFASGRFYCMSSSPFAVLVFDVAENVWSKVQPPMRRFLRSPALVELGGGREGAARVALVSAVEKSRLSVPRSVRLWTLRGGGGGGGGGAWTEVARMPPEVHAQFAAAEGGRGFECAAHGDYVVLAPRGPVAQAPTSALVFDSRRDEWRWAPPCPYVVVAHHGGAGAAGFRVFAYEPRLATPAIGLLDATAPVALHGMHDG
The following text describes a protein:
Function:
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation. The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron. May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface.
Subcellular Localization:
Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus.
Sequence:
MAAVELEWVPETLYNTAISAVVDSYGRARRRDIRSLPENIQFDVYYKLYQQGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCFQALMDHGVKVASVLAYSFSRRCSYIAESDSAVKEKAIQIGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLHDEILHWFRAVECCVRLLHVRNGNCKYHLGEETFKLAQSYMDKLAKHGQQANKAALYGELCALLFAKSHYDEAYKWCIEAMKEITVGLPVKVVVDVLRQASKACVVKREFKKAEQLIKHAVYLAREHFGAKHPKYSDTLLDYGFYLLNVDNICQSVAIYQTALDIRQSVFGGKNIHVATAHEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHILPEDHLLLASSKRVKALILEEIAIDCHNKETEQRLLQEAHDLHLSSLQLAKKAFGEFNVQTAKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQLLGQEDYEVALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKLFGEGYSGLEYDYRGLIKLYNSVGNYEKVFEYHNILANWNRLRDRQFSVTDALEDVSSSPQSTEEVVQSFLMSQNVDGQSS