lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. ERG8 converts 5-phosphomevalonate to 5-diphosphomevalonate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Miscellaneous:
MISCELLANEOUS: Present with 79 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSELRAFSAPGKALLAGGYLVLDTKYEAFVVGLSARMHAVAHPYGSLQGSDKFEVRVKSKQFKDGEWLYHISPKSGFIPVSIGGSKNPFIEKVIANVFSYFKPNMDDYCNRNLFVIDIFSDDAYHSQEDSVTEHRGNRRLSFHSHRIEEVPKTGLGSSAGLVTVLTTALASFFVSDLENNVDKYREVIHNLAQVAHCQAQGKIGSGFDVAAAAYGSIRYRRFPPALISNLPDIGSATYGSKLAHLVDEEDWNITIKSNHLPSGLTLWMGDIKNGSETVKLVQKVKNWYDSHMPESLKIYTELDHANSRFMDGLSKLDRLHETHDDYSDQIFESLERNDCTCQKYPEITEVRDAVATIRRSFRKITKESGADIEPPVQTSLLDDCQTLKGVLTCLIPGAGGYDAIAVITKQDVDLRAQTANDKRFSKVQWLDVTQADWGVRKEKDPETYLDK
The following text describes a protein:
Function:
Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. Promotes clustering of HT2RC at the cell surface; Scaffolding protein that facilitates the localization of proteins to the cell membrane. Required for the correct formation of tight junctions and epithelial apico-basal polarity. Acts (via its L27 domain) as an apical connector and elongation factor for multistranded TJP1/ZO1 condensates that form a tight junction belt, thereby required for the formation of the tight junction-mediated cell barrier. Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells. Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration. May regulate the surface expression and/or function of ASIC3 in sensory neurons. May recruit ARHGEF18 to apical cell-cell boundaries.
Subcellular Localization:
Apical cell membrane; Peripheral membrane protein. Cell junction, tight junction. Cell projection, dendrite. Cytoplasm, perinuclear region. Postsynaptic density. Synapse, synaptosome.
Sequence:
MPENPATDKLQVLQVLDRLKMKLQEKGDTSQNEKLSLFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCTANFDFSRKGLLVFTDGASTSGNAHRSTNNQSVSGLFPWTTKLGNEDFSSIMQQMAQGRHIESIDIERPSTGGLGFSVVALRGQNLGEVNIFVKEVQPGSIAGRDQRLKENDQILAINHTPLDQNISHQQAIALLQQTTGSLHLVVAREPVHTKSSASTSLTDVTLPETVRWGHIEDVELVNDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGGTNVQGMTSEQVAQVLRNCGNSVRMLVARDPIGEVSVTPPTPAALPVALPAVANRSPGSDSSTPCETYDVELIKKDGQSLGIRIVGYVGTTHTGEASGIYVKSIIPGSAAYHNGQIQVNDQIIAVDGVNIQGFANQDVVEVLRNAGQVVHLTLIRKRTSSSASPLEGNSDRGTVVEPLKTPALFLTGAVETETNLDEDEETEERIDNLKNDNIQALEKLEKVPDSLENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRTTEASLPAMEANRNIDVHTEEDDDGELALWSPEVKTVELVKDHKGLGFSILDYQDPLDPTRSVIVIRSLVPDGVAERGGELLPGDRLVSVNEYCLDNTTLAEAVEVLKAVPPGTVRLGICKPLVEEKEEESNILYSNNNEDKTETSGTIHGLNSSLILEAPKGFRDEPYFKEELVDEPFLDLGKAFQSQQKEIDTSKEAWEMHEFMAPRMQEMGEEREMLVDEEYELYQDHLQSMESYPSPHIQEAAPVPSMKELHFGAQWFCDHELPEPQEARSVMSVYSQEMQQCGYSAENTMKENVGIDSLPSMSSTEGNSPRGRFDDLENLNSLTKSSLDLGMMIPTDVQGPGLLVELPAVAQRREQEDLPLYQLPRTQAVSKASAYTGILSSRYATDPCELPEREEGEGEETPNFSHWGPPRIVEIFREPDVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNALKTGDKILEVSGIDLQNASHKEAVEAIKNAGNPVVFVVQSLSSTPRVIPSAHNKTNKIANNQDKNTQEKKEKRRGTAPPPMKLPPPYKAPSDDSDETEEEYAFTNKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAAKDGRMRIGDELLEINNQILYGRSHQNASAIIKTAPSKVKLVFIRNEDAVNQMAVTPFPLPSSSPSSIEDQSGTELVGSEEDGSVEVGIRQLPESASSKLAGSQSKQQKYSTKVSFSSQEIPLAPASYHSTDADFTGYGGFQAPLSVDPATCPIIPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGIDLRSASHEEAITALRQTPQKVRLVVYRDEAHYRDEENLEVFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDGRLIQGDQILSVNGEDMRSASQETVATILKCAQGLVQLEIGRLRAGSWTSSRKTSQNSQGSQNSTHSSFPPSLAPVITSLQNLVSSKRPSDPSPKGSGTDVGPRTVEIIRELSDALGISIAGGKGSPLGDIPIFIAMIQASGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRIILQVVADTNISAIATQLENMSTGYHLGSPTTEHHPEDTETPPPKIITLEKGSEGLGFSIVGGYGSPHGDLPIYVKTIFAKGAAADDGRLKRGDQILAVNGETLEGVTHEQAVAILKHQRGTVVLTVLS
The following text describes a protein:
Function:
Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.
Miscellaneous:
MISCELLANEOUS: Present with 5910 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MPLSQKQIDQVRTKVHYSEVDTPFNKYLDILGKVTKLTGSIINGTLSNDDSKIEKLTEQNISQLKESAHLRFLDLQSSIDTKKVADENWETCQQETLAKLENLKDKLPDIKSIHSKLLLRIGKLQGLYDSVQVINREVEGLSEGRTSLVVTRAEWEKELGTDLVKFLIEKNYLKLVDPGLKKDSSEERYRIYDDFSKGPKELESINASMKSDIENVRQEVSSYKEKWLRDAEIFGKITSIFKEELLKRDGLLNEAEGDNIDEDYESDEDEERKERFKRQRSMVEVNTIENVDEKEESDHEYDDQEDEENEEEDDMEVDVEDIKEDNEVDGESSQQEDNSRQGNNEETDKETGVIEEPDAVNDAEEADSDHSSRKLGGTTSDFSASSSVEEVK
The following text describes a protein:
Function:
Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MTTAVSSPDEQEGLRQQSEHLHHLFPAPPISSALGTPKPCAPDPPPRSLAWGAVRKLRRTQGQGCAAITWQVLEACNQDTREHNDGRPPAPRVCACCSLVADGAVPGTTQWGPCQLQWGEGVAGQPLGAAPTFLQQRFTFSVHWSDDSDTFVCRSWDEFRRLNKTLKETFPEEAGLLRRSHRVIPKLPDASLLVRSGRTGRGLAHLRQLDTYLRTLLAAPEHVSRSPTLTSFFEPQPSDLDPTLPPGSLVILPAPEEPLHRPAGSLAIRSLKAQSLRCLQPFHTQDTRGQPFHAQAHEALNVLLRHPSGWWLVENEDRQTAWFPAPYLEAAALGQGRERGVPLGNSGSQFCASCAYESSQADELSVPAGARVHVLKTSDRGWWLCRFRGRAGLLPAVLLRPDGLGALLSGPGLHCGANSGEDGAGEARSSPEPFQTMTIPPTVPARPPLSAIQSRCCTITRRALGQDRRDQGHP
The following text describes a protein:
Function:
Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Sequence:
MATEKVLTKGDADAIAVVALELPSDNASGSNVEKAGPESRRPMATKRALIAWLVLCFSTGPTAGMAFRYVPAVLQSAANVLGHIPGTNKPCAKRGVIRCVVPFGTGEVDYNSYIASEGVVCIFISGVADFTHNRKNLLILGIVLFGTFALPFASMTSKTYRNLVSGSILWVFMTTVQGIYGTLSSSYIPLFMREAGWIQARTRIGQDGRLVVTEEERATKELFNRGTMVSVLGLLSGNVGSILGQGIELLKSIPKYPEAFKLCVGWVLWNTGYSNFNSVIGLLFREVSGLGTGDRLYTVYTFMAVTTASIGSLTWMFVFPRTNIKIKTWAYCFLAINIFCIFWGCLGIGKNVKIGYKYVPEFWIEQTLFCMTSSALRSANRVMYASMLPRGREAHFFGLELTLDLATGWVNPLVQSVIQDKTHNLRYPMLPNFFLLVAALGFYIWCDLEKGVKDSLKEFDDAAPAVDDGT
The following text describes a protein:
Function:
Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Sequence:
MTFVSASLAEKIRNLCFDHYKNRLSGNGKPKTGSEWTVMSAIVMQLHNSKRCCIFLYDELEYALKDKESIFQCIGEKFRLCEDVEFHFFTTSMPCGDASIIPKSKLSCSYEIINNENIGEVVVDNPSKKRSLDDSTEGAANKKFKIGDMPSGDIYRTGAKCMKGEDKHLPGKDYHVVGVLRTKPGRGDKTKSLSCSDKLCKWNVLGIQGALLMHFLAEPIHIKSYIINSSIFDETALLRSLSMRLEDKPVLPEAYSMCKFLIFNIHDDKFEHSRSHSSNSSPCPTTICWYYNNDKQFKQDVLTRGCLLGLTKKDKSSKKCSFVAKLSLFKKFQQLKQLHSKRFHDSKLSTLKLETYSEFKQASNDYQLAWKILKSFNVFRNWPDTYSNFHNFVV
The following text describes a protein:
Function:
Transcriptional inhibitor with a significantly increased number of target genes in response to oleate.
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion.
Sequence:
MMPLKKRQRQTLVCSNCKRRKSRCDRGKPACGNCIRLGNRETCHYFISPSEKGGDGGDSPGESAGSNGALERWQFVRAHSCGRVDLTAGRTVVFGKRSAVYVAGVLSTDAVRYRDLYLELLSVFSHAAIKKTVSQLHAQAQVGAQEASLPNSVKRVIRMEDEGMLQESSPYILAKHKKVHQSLVDGFAQSRYEGRQQFADVEEAAKQHLVERYIFLQKVLPAFKKHVLPLIPIYDERMLCVTVEQLYDDYQKRGKFSAKNGDLITVATILLITRLVYLAIRFDKCSVVNVKYNRILELDTEPYAALAYELLPRDKLLRKVTLPQLQCLILLRFHNWCSPMDGDGESLQYSNVLMGTIYACCKEIGASWLSFKEPDKYDFAKARGSNSRFTMAFAEMEPGEVDSANESVVKLYQQIWAVVLHWDRNVSMLTGLEPIIGTSMKPAAMSSYNNWYADMISLDYLKWQLLTRINEDPSEVNLEEVKPIISEIRQRLGQFTSESELAFEQELILQLVELSILHAAFIGPTSNVSAAEHRKNYQELLERIIHLSGIFITYFHDPPTTNHQYGRFYTNKIVEVAMYRVYQILTGLILRISSACQDQSLKPTLMKFYKNLCSLYFNELGYDYYQVFKRLFEAKVKYKILEQTANPVFIMLRYLFAEIQSGNMESMKSQELIGLIYGEYKKMGGELNLDMMDLWNHIVPTQCDHNIGLNSLFTTEIFPTDQYSDYNLFVSFYDYASNKLTEDTNQAAEKSIAHNPSTSIHDLCKGGASPHFDLLEGILDPLDFMTYLDSIPGET
The following text describes a protein:
Function:
Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.
Subcellular Localization:
Secreted.
Sequence:
MASFGLGLLLLLLLLTTHPGSSKAQHWSHGWYPGGKRASSSSQEPQHAPWLPGRVLGTAAGSPGQIAHSLPSNALAPPEDTVPWEGKTMVQWLLRGKQHLVQKLLTRPRRCAPLPSNKV
The following text describes a protein:
Function:
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
Sequence:
MSGTKWTDEQRQAIFTKDCNLLVAAGAGAGKTAVLVQRIIEKILDKGEPIDIDKLLVVTFTNAAAAEMRERIGDAISKGLDEDPESKVLRKQLTLLNKSNIMTIHSFCLQVIKNNFHTMEIDPNFRICDETEGILMKQEAIDELFDELYEIENEDFINLVESYASRKDTRLQEVVLELHRFAKSAPFSYDWLLNMAEEFNVGEEFNFEETPWADMIMEDMKVLLHGFKNMLQQSIDVILNSEGIDYYYEPFKMDLSFINSLLEKSSFKEFRGEIIAYDFPKLPLKRNKDADKEAKERVKKLRDKVKKKIVELKNILDSYENEFIKKEFIFLYPSMKALSNLVILFDKKYEAKKRERDLIDFNDIEHLCLSILTDKNSEGHIIPSDIALDYRKKFAEVLIDEYQDSNLVQEVIMSMVSRVKGYWSFYNGQLMFNEEEINLEEPQICLDIPNRFMVGDVKQSIYRFRQAKPEIFLDKYNEYSEEEGTKNRKVKLFKNFRSRKEVINGVNYLFKQIMSKTIGELDYTEEEALKVGASYGEEVKGEPIELCLMDKKYEISEEVLKEYNVDEEEALDNIQLEGRLVAKKIQKLVGNNLEGGLKVFDKKLGEYRNLQYRDIVILMRATSNWAPIFVEELAKEGIPVFADTNSGYFDTAEIKTMISLLQIIDNPLQDIPLLSVLRSPIASFTDDELIDIRMVNKNITFYECMEIIYRLYKNEKLDSYYSFYIEDENKINKIIKDMNEKLKNKICSFIEKLKLWREKSIHIDIDEFIWFLYVETGYYGYAGALQAGEQRQANLRILFQRAKQYAKTSYKGLFNFINFINKLKFSSGDMGSAKILGENENVVRIMSIHKSKGLEFPVVILSGTGKNFNMTDLNKNILFHRDLGYGPDYVDTERRIAYPSLVKNIIKNKIRLETLSEEMRILYVALTRAREKLIITGLINNMDKTVEDWLNLSEDKNKVPEYAVMSGKTYLDWIGPALIKHKDAVSFREELKMTSELSNIVDDKSKWKIELWNKRELLKEKVEEDEVEISEKIKETLMNLEESNYKEEIYKRLSFKYKYDNASSIPTKLSVSDVKKQFILDEKENTEELFKKLELRKPMFMEEKKKISPSERGTIIHLFMQHLDLKKAENEEDIKEQINRLIEREFITYEQSKVINPYKILKFCRGELGKRILNSNNVNKEMPFSIEIPALEIYKELDKEIYKDEKLIIQGVIDCYFEEEDGLVLLDYKTDYVNDIEEIKNRYEIQIKYYEEALNRITGKNVKDKYLYLFSVDNYIKID
The following text describes a protein:
Function:
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Sequence:
MNKGSKIAVLGVSGLVGSALVRKLLERGYEKVIGTYKSRKPNFEDIQLFQVDLTNQSETETFFAEQAPEYVFLAAAKVGGILANNTYKAEFIYENMAIALNVIHSAYKYGVNKLLNLGSSCIYPKHAPQPLKEEYLLTAPLEPTNEPYAIAKIAAIKLCRYYNEQYGTNFLSVMPTNLYGPNDNFNLETSHVLPALIRKFHLAKLLEEGDIEGIKRDFQKYPIGFGLDEKLDLSDKSLISQILNHLGIKFSNSANNFENRTFKNVIVTMWGAGKVYREFLHVDDLADACVFLMENVDAWSLSPYHPKIKIEHRAFNLEPMLPDYLINIGTGEDLTIDELAHTIKNIVGFRGDINYDTSNPDGTPRKLLDVSNIKRLGWSYKIGLKDGIKRVYEWYKDNL
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:
MMHPRVKLVSLLVLVVLLQQCARAQIINRTPHFIPGSGDMARFSLLENTPVGSVVYQLRGVDPEGSKLRFSISGPVFSVDRDSGVVRLRQSLDREQQDTVEVIISLTDEGVLGTEPNTVSLRREIPIRDYNDNPPVFVGRPYSATISEATKPGSNVTVTPDIVATDQDEGANAELTFSCYQDPAKGADDICDVFTVHTEKIAQGKFGAWIELRRPLDFETRPSYILTIQARDGSPTNSLRAVASVAITILDVQDQPPIFINAPYSATIPENTIEGTRVLTINATDGDTGSPNPLMLMLENEPMGHFKLNYIGHPRSGVAELITTGKPLDREDPIITQNGGAYTFSIRATELINNELPGDSTTSQITIVLTDVDDHVPEFSQPAYEVSIPENLEQDTPLPGLAIVVTDRDLGPNSHYTLALRNLHNSEGVFAVVPTQGEGRTPIVVKVLDSSRLDYDVPSEEAKTFRFQLVASVDGEEKSTANVTVRLQDANDNSPTFPQASYSLQVRENSPQGFKIADLSATDHDAGMFGQLAYAVKGFGAEFFRTHPTEGGLYVERQLDYEEQKSYSLALVARDGGGRETNANVFIDVMDENDNHPAFEALEYTRTIREGATEFEPQFFVRAVDVDGPTQGGGRVSYAIESENSISGHVFTVDRDSGEIKITRPVSSMDTDRGQYELLVVATDHGVPPLKNDTRVLVRVGLSGNQRPIFRGHATAGNRDIPGPPSYRASIPENAPAGYNVTQVSATDPDGLDELLRYKIVGASDNFVINDLTGLITVTRDARLDRDTNPESYAIVVNAIDAGFPIPETATTTVHVKIQDINDKPPKFTQQSYTAYVSERSAIDSEVLRVTAKDTDLSARIEYTLVEPITAVTKGGIPLLTTSSYDYRQAFRIDRDDGTIFVNSTLNYNYAAVITLTVRATDTAAELYPERQFDQTEVTLYVQSFKDTNPLFRNKGWSTVRPKIEVKVKEEAPVGSVVFRIEADDPVADVPITDFELMMPDVDGIFGLNERTGEIMLLQRLDYETYNKTTIDFVVKAITSNRKRHSLAYVNVTVENVNDNAPVFERDSYRVTVLESDRYPHVVTTVSATDQDVVRTEKDTLLGYNVIRYSLFGSHSNLFTIDNQTGEIRIGPGQVLDREKQSVLKLIVVAEDAPGRPQDAKKATTEVMVDVLDVNDNAPIFGQRSYTAVIPENVLVDTFVIAITAHDPDEGLGGEVRYDILNEGEANGLLQINPKTGEIKTKAMLTGKGRAEPYELVIRAQDSGGQLPKQSSLYNDVSFTLYIGDISANDGIPFFIAPQVGQTANVTENATVGAPVFQVIASDPDSPATPSGTLRYRIQSDIEDAKSFNINAKTGLITTTRSLDREIKSAYNIIIEVSDMGEPPQASTVVLRINVLDIDDHEPRFVREVEAQPYELEVLEEQPAGTIVGNVSALDEDVGPNGAINYIIIDGNELGLFNVTRTEDNQAIIRTKKPLDRETLESVRLTIRCFKLNTVPDPLTHESYNRHDKSQLQLLIRVLDIDDHAPRFERENQTIGIRHNVPIDTPIANGRAFDEDPTARPIVYSIQSINFVPQFYRRDNRTEEYGDVFSLNPDTAEIRTTRSMSNFVDGYFQLMVRAANSDEAERISETQMKIFVIRDKSLLRFVFSRPPTEVSGVLDRFTVEMQERLANANLELSVFDAQVLSQPDHSLDFSSTSSCFQLTRHGSALTPVEMMRIMDDAEMKETLAEVYHRYSVHKIDSCAVSKKPPATALIASSGTWLVILAGLIGFAAFASTMTACCLAKRYKNQVRSTINSQRIVGSDIYGSATPVLYTEPIYGAL
The following text describes a protein:
Function:
An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigD. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor. Neither S1P nor S2P proteases have been so far identified for this anti-sigma factor.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Domain:
The cytosolic domain interacts with ECF sigma factor SigD.
Sequence:
MREFGNPLGDRPPLDELARTDLLLDALAEREEVDFADPRDDALAALLGQWRDDLRWPPASALVSQDEAVAALRAGVAQRRRARRSLAAVGSVAAALLVLSGFGAVVADARPGDLLYGLHAMMFNRSRVSDDQIVLSAKANLAKVEQMIAQGQWAEAQDELAEVSSTVQAVTDGSRRQDLINEVNLLNTKVETRDPNATLRPGSPSNPAAPGSVGNSWTPLAPVVEPPTPPTPASAAEPSMSAGVSESPMPNSTSTVAASPSTPSSKPEPGSIDPSLEPADEATNPAGQPAPETPVSPTH
The following text describes a protein:
Function:
May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular Localization:
Secreted, cell wall. Membrane; Peripheral membrane protein.
Sequence:
MASSSLKCFSFIVVLTTFFAISLKPCYCHNKTHWNTAGITWYGDREGPGTTGGACGYGDAVAKHPYRCMVSAGGPSLFKDGKGCGACYRLKCDHPLCTKKPIKVMISDECPGCTKESVHFDLSGKAFGALAKRGKGDQLRNLGELKVSYKRACCKHPKTMIAIHVDAGANPYYMSFAVKFANGDGNFACIEVQPAGGQYMKMEEMRSAVWRLSPGVPLKGPFNIRLTSAVSGKKIIAKGVIPEKWSPGAIYHSKVNFPVQRKQK
The following text describes a protein:
Function:
May function as a growth and differentiation factor involved in neuritogenesis and more particularly in neurite extension.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MGVGGTSASDTALSLCPTAPEWPPRNGSSGRAWGGPLQSGAPINSTDPLGPQLEPPGGGPATADPTVGCMGCSGEGAASSVPPVPDAAQDPRLGVTGPTDGDGGVVALGSPEEVGSGEQPTRAGVGPTEGLTPRPPGLPSPGLGLSSPGPNLGLPSLDLPNPNLGLPDPNLGLPNPSLGLPSPGPTPDRPIPNPNPSLDLPDPGLAIQTPNLGLSNPNIPLPSPSPGPGTEPDLLPVAEDSEVSMELPQPSSSPAPAQRARGRTDRTWLGAPEPISAAPGTAEPPEIIDVDYYDVFDGGHGPGGGHGAGGAAQREPGGAATPWGLHELYDDFTPFDEADFYPTTSFYAEGDDDAEEELEEDEEEEEEEDGGLEDENGYRPPASAAPRVPPPPSPTEGTPMARPRPGERAVPENSSECRSGYVRHNSSCRSVCDLVPSYCHNGGQCYLVESHGAFCRCNTQDYTWHKGTRCEAIVTDFQVLCVAVGSAALVLLLLFMLTVFFAKKLYLLKTENSKLRKTKYRTPSELHNDNFSLSTIAEGSHPNDDPGAPHKLQDPLKPGLKDEEPLSILSTAPEEGSKGEPGGCGVPCLHNNLG
The following text describes a protein:
Function:
Catalyzes the glutathione-dependent reduction of S-glutathionylquercetin to quercetin. In vitro, possesses glutathione-dependent thiol transferase activity toward 2-hydroxyethyl disulfide (HED).
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MSVGLKVSAFLHPTLALSSRDVSLSSSSSSLYLDRKILRPGSGRRWCKSRRTEPILAVVESSRVPELDSSSEPVQVFDGSTRLYISYTCPFAQRAWIARNYKGLQNKIELVPIDLKNRPAWYKEKVYSANKVPALEHNNRVLGESLDLIKYIDTNFEGPSLTPDGLEKQVVADELLSYTDSFSKAVRSTLNGTDTNAADVAFDYIEQALSKFNEGPFFLGQFSLVDVAYAPFIERFRLILSDVMNVDITSGRPNLALWIQEMNKIEAYTETRQDPQELVERYKRRVQAEARL
The following text describes a protein:
Function:
Involved in a late nucleoplasmic step of 60S ribosomal subunit assembly.
Miscellaneous:
MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MNYNNFENSKGDGHSRLPKPTYSGTLSDGYDESKIKRQKTDSAFNAAYSPHMYPNSPYYEGSWNTGYTPQLHHVAPHNQYFHPIQPSTQYNYTSPPNYTENYIPPVHQNISYAPALNLQKWPSSYCENTQALKNDKDYQTSISYEDVAIPTVKEIQLIEKNRGKDTFMNEISPVPSSKDQASAEPTEIPRKDPELANSNAEDDHNNLGLEDDDRDEQLESEGLGKVVLVPGTSIALITDEDVKKWREERKKMWLLKISNNKQKHMQEMGIKEDELKSQPSIFKESRKEKQFIQSIQNQVQRGNPKIDLNLKLIQREFANENSQLLDFIRELGDVGLLEYELSQQEKDVLFGSSEDNNKNHYKPNYKNRKPNLSRANFTRNK
The following text describes a protein:
Function:
Required for biogenesis of the 60S ribosomal subunit.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVKPSKILEKIKKRTEPVAEPVVEEESDEEIIEQEGSEEEEEIVEEESEEEEEEVEEENKNIEENKKDQSIYTKKRVLFTSTRGIGSKYRHLMADLISLIPHSKKEDKIDDRKTLSLINETCEMKSCNYAILFDVRKGTDCFLWMAKTPLGPTVKFHITNVHTLDELQMTGNCLKGSRPFLHFDKSFDSEVHLQLIKELITQIYSTPKGHVKSKPFFDHVFSFFYQDGRIWFRNYQISDQEFKKDSLLTEIGPRMIMHIDKIFSDGFGGSVLYSNPNYVSPNNTRSDHKLSKANKYIKRKYQKGKAEERQKISFIEPSEVDTVFDN
The following text describes a protein:
Function:
Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of ether lipids. Ether lipids are essential components of brain membranes.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MAEENLKIQEVFAGKDGPSVLTGVRRIFYLVTPNETSFRTVEEVPKYVAQASPFFFGMIFLELFVASLKNKQTPTRLNDSISSMSAGMLQQMSQLFSKGVYLMVYIWVYENYRLVDLPWDSPITWWTAFILVEFGYYWLHRMSHEVNILWAAHQVHHSSEDYNLTTALRQSTTQLVGTFWFSYLPLAFLVPPAAFSAHKQFNLLYQFWIHTELVTSLGPLEYILNTPSHHRVHHGRNRYCIDKNYGGTLIIFDRIFGTFAKEEEKVVYGLTHPLNTWDPIWVQVCHYAHIWNTFWATPGLTNKLSVLWKGPGWAPGKPRLGCIEDIPKVKYPEPMYDSKVSSLWSVYVAVHFFLAMVLYQELFAVVKCL
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Miscellaneous:
MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MNNWQHFFNNPVDLSEHLKKPYFRFDNRDKEITAISFDEKANLIWSGDSYGCISSYDPTFQLYTRYRGHIGGNSVKDILSHRDGILSISEDSLHFANRRGVTKLNLTSIDIAAFSELNTMCYSPHSLKNNIYCGGDNTNWGIASIDLNRGCLDSLLNYSSKVKLMCSNNKVLSIGRQTGTVDLLDPTSNRTIKSFNAHSASISAMDLRDNTLVTVGKSKRFYNLYADPFVNVYDLRTMRQLPPVSFSKGTTMGSGGADFVQLHPLLPTVMIVASSSGSFDFIDLSNPTLRTQYVHPCQSIKKLCLSPNGDVLGILEADNHLDTWRRSSNNMGMFTNTPEMLAYPDYFNDITSDGPISVDDETYPLSSVGMPYYLDKLLSAWPPVVFKSEGTIPQLTGKSPLPSSGKLKSNLAVISSQNEKLSTQEFPLLRYDRTKYGMRNAIPDYVCLRDIRKQITSGLETSDIQTYTSINKYEVPPAYSRLPLTSGRFGTDNFDFTPFNNTEYSGLDPDVDNHYTNAIIQLYRFIPEMFNFVVGCLKDENFETTLLTDLGYLFDMMERSHGKICSSSNFQASLKSLTDKRQLENGEPQEHLEEYLESLCIRESIEDFNSSESIKRNMPQKFNRFLLSQLIKEEAQTVNHNITLNQCFGLETEIRTECSCDHYDTTVKLLPSLSISGINKTVIKQLNKKSNGQNILPYIEYAMKNVTQKNSICPTCGKTETITQECTVKNLPSVLSLELSLLDTEFSNIRSSKNWLTSEFYGSIIKNKAVLRSTASELKGTSHIFKYELNGYVAKITDNNNETRLVTYVKKYNPKENCFKWLMFNDYLVVEITEEEALKMTYPWKTPEIIIYCDAEELRKPFFSVDTYSINYDILFRDYFANGIRDTARREYKLLTHDEAPKSGTLVAIDAEFVSLQSELCEIDHQGIRSIIRPKRTALARISIIRGEEGELYGVPFVDDYVVNTNHIEDYLTRYSGILPGDLDPEKSTKRLVRRNVVYRKVWLLMQLGCVFVGHGLNNDFKHININVPRNQIRDTAIYFLQGKRYLSLRYLAYVLLGMNIQEGNHDSIEDAHTALILYKKYLHLKEKAIFEKVLNSVYEEGRAHNFKVPETSKG
The following text describes a protein:
Function:
Microtubule-stabilizing protein involved in the control of cell motility and neurite outgrowth. Facilitate microtubule stabilization through the maintenance of acetylated stable microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Midbody.
Sequence:
MESGPRAELGAGAPPAVVARTPPEPRPSPEGDPSPPPPPMSALVPDTPPDTPPAMKNATSSKQLPLEPESPSGQVGPRPAPPQEESPSSEAKSRGPTPPAMGPRDARPPRRSSQPSPTAVPASDSPPTKQEVKKAGERHKLAKERREERAKYLAAKKAVWLEKEEKAKALREKQLQERRRRLEEQRLKAEQRRAALEERQRQKLEKNKERYEAAIQRSVKKTWAEIRQQRWSWAGALHHSSPGHKTSGSRCSVSAVNLPKHVDSIINKRLSKSSATLWNSPSRNRSLQLSAWESSIVDRLMTPTLSFLARSRSAVTLPRNGRDQGRGCDPGRGPTWGRAGASLARGPQPDRTHPSAAVPVCPRSASASPLTPCSVTRSVHRCAPAGERGERRKPNAGGSPAPVRRRPEASPVQKKEKKDKERENEKEKSALARERSLKKRQSLPASPRARLSASTASELSPKSKARPSSPSTSWHRPASPCPSPGPGHTLPPKPPSPRGTTASPKGRVRRKEEAKESPSAAGPEDKSQSKRRASNEKESAAPASPAPSPAPSPTPAPPQKEQPPAETPTDAAVLTSPPAPAPPVTPSKPMAGTTDREEATRLLAEKRRQAREQREREEQERRLQAERDKRMREEQLAREAEARAEREAEARRREEQEAREKAQAEQEEQERLQKQKEEAEARSREEAERQRLEREKHFQQQEQERQERRKRLEEIMKRTRKSEVSETKQKQDSKEANANGSSPEPVKAVEARSPGLQKEAVQKEEPIPQEPQWSLPSKELPASLVNGLQPLPAHQENGFSTNGPSGDKSLSRTPETLLPFAEAEAFLKKAVVQSPQVTEVL
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Miscellaneous:
MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
Sequence:
MARQGNFYAVRKGRETGIYNTWNECKNQVDGYGGAIYKKFNSYEQAKSFLGQPNTTSNYGSSTHAGGQVSKPHTTQKRVHRRNRPLHYSSLTSSSACSSLSSANTNTFYSVKSNVPNIESKIFNNWKDCQAYVKHKRGITFKKFEDQLAAENFISGMSAHDYKLMNISKESFESKYKLSSNTMYNKSMNVYCDGSSFGNGTSSSRAGYGAYFEGAPEENISEPLLSGAQTNNRAEIEAVSEALKKIWEKLTNEKEKVNYQIKTDSEYVTKLLNDRYMTYDNKKLEGLPNSDLIVPLVQRFVKVKKYYELNKECFKNNGKFQIEWVKGHDGDPGNEMADFLAKKGASRR