lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for DNA interstrand cross-link repair. This requires cleavage of cross-linked DNA to generate DNA double strand breaks (DSBs). This protein may have 5' exonuclease activity on single-stranded and double-stranded DNA, which could be necessary for the processing of DNA double strand breaks prior to religation.
Subcellular Localization:
Nucleus.
Sequence:
MSKRKSSSILDFFKKSNNGKNMWGNEAVSVEKTDSTTKPSTVKNAISSSQIKNEKFSQEVLLQFNDPSFTSEVGESPQWQSFGDANILEPLKNELVKNEESTMSELLLCPICGITLESLTVDANIHVNDCLDGRTTEAVSKKLKKDSVVKADPSNSSTFPISDSCKQALLPLPGKQINVRSVVPFYKLMPYNIPFAVDAFAYGAIDGVEAYFLSHFHSDHYGGLTPKWKHGPIYCSEVTGNLLINVMHVDEQYVKRLKLNQPYNIMGITVYVLDANHCPGSAMFVFETLQSNQTRRVLHCGDFRASKDHVMHPVLREKTIHKVYLDTTYLNPKYTFPPQADVVQACADKAISIKKSTDSRLLVVVSTYSIGKEKVAVAIAKSLSSRIYVVPRKMHIIKQLENQDLIDLLTDDPTQASVHMVTMMGIHPNSLLDYLEQYNSSFDKIIGYKVTGWTFQPLENRAQLSSSLDSIISRPPKFVEYDLRAIRGSTDKVAAFVAPYSEHSSFYDLTMFCLSMNIGHIIPTVNVGSQRSREKMNVWLDRWAWRRKKQGLLSLENVDW
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MFLFLLQHYLSIITKLSPERGGTILERHITTKLNVKDNSSFLFSFSLAAASTSSSSPQPSLANDTGEALTDILILTPTYEKNEDLNCQHQKKKTQMKKLCRTKKVKEHCCVECEKSYTTAYQLRRHMRIHTGENLFSCKECECGKSFTRIGKLSLHMRIHTGEKPFSCKECGRSFSRVDSLIGHMRIHTGEKPFSCKECGKCFTLSCSLTDHMRIHTGEKPFPCKKCGRSFRRSSKLSVHMRIHTGEKPFTCEVCGRSFSHAKSLTNHMRIHTGEKPFSCEECGRSFSQATSLTNHMRIHTGEKHRGRTVRPSVITVILSLISLSEENRGDSMGS
The following text describes a protein:
Function:
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Miscellaneous:
MISCELLANEOUS: Present with 876 molecules/cell in log phase SD medium; MISCELLANEOUS: Partially functionally complemented by T.brucei CLS/cardiolipin synthetase, but conversely does not functionally complement T.brucei CLS/cardiolipin synthetase.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence:
MIQMVPIYSCSALLRRTIPKRPFYHVLSGLTVRFKVNPQLNYNLFRDLTRREYATNPSKTPHIKSKLLNIPNILTLSRIGCTPFIGLFIITNNLTPALGLFAFSSITDFMDGYIARKYGLKTIAGTILDPLADKLLMITTTLALSVPSGPQIIPVSIAAIILGRDVLLAISALFIRYSTLKLKYPGRVAWNSYWDIVRYPSAEVRPSQLSKWNTFFQMVYLGSGVLLLLYEKEEGCEKTEEDFEDRKQDFQKAFSYLGYVTATTTIMSGVSYALKRNAFKLLK
The following text describes a protein:
Function:
Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MASKPGPLTQWPWHNLGNYKYALVAPSAAYSTYRFVTASSAAERDLLNFMVFPMLLLRLLYGQLWITVSRHQTARSKHKIVNKSLDFEQIDRERNWDDQIILTALVFYLVSATMPQAQVAPWWSTKGMVVTAVLHAGPVEFLYYWLHRALHHHWLYARYHSHHHASIVTEPITSVIHPFAEEVVYFVLLAIPILSTVATGTVSVVTANGYLVYIDFMNYLGHCNFELVPKCLFHVFPPLKYLLYTPSFHSLHHTQFRTNYSLFMPVYDYIYGTTDKSSDELYERTLQGRDEAAWRPDVVHLTHLTTPESVFHNRLGFAAVASNPLGAAASGHLLRAASAVASPLLSLFASTFRSEANRLDKLNIETWVIPRFTSHYTSKSDGYKVSRLIEKAVSDAEASGARVLTLGLLNQGYDLNRNGELYVVRKPSLKTKIVDGTSLAVAAVLNMIPQGTKDVLLLGNANKISLVLTLSLCKREIQVRMVNKELYECLKQQLQPEMQEHLVLSCSYSSKVWLVGDGVTDEEQMKAQKGSHFVPYSQFPPNKARNDCVYHCTPALLVPESFENLHVCENWLPRRVMSAWRAAGIVHALEKWDGHECGGRVTGVQKAWSAALARGFRPYDDHHHPGITHDGRGGL
The following text describes a protein:
Function:
DNA-binding protein that recognizes sequence-specific replication termini (Ter sites) within rDNA. Binds to rDNA terminator elements and mediates efficient RNA polymerase I transcription termination. Required for rDNA silencing at the non-transcribed spacer 1 (NTS1). Promotes the association of SIR2 with NTS1 and contributes to maintenance of rDNA stability.
Miscellaneous:
MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MDSVSNLKSTNFQNNNDPKESVEEAVLRYVGVDLKNHIKKTKKKLKKQKKRKHGSKMSHEDEDTDMDWYLKTSGSKDLRKVDDIEPNSVAVAAVAAAYNSSMREKDKRSCHKKSSNSRSERKKHRKRKSSKERKAKIKMVLDPQLTTLDDGITTTAFLPDDLIAETAFDKYVDTEKAYLAKHPSKSLEVNEDDKENNFNNNSSTLVRIYTDLEGIPNDGSYIKRTPKIPEKDVKSDDLILAPEENNGDTALLRSDIVKASVIDGAITKSIGKKFTPSEENALDQFIEEYMKIRGLDRRQMCERIWSTDGVIRDGFWANISKVLPYRTRSSIYKHIRRKYHIFEQRGKWTPEEDQELARLCLEKEGHWTEVGKLLGRMPEDCRDRWRNYMKCGSKRGSKRWSKEEEELLTTVVNEMIEEAHQYQRMKALEAANKNDRYNQMYSRGPKGKRISDNPTFKDMINWTVVSERMSGTRSRIQCRYKWNKLVTDEAARSMLSIPVSERKWLLERLKQLPKTSYSNIDWNSIATYKPGYPRTGLELRLCYEQMREKIHDFKGRSTAEIIDSLLEQIN
The following text describes a protein:
Function:
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Sequence:
MRGEREFRKVRAHGAAVRDPLFTLRLTDYRPRYGERWHPRAIIGLVVSKKTLKHAVKRNRARRRVREALRTMPPELLPGGLPACRAILMLNPGVLTVPFPELQAALAQALQRGAGATKRGGAKGKGGKKGGGQVAGERAGNESGSGRVSAEVNPTSASPASPAEKS
The following text describes a protein:
Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Localization:
Postsynaptic cell membrane; Multi-pass membrane protein.
Sequence:
MLFKSTEASKHIEANPHAKRLYDDLLSNYNRLIRPVENHTQTLTVWLGLKLSQLIEMNLKNQVMTTNLWVVQRWYDYKLKWEPEEYGGVEMLYVPSEHIWLPDIVLFNNADGNYEVTLMTKATLSYTGEVIWKPPSIYKSSCEINVQYFPFDEQSCLMKFGSWTYNGLQVDLKHMDQVSGNNIVKVGIDLSEFYLSVEWDILAVPATRNEEYYPCCTEPYSDITFKITMRRKTLFYTVNLIIPCVGITFLTVLVFYLPSDSGEKVTLCVSILLSLTVFFLLLAEIIPPTSLAVPLLGKYLLFTMILVTSSIWVTVCVLNVHFRSPSTHKMSPIVRKIFLQFMPKLLIMRRTTYTLPEYDDSLPPRGYSGEIEMQLNMRDPFNTDFKMKAHSSMSSSNITPRFLSANVLSALQGVRFIAQHIRDADKDNEIVEDWKFVSMVLDRFFLWVFTLACIGGTFGIILQAPSLYDTRVPVHQQLSEIPLTKIFQIPPSRTHIPTQ
The following text describes a protein:
Function:
Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.
Sequence:
MPLSTYDAAPLLHSYDDSPQRWSGVTNGHQAGVIIDQFRGGKAIIIEGGTSTGDTKSIGGGSDLRLVITANPSEIERNYEQPTNRGGGGGGGVIGVSCGGQTPPTPSVGKTLLNTSPNLLPITTATDTFNNLKNLVKIDKGSSPSSGSNSLGGNYRKGGSNGSGYKSAGGNGGSPAISGNSEGGRNGSRSSGGPTGHFSTGYSKNSVKIRQHDSEVSPRPRRSYQGDSSSSRYYPKNSDILGQGLGGNSDSYNGSSSSGRYQQQDQQGGSHRGSRSNYHSNSDGSYNRSINSNSVGGGGSGAVGSGSGGSNYRSARNYENGNGSNGTQPRYGSGNGNGNSSNSNSSSGYNGSAASSTNSKSSYGASRGGNDGGVSSGYSSNYRDNYEDSPSHQRYNNTNSLERNGGGGSGAGASGGPRSYGRSDADRYGGTPSSRTPNLRNGSASAQISGSTSNSSNISLNSGSASAAGGGTPHSQQQQERSQAGKASTPPPITGRWIPPSLRPQHGLTQSEKNDAVFRRVRGILNKLTPEKFQELSDELLKLDLNSIAILKGVILLIFDKALDEPKYSSMYAQLCKRLSEEAPSFDKEPSNSSTFLRLLIAVCRDKFNNRLKRDENDNRPPPENEADEEERRHLAKQRMLGNVKFIGELNKLDMLSKNVLHQCIMELFDKKKKRTAGTQEMCEDMECLAQLLKTCGKNLDSEQGKELMNQYFEKLERRSKSSEYPPRIRFMLKDVIELRQNNWVPRKLGTTEGPVPIKQIRSDDDSIIRTPFPNRNRDMRNNDRDSDSWMNRFHLNIQPGGYNDMFSGLSVTGASPIVSPFATSNRDRDRDNRQYNNRGDRNRDRDQGGSGGANYGNRYNKHNQNGGGSGGGSSNNRDRDDSRRNNDRDRDRNDGQYGGNQLLGSKELAPRFKRNLITTNQDAVENLQMRPAANSLLFRAASQNQKFPATLPMSTPPNSSGSNNQGSSQGQLSNSHYPMLGTPTSHLINPTRPSSTPSAEYADNRTLLGVQQERGLKATSSSPNFSSGAEKLDLDGQAGRKGSHDGKDQGKNGSVERPSTPAGGIGSAKQQKKDKGPNKEELSKKASQYFKDRFYYDEEEDAEVTEIEIKDIDETKTEEADAAPVEVSEVKEDAAIPVTTPDRFTKLVDGFLELKLPEKALKDVCINLLMEVLDRVNDVFLERAVRLLQTLRKQSNIKPNIVVEIFKQVVNKMNEREALNPRIVSLVASLLAKTICEPALLKLSDIANFTDNGQHYPLFLLVLQQLVKVIGKDALEEKFRASKVDLMNSLPEADRNKERLAGILEDRKLSFLYPLLKVQAEMLKQLQSDPNPNNFYKWIKANVDNKYYKDPGFIQALMTVVVKYVTKETTLADNLDPKEHPEKSVTQKEQQLLENYSQMLQTFLGQNELQLMALYALQTFCYNENFPKGMLCRWFKYLYESEIIEEEAFVLWKEEISDKYPGKGSALFQVNAWLTWLQEAESEDDED
The following text describes a protein:
Function:
Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate; Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MSKHKPKKAAGEQQEPPPPPQPAVIPNSGHLPSVKTSPDTTLEPLQLTSDDRNQFQMLKQPEARCCVSKFDKAPDKALVCFQYLSQGGANVIFKIHSWPQKPSQQDQPFLFVDAKLASTKATPIHSLQLVDKVLRINKGLLKTLRCEEVISGFYGHVRPLFAAGGVTTIVGPAYTQLPIKMHDRDYTEYLMEHQGVILYSSVMVNLTSKSDAIGVERGLGSAQQLLTSQRWGILLPDMSPTPGNSVTIELKPKWLAQSPTAPSKAIRCRTCALQVLKPKDPSKYLCPLQLLNGNFDVVNKWVLSRVAEQAAGPTQDTKRNSAISHEITSYLMKGPGKSLLEHLRVLQVSLDHHGILNGNKIGSPKKELHNMFEHNVRLAMTLRDCSLYIRIAYSKDGAVPSSIECKLGDLDFKSADKMDDWAAKETELIESGSYTREIKEDLGCLIPHINAANQAWLQRLTYLH
The following text describes a protein:
Function:
Involved in photosystem II (PSII) assembly and/or repair under high light stress. Required for binding of chlorophyll and carotenoids by the Ycf39-Hlip complex. The Ycf39-Hlip complex binds D1 at an early stage of PSII assembly along with Ycf48, ribosomes and ChlG, the last enzyme in chlorophyll biosynthesis; it may be involved in chlorophyll reuse and delivery to D1 in the initial stages of PSII assembly. Binds chlorophyll a and beta-carotenoid in a 3:1 stoichiometry in the presence and absence of Yfc39; in the Ycf39-HliC-HliD complex, HliD binds all the pigment. The Ycf39-Hlip complex efficiently quenches chlorophyll fluorescence, contributing to photoprotection. Deletion of 4 to 5 members of the Hlip family suggests the proteins are involved in regulation of chlorophyll biosynthesis, in stabilization of chlorophyll-binding proteins and/or in reuse of chlorophylls, and may regulate tetrapyrrole biosynthesis (Probable). Might bind chlorophyll and/or carotenoids in association with HliC (called the ScpBE pair) (Probable); The Hlips might regulate tetrapyrrole biosynthesis, maybe at the level of aminolevulinic acid synthesis and probably stabilize PSII assembly intermediates.
Subcellular Localization:
Cellular thylakoid membrane; Single-pass membrane protein. Note=Not detected in cell inner or outer membranes.
Sequence:
MSEELQPNQTPVQEDPKFGFNNYAEKLNGRAAMVGFLLILVIEYFTNQGVLAWLGLR
The following text describes a protein:
Function:
Transcription factor which regulates nonfermentable carbon utilization.
Subcellular Localization:
Nucleus.
Sequence:
MTKRISAEEKLNRKPISRACVFCHEKHLQCDVGRPCQNCEKRNIGESCRDNVRKVRKTRGRTPRSGVMNLRRARREHEDELAIATKSRGAGEPGSTGLPQVPSLSTLFDANVDPVIDEELLPATYVDPLGPSDVELPTSGAESFGSVWASSEYTKLNEILGSPGIERPRKHVPSKYEPFAVPATAEHSPSPSTPIELLQDHAGLLFRNTLRRHISLDTAQSSYQASTQDTQASTVASSVSCEGAQFPASEAEYTSPYSFRQLVRSPEDLYRHQNSIFPHNYRQAYLELLNILRARFLSAQDEIAREEGPKQLHSIAQSIKTYYAPIFVTLTSNLIESDLKMHELILQRTLLEYENMSKMVNCIPMCIWRRSGEICYVSNEFISLTGFSRRELLMRRRFIMEFFDNHGIVDYFKLFNEYLAFSSKEGFSSTSDGQAVFSECNLLMANNSFLKCACIWTVKRDSFNIPMLVMGQFLPIFDMDHT
The following text describes a protein:
Function:
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Subcellular Localization:
Virion. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle.
Sequence:
MAVISKVTYSLYDQKEINATDIIISHVKNDDDIGTVKDGRLGAMDGALCKTCGKTELECFGHWGKVSIYKTHIVKPEFISEIIRLLNHICIHCGLLRSREPYSDDINLKELSGHALRRLKDKILSKKKSCWNSECMQPYQKITFSKKKVCFVNKLDDINVPNSLIYQKLISIHEKFWPLLEIHQYPANLFYTDYFPIPPLIIRPAISFWIDSIPKETNELTYLLGMIVKNCNLNADEQVIQKAVIEYDDIKIISNNTSSINLSYITSGKNNMIRSYIVARRKDQTARSVIGPSTSITVNEVGMPAYIRNTLTEKIFVNAFTVDKVKQLLASNQVKFYFNKRLNQLTRIRQGKFIKNKIHLLPGDWVEVAVQEYTSIIFGRQPSLHRYNVIASSIRATEGDTIKISPGIANSQNADFDGDEEWMILEQNPKAVIEQSILMYPTTLLKHDIHGAPVYGSIQDEIVAAYSLFRIQDLCLDEVLNILGKYGREFDPKGKCKFSGKDIYTYLIGEKINYPGLLKDGEIIANDVDSNFVVAMRHLSLAGLLSDHKSNVEGINFIIKSSYVFKRYLSIYGFGVTFKDLRPNSTFTNKLEAINVEKIELIKEAYAKYLNDVRDGKIVPLSKALEADYVESMLSNLTNLNIREIEEHMRQTLIDDPDNNLLKMAKAGYKVNPTELMYILGTYGQQRIDGEPAETRVLGRVLPYYLPDSKDPEGRGYILNSLTKGLTGSQYYFSMLVARSQSTDIVCETSRTGTLARKIIKKMEDMVVDGYGQVVIGNTLIKYAANYTKILGSVCKPVDLIYPDESMTWYLEISALWNKIKQGFVYSQKQKLAKKTLAPFNFLVFVKPTTEDNAIKVKDLYDMIHNVIDDVREKYFFTVSNIDFMEYIFLTHLNPSRIRITKETAITIFEKFYEKLNYTLGGGTPIGIISAQVLSEKFTQQALSSFHTTEKSGAVKQKLGFNEFNNLTNLSKNKTEIITLVSDDISKLQSVKINFEFVCLGELNPDHSLFEKKQDRYVVDIIVNKLYIKRAEITELVVEYMIERFISFSVIVKEWGMETFIEDEDNIRFTVYLNFVEPEELNLSKFMMVLPGAANKGKISKFKIPISDYTGYDCFNQTKKLNKMTVELMNLKELGSFDLENVNVYPGVWNTYDIFGIEAAREYLCEAMLNTYGEGFDYLYQPCDLLASLLCASYEPESVNKFKFGAASTLKRATFGDNKALLNAALHKKSEPINDNSSCHFFSKVPNIGTGYYKYFIDLGLLMRMERKLSDKISSQKIKEMEETEDF
The following text describes a protein:
Function:
Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MERPEAGGINSNECENVSRKKKMSEEFEANTMDSLVDMPFATVDIQDDCGITDEPQINLKRSQENEWVKSDQVKKRKKKRKDYQPNYFLSIPITNKEIIKGIKILQNAIIQQDERLAKAMVSDGSFHITLLVMQLLNEDEVNIGIDALLELKPFIEELLQGKHLTLPFQGIGTFGNQVGFVKLAEGDHVNSLLEIAETANRTFQEKGILVGESRSFKPHLTFMKLSKSPWLRKNGVKKIDPDLYEKFISHRFGEEILYRIDLCSMLKKKQSNGYYHCESSIVIGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK
The following text describes a protein:
Function:
Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Sequence:
VNILLDKEANFNNFFMEQALKQARIAFDKNEVPVGAVIVDRLNQKIIASTHNNTEEKNNALCHAEIIAINEACNLIYSKNLNDYDIYVTLESCAMCAAAIAHSRLKRLFYGAFDSKHGAVESNLRYFNSSACFHRPEIYSGILAEDSGLLMKEFFKRIR
The following text describes a protein:
Function:
Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin; Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress; Leumorphin has a typical opioid activity and may have anti-apoptotic effect.
Subcellular Localization:
Secreted.
Sequence:
MKALSTKFNPVVCSLQCEGSLLPGDEWESCSQLLSSQEGIIEVKKEQELVSPLVDSQGIMVKRYGGFIRKPDKNKFLNGKRENTSFSKRYGGFLHKYTLRDLQDLSSNSETKLESPDAEELGWSSPTWETKDEMKRYGGFLRKYPKRSSAQEGDSEQGLEKKRRLQEGLEPGQAIVTGQEIETGQEVDLEHGTAELEKRYGGFLRRIRPKLRWDNQKRYGGFLRRQFKVNARSEEDPTMFSGELSYL
The following text describes a protein:
Function:
Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy; Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila.
Domain:
Both the BIR and NACHT domains are essential for effective inhibition of pro-CASP9 cleavage. BIR3 domain binds to procaspase-9 and the NACHT domain interacts with the NACHT domain of APAF1 forming a bridge between pro-CASP9 and APAF1.
Sequence:
MATQQKASDERISQFDHNLLPELSALLGLDAVQLAKELEEEEQKERAKMQKGYNSQMRSEAKRLKTFVTYEPYSSWIPQEMAAAGFYFTGVKSGIQCFCCSLILFGAGLTRLPIEDHKRFHPDCGFLLNKDVGNIAKYDIRVKNLKSRLRGGKMRYQEEEARLASFRNWPFYVQGISPCVLSEAGFVFTGKQDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLRSKKSSEEITQYIQSYKGFVDITGEHFVNSWVQRELPMASAYCNDSIFAYEELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQNMKSSAEVTPDLQSRGELCELLETTSESNLEDSIAVGPIVPEMAQGEAQWFQEAKNLNEQLRAAYTSASFRHMSLLDISSDLATDHLLGCDLSIASKHISKPVQEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQLKNQVLFLLDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPFYNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSFDDVAVFKSYMERLSLRNKATAEILKATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDEDLTMCLMSKFTAQRLRPFYRFLSPAFQEFLAGMRLIELLDSDRQEHQDLGLYHLKQINSPMMTVSAYNNFLNYVSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLRGLWQICPQAYFSMVSEHLLVLALKTAYQSNTVAACSPFVLQFLQGRTLTLGALNLQYFFDHPESLSLLRSIHFPIRGNKTSPRAHFSVLETCFDKSQVPTIDQDYASAFEPMNEWERNLAEKEDNVKSYMDMQRRASPDLSTGYWKLSPKQYKIPCLEVDVNDIDVVGQDMLEILMTVFSASQRIELHLNHSRGFIESIRPALELSKASVTKCSISKLELSAAEQELLLTLPSLESLEVSGTIQSQDQIFPNLDKFLCLKELSVDLEGNINVFSVIPEEFPNFHHMEKLLIQISAEYDPSKLVKLIQNSPNLHVFHLKCNFFSDFGSLMTMLVSCKKLTEIKFSDSFFQAVPFVASLPNFISLKILNLEGQQFPDEETSEKFAYILGSLSNLEELILPTGDGIYRVAKLIIQQCQQLHCLRVLSFFKTLNDDSVVEIAKVAISGGFQKLENLKLSINHKITEEGYRNFFQALDNMPNLQELDISRHFTECIKAQATTVKSLSQCVLRLPRLIRLNMLSWLLDADDIALLNVMKERHPQSKYLTILQKWILPFSPIIQK
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MPIHLEIVTAERVILSDDVDMISAPTKDGRVGILPRHAPLMTILEPGELDIIKNGERTPFAVSGGFMEVLPHRVTILADTVERADEIDEARAEQARAEAEARRREAQSERDMALAEAKLRKEMVRLRVAQLHKIKRRQS
The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MIFPVFSVLFLLFHQAIPSVSGVEFFSSIHEMTKVFGYEQKMVLHMQKFLSDNQDKLDFLKARLREFENERNEAREWGPSYFESPINKYLLNKRLTVDWQRVENLMATSTGEKPLTRLRKFRNRETMPDKKELEGAIDGLLRLQYVYRLKAKDLARGILDGVDYGTQLNSEHCVDIARLALRDQHPRLAHSWLIEANDRLTGGEKEEQLKPQILALLVQAKKELEDFRGLNDTYQELIGIQSASEEHAKNYETFLNALSEKALLNESKPILEHAPIPEEGEPVGEFQAYSLTCSGHWRLTPKEQRHLRCGYVTETHPFLWIAPLKAEELFQDPLLVLYHDVIYQSEIDVIRKLTENRLMRATITSHNESVVSNVRTSQFTFIPVTAHKVLSTIDQRVADMTNLNMKYAEDHQFANYGIGGHYGQHMDWFYQTTFDAGLVSSPEMGNRIATVLFYLSDVAQGGGTAFPQLRTLLKPKKYAAAFWHNLHASGVGDVRTQHGACPIIAGSKWVQNRWIRENDQSDRRPCELWDDSLATYAQILELNKQNE
The following text describes a protein:
Function:
Component of the mitochondrial large ribosomal subunit (mt-LSU). The mitochondrial ribosome (mitoribosome) is a large ribonucleoprotein complex responsible for the synthesis of proteins inside mitochondria.
Subcellular Localization:
Mitochondrion.
Sequence:
MNEARARIIINLRLSMDSLMRVFSHRSPPPSFGFACDVGAHPSSTAQNLPMTYGSVREMIDDFSIVFGVPKYRTSKPKKVTRKFSFTRLLQPIDNLVTCPACSNIHPSDTICDACYAKVHQLTSEIKKKMMQYNPYVGEKQDKEVYVKFRGEPDAPAAVVKGKRVLEIEKERPTWFKKLTLKE
The following text describes a protein:
Function:
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MIDVRKYIDNAALKPHLSEKEIEEFVLKSEELGIYAVCVNPYHVKLASSIAKKVKVCCVIGFPLGLNKTSVKVKEAVEAVRDGAQELDIVWNLSAFKSEKYDFVVEELKEIFRETPSAVHKVIVETPYLNEEEIKKAVEICIEAGADFIKTSTGFAPRGTTLEEVRLIKSSAKGRIKVKASGGIRDLETAISMIEAGADRIGTSSGISIAEEFLKRHLI
The following text describes a protein:
Function:
[Isoform Kastor]: Regulates sperm development. May be involved in mitochondrial sheath formation; [Isoform Polluks]: Regulates sperm development. May be involved in mitochondrial sheath formation.
Miscellaneous:
MISCELLANEOUS: Isoform Kastor and isoform Polluks are conserved only in mammals.
Subcellular Localization:
[Isoform Kastor]: Mitochondrion outer membrane; Single-pass membrane protein; [Isoform Polluks]: Mitochondrion outer membrane; Single-pass membrane protein.
Sequence:
MIVLGWMLFVGLATYMGTFPEAMPPTLKWKERLPGQENKARRRIQALEEELLL
The following text describes a protein:
Function:
May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis. Required for proper localization of bile salt export pump ABCB11 at the apical/canalicular plasma membrane of hepatocytes; Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Can hydrolyze ATP in the presence of actin, which is essential for its function as a motor protein. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.
Subcellular Localization:
Cytoplasm.
Sequence:
MAVAELYAQYNRVWIPDPEEVWKSAEIAKDYRAGDRVLRLLLEDGMELEYPVDPGSLPPLRNPDILVGENDLTALSYLHEPAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNLYQLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGHRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEEL
The following text describes a protein:
Function:
Component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway. In the Dom34-Hbs1 complex, dom34 recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following ribosome-binding, the Dom34-Hbs1 complex promotes the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MRLVKNKIEYGGAGSVTLIPEEPEDMWHAYNLIVPGDLLYATAIRRVTTTAASTGSTSSSRVRLTLEIRVKNLDFDPQNSQLHVSGQIVNETPHTKIGQHHTLDLELNRQFTLEKGTGQDGEGSGWDSVAVEALKDAVDEGGNRRAEAVAVVMQEGLAHICFIGQFRTVLKQKVEISVPRKRAGGSDHDKTMTKFYQTTLDTLLRHMEFNLSSTSMTSNDPVRPVLLASPGFTATAFQKHIQSVANTTTPALKRLLPSIVVVHSASGYLHSLTEVLQSPTVKALLSDTKHARETKLMDDFYEQLRKETNKATYGPREVENAVEQGAVGRGGGILIISNRLFRSQDIAERKRWVALVDRVRDVEGGEVRVLSSEHESGKRLDGLGGIAAILTFPISDDLEEDSE
The following text describes a protein:
Function:
Probable carboxypeptidase.
Subcellular Localization:
Secreted.
Sequence:
MAKDYVFYVLKSLLLILQLVLLIHDADSASIVKFLPGFEGPLPFELETGYIGVGEEEEMQLFYYFFKSERNPEEDPLLLWLSGGPGCSSISGLLFENAGPLTIKLEEYNGTLPSLVSTTYSWTKTTSIIFLDQPVGTGFSYSRTQLVDKPKEAYFLSLFFLVVVQWLGKHEEFISNPLYVGGDSYSDKVVPALVQEISKGNYQCCKPPINLQCYVLGNPLTEFETDMNSRIPFAHGMALISDELYESLKIICKGKYVNADPSNTECLKLVEEYNKCTETVNPYLILEPFYEAETPDSYVTTYWANDESVRKALQINKESIGRWIRCNLDIPYTQDIISSVPYHVDNSIDGYRSLIYSGDHDLGMPYLGTQAWIRSLNYSVIDDWRPWTINSKLAGEVDTLLNLNQRKALSCFKGGSVANLCKHYIGVGEEEEVQLFYYFIKSERNPEEDPLFIWLNGGPGCSSISGLLFENEGPLTMKLEVYNGTLPSLVSTTYSWTKTSSIIYLDQPVGIGFSFSTQHVDTPSDSGEARRIHEFLQKWLVKHEEFIPNPFYVGGHSYTGKIVPPLVQEISKGNYQRHKPTINLQGYLLGNPVTEFEIDWNSRIPFAHEMALISDELYESLKRICKGKYVNVDSGNIECLKLLEEYNKFTKTVNPFLISEPSCETETPDCYIYRHLLATYWANDESVRKALQINKESIGRWVRCNFDIPYTHDIINSVPYHVDNSINGYRSLIFSGDHDLGVPYLGTQAWIRSLNYSVIDDWRPWMITHKLAGYTRTYANKMTFATIKASGHTAEFKPEESSVMFQRWISGQPL