lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis. Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins. Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2.
Subcellular Localization:
Cell junction, tight junction. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MSGPADETAGDLPVKDTGLNLCGMGGLQETSTTRTVKSRQAVSRITREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYEQVGGGPKRLGRDVEMEEMIEQLQEKIHELERQNEVLKNRLISAKQQLQIQSYRQTPYNYVQSRVNTGRRKANENVDLQECPRKGIRFQDVAVAETLQPMLTKYGNTLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSVMEGKFVQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMTFSERRIEELQDRINDLEKERELLKENYDKLYNSAFSAAQEEQWKLKEQQLRVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLIQENRELRLQYLEQKQQLDELKNRMKFYNQESDINADELSEALLLVKAQKSQKNGDLSFLEKVDNTINKDLECSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTQKMENLQQDYELKVEQYVHLLDVRAARIQKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETVHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPIVQGLHPEYNFTSQYLVHVNDLFLHYIQKNTITLEVHQAYSTDYETIAACQLRFHEILEKSGRIFCTANLVGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPGQTQGLSQQAPKTAQLSSTDSTDGNLNELHVTIRCCNHLQARARHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMCFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHKKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFILKAESEAVQRLPPASSVSTLIVAPTPKPRQRLTPVEKKVSFVDITPHQPSETSSPPEDMKEVSPEVEHTPEIEINMPAVSHIPEVSQESSIDKVKENIEKVQQGKDDDVSLLSEGQLAERSLPSSEDETEITEELEPEDEEDRSASDSDECIIPGPVSRSIKQPSEKIQIEIIALSLNDSRVTEDDTIQRLFVECRFYSLPAEETPVSLPKPKRGQWVYYNYSNVICVDKENNQAKRDILKAVLLKQEMPNRSIRFTVVSDPPEDEQDLECEDIGIAHVDLADMFQEGRDIIEQNIDVFDARADGGGIGKLKVTVEALRALRSVYEQYRDDLEA
The following text describes a protein:
Function:
Bifunctional wax ester synthase/diacylglycerol acyltransferase (By similarity). Involved in cuticular wax biosynthesis (By similarity).
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEIETRPHISGDEKEEEQPLSPAARLFHAPEFNCNIISVIGFKSKLDPCVFIRGFKESFIRHPRFSSKLVTDENGQNQRWVRTNVVVEDHFIVPKIKPQNIENSNAFLEDYVSDLMKIPLDTSRPLWELHLLDLKTSDAENVAVLKIHHSVGDGMSIMSLVLACMRKTSNPDELPSLPYQYRSSSRSSLLTTGSRSDSRLLWLVKVIWTAVILGLNTVCDALEFIVTTLFVKDTETPIKGDFLSTKSKQLRLVHRTVSLDDIKLTKNAMNMTINDVVLGVTQAGLSRYLARRYGEEETKNRKQKKLPKRIRLRSALLVNLRPTTGIQDLADMMEKGSKCRWGNWFGYVVFPFSIALRDDPLEHLEIAQKTISRKKNSYGAMLTYIFCRIIVKLLGIKVAASIINRMVSNTTMTFSNMVGPVEEVSFYGHPITYFASSAYGHPHALTIHCQSYMNKMTITLIVDPTVISDPHRLCDDWEESLRSIKAAVTKRESLRLWDYLRILHNRVAWLLYQIAGLLYRML
The following text describes a protein:
Function:
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with msh2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. Msh3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions (By similarity). Involved in termination of copy-synthesis during mating-type switching.
Subcellular Localization:
Nucleus.
Sequence:
MRGMSYNITHECDAINILSDNLHEGAISEDMVALSGPAIELLENNVGSSKNSYQEDEGSSSIDENAPLISIKRKRRIRTVKSTSNKELVQRKASKPTKQKSVFTPLEQQYLELKKNYQETILAIEVGYKFRFFGKDAKIASEVLGISCYFEHNFLNASVPSYRIDYHLERLINFGLKVAVVRQTETAALKSTSSSRNTLFDRRVARVLTKGTTLDDSFFRFEQTQHGTLQASQFILCVADNVDKSKAKSGRVQVGLIAIQLSSGTTVYDHFQDDFLRSELQTRLSHFQPCELIYSNKLSSESVALLNHYVSTEKTCGRVVRVQHAVQQDVKLALENLQDFFSSKCIMSGSKIIELHMEKVKSLHSLSIICLDMAISYLMEFSLEDLFVASNFYQPFDSISSMVLSKQALEGLELFVNQTDHTPVGSLFWVLDRTYTRFGQRMLQRWLQKPLVDKENIIERLDAVEELAFNSNSQVQAIRKMLYRLPDLEKGLSRIYYQRGFYKAASAFSKNSYSCFKSALLRRLIQQLPSISSIIDHFLGMFDQKEAENNNKVDMFKDIDNFDLSEEPNDVDYELAQEIRELKMSILMVRTEMDFHLQELRDYLEYPNLEFSIWGNVKFCIEVSKGCKKIPPDWIKLSSTRSLFRFHTPKIQSLLIELSSHEENLTISSEKIYRSFLSRISEHYNELRNVTTVLGTLDCLISFARISSQSGYTRPEFSDKELLIHESRHPMIELLSDKSFVPNHIHLSSDGVRCLLITGPNMGGKSSFVKQLALSAIMAQSGCFVPAKSALLPIFDSILIRMGSSDNLSVNMSTFMVEMLETKEVLSKATEKSMVIIDELGRGTSTIDGEAISYAVLHYLNQYIKSYLLFVTHFPSLGILERRFEGQLRCFHMGYLKSKEDFETSVSQSISFLYKLVPGVASKSYGLNVARMAGIPFSILSRATEISENYEKKHRNARKNVFIRKVAKLLMILNAEEIDFKRLFYDLTAFEEI
The following text describes a protein:
Function:
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the second glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSEIYPSLAQCAIVAGALKILLFPAYKSTDFEVHRNWLAITNSFPLWDWYYEKTSEWTLDYPPFFAYFEWVMSQVAKLVDPAMLKVYNLEFIDSSHGASKRAAQAAAISILLSPGLFIIDHIHFQYNGAMYGILIASLVLARKKSTLLWSGLLFAALLCMKHIYLYLAPAYFVFLLRAYCLSPKSVFRIQFLNCVKLGAGIGAILGTAFGPFALKGQIPQIFNRLFPFSRGLCHAYWAPNVWAMYSFVDRVLIVLAPRLGLSVKEGALQSVTRGLVGDTAFAVLPDVTPRVCFALTLIFQAIPLLKLFAQPTWDNFIGAVTLCGYASFLFGWHVHEKAILLVIIPFSLIALKDRRYLGAFRPLAVAGHVSLFPLLFTPAEFPLKTVYTVFWLILFLMAFDRLAPASSRARFFLFDRFSTLYITISIPLIVYCSLGHGIVFGKSYEFLPLMFTSSYSAIGVVGSWVGFMVVYFTS
The following text describes a protein:
Function:
E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation. Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs. This ubiquitination results in the suppressed expression of miR-138-5p leading to increased autophagy. Upon enteroviral infection, promotes 'Lys-63'-mediated ubiquitination activation of IFIH1/MDA5 leading to innate signaling cascade. Mechanistically, selectively recognizes MDA5 filaments that occur on dsRNAs. Plays also a role in limitation of inflammation through different mechanisms. First, promotes 'Lys-48'-mediated ubiquitination of VCAM1 leading to its degradation and limitation of LPS-induced lung inflammation. In addition, negatively regulates inflammasome activation by promoting 'lys48'-linked ubiquitination of NLRP3 which is critical for the inhibition of NLRP3 inflammasome activation in resting macrophages.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVCPLRRKLWQNYRNLTFDPVSANRHFYLSRQDQQVKHCRQSRGPGGPGSFELWQVQCAQSFQAGHHYWEVRASDHSVTLGVSYPQLPRCRLGPHTDNIGRGPCSWGLCVQEDSLQAWHNGEAQRLPGVSGRLLGMDLDLASGCLTFYSLEPQTQPLYTFHALFNQPLTPVFWLLEGRTLTLCHQPGAVFPLGPQEEVLS
The following text describes a protein:
Function:
Component of the ceramide synthase complex required for C26-CoA-dependent ceramide synthesis. Facilitates ER-to-Golgi transport of GPI-anchored proteins (By similarity). Has a role in meiosis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGNNTSRRSQSQKFKNIPSISAGSFSTMPVQHRGRRRRSKSIVGRAAQNAVLRSKEKTWIVPLILLTLLVGWYFVNPNGYIKYGIFLSYPIPGTNPAQYGKGRLDIAFCLFYALFFTFCREFIMQEIIARIGRHFNIRAPAKLRRFEEQAYTCLYFTVMGSWGLYVMKQTPMWFFNTDAFWEEYPHFYHVGSFKAFYLIEAAYWIQQALVLILQLEKPRKDFKELVVHHIITLLLIGLSYYFHFTWIGLAVFITMDTSDIWLALSKCLNYVNTVIVYPIFVIFVFVWIYMRHYLNFKIMWAVWGTMRTINSFDLDWAAEQYKCWISRDVTLILLTALQLVNIYWLILILRIGYRAFTTNDTHDERSEDEDEEVSDEKSSAKKND
The following text describes a protein:
Function:
Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Subcellular Localization:
Fimbrium.
Sequence:
MKIKTLAIVVLSALSLSSTAALAAATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQVRTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSATNVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQYQ
The following text describes a protein:
Function:
As part of the augmin complex, plays a role in centrosome-independent generation of spindle microtubules. The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle.
Sequence:
METNVDFSSISSKLYRKYAQHVRNLKDVCVSKTVMKPGAFFDSLQQMMEEEAAATTPPRDLSSVADYAELFKTLEEYPANLQKMPKKRELQRTNSTLLRGADESVAMGINTSNVSLSLTRLEEQRSAVDVYNDFKGFQRKLAKIYDEAAALDTTESIYKQKLTQLHGFAQQLEKLMPTGGESPPDAFTSEQQEKLLTIAANMEQLNYLRSNSLQLPNPNEILATGSLAARLEMFVEVLTYTLLQVSSYNMAMI
The following text describes a protein:
Function:
Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex. Promotes the localization of SACM1L at endoplasmic reticulum-plasma membrane contact sites (EPCS).
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSGARGEGPEAGAGGAGGRAAPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDVPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPVPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSRVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSNPLEFNPDVLKKTAVQRALKSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQCSLGNLKVPLSQLLTSEDMTVSQRFQLSNSGPNSTIKMKIALRVLHLEKRERPPDHQHSAQVKRPSVSKEGRKTSIKSHMSGSPGPGGSNTAPSTPVIGGSDKPGMEEKAQPPEAGPQGLHDLGRSSSSLLASPGHISVKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHACRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVALASEELAKGWTQWYDLTEDGTRPQAMT
The following text describes a protein:
Function:
Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons. In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination. Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots. Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Note=Localized into a broader band at the endodermal plasma membrane, embedding growing CASP microdomains. In endodermal cells, first observed on all cell sides, but quickly relocated in the transversal and anticlinal sides of the plasma membrane, but excluded from the Casparian strip membrane domain (CSD).
Sequence:
MQPLVLLLLFILCFSGLGQPGIINNDLQTLLEVKKSLVTNPQEDDPLRQWNSDNINYCSWTGVTCDNTGLFRVIALNLTGLGLTGSISPWFGRFDNLIHLDLSSNNLVGPIPTALSNLTSLESLFLFSNQLTGEIPSQLGSLVNIRSLRIGDNELVGDIPETLGNLVNLQMLALASCRLTGPIPSQLGRLVRVQSLILQDNYLEGPIPAELGNCSDLTVFTAAENMLNGTIPAELGRLENLEILNLANNSLTGEIPSQLGEMSQLQYLSLMANQLQGLIPKSLADLGNLQTLDLSANNLTGEIPEEFWNMSQLLDLVLANNHLSGSLPKSICSNNTNLEQLVLSGTQLSGEIPVELSKCQSLKQLDLSNNSLAGSIPEALFELVELTDLYLHNNTLEGTLSPSISNLTNLQWLVLYHNNLEGKLPKEISALRKLEVLFLYENRFSGEIPQEIGNCTSLKMIDMFGNHFEGEIPPSIGRLKELNLLHLRQNELVGGLPASLGNCHQLNILDLADNQLSGSIPSSFGFLKGLEQLMLYNNSLQGNLPDSLISLRNLTRINLSHNRLNGTIHPLCGSSSYLSFDVTNNGFEDEIPLELGNSQNLDRLRLGKNQLTGKIPWTLGKIRELSLLDMSSNALTGTIPLQLVLCKKLTHIDLNNNFLSGPIPPWLGKLSQLGELKLSSNQFVESLPTELFNCTKLLVLSLDGNSLNGSIPQEIGNLGALNVLNLDKNQFSGSLPQAMGKLSKLYELRLSRNSLTGEIPVEIGQLQDLQSALDLSYNNFTGDIPSTIGTLSKLETLDLSHNQLTGEVPGSVGDMKSLGYLNVSFNNLGGKLKKQFSRWPADSFLGNTGLCGSPLSRCNRVRSNNKQQGLSARSVVIISAISALTAIGLMILVIALFFKQRHDFFKKVGHGSTAYTSSSSSSQATHKPLFRNGASKSDIRWEDIMEATHNLSEEFMIGSGGSGKVYKAELENGETVAVKKILWKDDLMSNKSFSREVKTLGRIRHRHLVKLMGYCSSKSEGLNLLIYEYMKNGSIWDWLHEDKPVLEKKKKLLDWEARLRIAVGLAQGVEYLHHDCVPPIVHRDIKSSNVLLDSNMEAHLGDFGLAKVLTENCDTNTDSNTWFACSYGYIAPEYAYSLKATEKSDVYSMGIVLMEIVTGKMPTDSVFGAEMDMVRWVETHLEVAGSARDKLIDPKLKPLLPFEEDAACQVLEIALQCTKTSPQERPSSRQACDSLLHVYNNRTAGYKKL
The following text describes a protein:
Function:
Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Miscellaneous:
MISCELLANEOUS: Present with 6990 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT1 phosphatase activity.
Sequence:
MSTPTAADRAKALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQSIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKNIKAYHRRALSCMALLEFKKARKDLNVLLKAKPNDPAATKALLTCDRFIREERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPKLEFEQLYDDKNAFKGAKIKNMSQEFISKMVNDLFLKGKYLPKKYVAAIISHADTLFRQEPSMVELENNSTPDVKISVCGDTHGQFYDVLNLFRKFGKVGPKHTYLFNGDFVDRGSWSCEVALLFYCLKILHPNNFFLNRGNHESDNMNKIYGFEDECKYKYSQRIFNMFAQSFESLPLATLINNDYLVMHGGLPSDPSATLSDFKNIDRFAQPPRDGAFMELLWADPQEANGMGPSQRGLGHAFGPDITDRFLRNNKLRKIFRSHELRMGGVQFEQKGKLMTVFSAPNYCDSQGNLGGVIHVVPGHGILQAGRNDDQNLIIETFEAVEHPDIKPMAYSNGGFGL
The following text describes a protein:
Function:
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLAGGVPHGTVAFAYLAVVFAVTGINHLDGVADAGDAAVVHGDPADRRTVLKDTTTGVGAIAAVVVVVAGLVTGSLGVAALPTWTAVGVVVATEVGAKTSMAAVACLAHAPHDGLGSQFTGNATPGALPAVAGVALPVALASVPSPAAAGALAGAVGAGALTRRWLTGLLGGANGDVFGAVNEVSRVVGLHAGVVVWTL
The following text describes a protein:
Function:
Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash (Ref.2). Hydrolyzes short chain esters from acetate (C2) to hexanoate (C6), showing more specificity for shorter chain exters. No activity for decanoate (C10) esters.
Sequence:
MDYEKFLLFGDSITEFAFNTRPIEDGKDQYALGAALVNEYTRKMDILQRGFKGYTSRWALKILPEILKHESNIVMATIFLGANDACSAGPQSVPLPEFIDNIRQMVSLMKSYHIRPIIIGPGLVDREKWEKEKSEEIALGYFRTNENFAIYSDALAKLANEEKVPFVALNKAFQQEGGDAWQQLLTDGLHFSGKGYKIFHDELLKVIETFYPQYHPKNMQYKLKDWRDVLDDGSNIMS
The following text describes a protein:
Function:
S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD(+) into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.
Miscellaneous:
MISCELLANEOUS: Thiol:disulfide oxidoreductases DsbA and DsbB are required for periplasmic toxin assembly, whereas DbsC is important for extracellular toxin secretion; MISCELLANEOUS: Experiments with temporal expression of PTX indicate that holotoxin secretion is at a rate of 3 molecules/min/cell. Also, more of toxin chains S1, S2 and S3 are produced than secreted; one half of each chain is incorporated into holotoxin.
Subcellular Localization:
Secreted. Note=The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.
Domain:
The region which spans amino acids 42-49 is required for enzymatic activity and contributes to the formation of a potentially important antigenic determinant.
Sequence:
MRCTRAIRQTARTGWLTWLAILAVTAPVTSPAWADDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF
The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MLSKQKHVTWFHVILFTTLIPLQRRVNGNPLVMDPNSICRKTRMLAGRHTDLCQSQPEIIQEVAKGARLGIRECQHQFHNHRWNCTSQGRNLAKILQQDIRETAFVYAVTAAGVMHAVTQACSQGALPQCGCVTLQSSSETYRVSPAEEVLIQASSLHDWHWEWGGCGDDVDFGYEKSRQFMDIRQRKGKSDIRSLIDLHNNEAGRVAIQIQMRTECKCHGLSGSCTLRSCWKKMPLFRQVGDQLMQSFHTAVRVMGGNDGKSLVSIDPDAPPLDANVLIYSAESPDFCKANHRSGTEGTGGRACNRTETGPGGCDSLCCGNGFADFTVEEEENCECRFHWCCEVQCQTCSQRKNVSLCL
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; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNLTFLGLCIACMGVSVGEGLLMNGLFKSVARQPDMLSEFRSLMFLGVAFIEGTFFVTLVFSFIIK
The following text describes a protein:
Function:
May be involved in the reorganization of actin cytoskeleton mediated by RND1, RND2 and RND3. Promotes RHOA activation mediated by GNA12 and GNA13.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSTPLASLSKLRRVPLQQDTQSTGRRSLPSRMRVFGEDEDELPSDGHGSEEKSYGCSPEKSFQMGRTVEETEAEIKCSCSIAHGHRSLPHDMGLISTLVKRVTELEQKVKMQAEENNVKDQWIKNLKSKLKNLQIDKGEQRLSIHTEELEAKCQRLQNQVQEMERFLNDYGLEWVGEPSEIEMEMETDLEPEKWTLKKLWKPGDSTVPPKVDFDELLENLRDLSLLAGEGQSLVHTSSSMAVLKTPEPVPLTLYQNGIIMFNGPFRPFSDVSTQQCIQDILDGFFPSELKKIYPNGVPFQVTDLRNVVYQEKHLPKAFSGPGYVIGSMNSKESEKLHEPVTDSIPFVGNTTFSQPPTLTKEQFLRKLPKFVIRHGEVIEVREPIRETMEGCSGTQEILVETERLRQTSSSPAPPEFPTVTLRIKSENGEQSFVLPMSPLDTIGDVRRYLAQARDMDPAMFEIFSVFPNTVYADDSKTLQACGLVPNAILLLRPPKNPHSAPSL
The following text describes a protein:
Function:
Probable guanine nucleotide exchange factor which regulates the Rho GTPase rho-1. Functions in ASE sensory neurons where it promotes neuronal degeneration under conditions of oxidative stress.
Sequence:
MLNPNDADDSDSSTDSSPPVAVPRPKRSATVSPSTRNSFYNSRRRSDANLNFFNERERQRERRRSMVRASRERSESRRASQQNLRKTNSEPNVDMPSIDVEALQKLLLSIPKFVSASRNRINQRHDSDSGGEMTTEIEELKDAAKSIQSLQRVLAYPSQTSSDRGGNRRLADPVESCLESSVFSDVDESSLATDTIEGRRSGISTRLGHPRGVMQFIPSIRNDQFVPTSEIRRNSISRKSSVPDGFMTSEMESEPVPNVRNRRRGIVDEMFSSSTSLLVDRPSETLAGVNRFAKLLDTFRSRPTSPEQHPSISWNPYVYSDGGEALETCGMEDSLHEADILLWKKRSRASLRRHYSVRHLAARELLDTEKSFVEGLEFLVTKYMRPLRQPLECTLIEASLVDKIFYRIPEILAHHQVLLTTLSQRIDQWHKDAILGDVLLAHFSKQSMIETYISFVDNFKFAKASIIQARQKHAFEKYYNRCCRDHPNKLDLDSLLISPIQRVPRYELIVKQMLKHTPVEHEDRERLLRAQRHIHCLAVAINQHKDGSEQMEQRLREIEAIVDGLDDLVTKDRTLLRHDIITLKGTDRERCIFMLSDLLLVTSVKKKPKVLYSKMSSQSMGFLEGNRFKLLFKVALEDVQISKDTLSQLEEVERKLESSREDDRVLKKMSQLCSLLKCERKVLMEMLETMETSNSMSIRELNEQMSSDPDLSAVHLDVLTSNGFEPFVLEFPNAEKRSVFEAMFKDAKATLAKNLLAAPSCSLKTIIAHQTRPGLQLCTATVVPGKRVDSTPSLWVCASDKFSGQVAVMALDTGEITIESCSAIGNAAVTAMCTVPPPMKLRKRKIKSQKSLEHLLNETIMDINSSGSDTESSSDEGTSTAGQTTVWIGNDDGEVFVVNSTERVRSRARDRLARLRNSITSICAANGNVLVATSYSNQVQLLLFRPASDGSWDLENPQTVGHVCQAPITSMQLIGRRVIIASGNWLHAYFVDTGKFQPPVEILPSSDVITLMYVTGQNVFLCGRKSTEVFVVDVFNLSIINHFNVVSFVRSQLSGREHILREHKMGCLRISCLTVARSHLWIGTSAGCVLSTSVQSARSQPTPDLRVCEIGHSGPCRILLPVHTPSHSNHPSRKQKRSSLNVPAQQSSQLMLVSCGEGLDDGTATQDPSTDAINHLIFWKCS
The following text describes a protein:
Function:
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MNSIKNHLMCEEINKRFNLHPKVREAMESIEREVFVPAPFKHFAYTLNALSMQAQQYISSPLTVAKMTQYLEIDHVDSVLEIGCGSGYQAAVLSQIFRRVFSIERIESLYIEARLRLKTLGLDNVHVKFADGNKGWEQYAPYDRILFSACAKNIPQALIDQLEEGGILVAPIQENNEQVIKRFVKQNNALRVQKVLEKCLFVPVVDGVQ
The following text describes a protein:
Function:
Rho GTPase-activating protein involved in the signal transduction pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSQVKGDSLKIIRNVFSKVSAIKSDTITASIRGENDSIQEFRIDIILNHILFTGTLGVLSSSLSTPNSCNSPLIGMRPHKSDIVLLEKAQIFAVPLISSMNYNVVESTIAISGIYGIPIITMDNTNTPHLKVAEKLVITRASNEFIQKTTIILDNINKFEQPILSIPYIPLFGQPLKNVMLCHRPLDNLQVPYFVFTASRYLENCATNEVGIFRLSGDAKEMKIIRKSIEEGIEVDWTQYNIHSITNIIKQFFREMPDGLVNSFDMNILIKSIENDSNETDALVHLKEALNQIYKPSHDILDILSHLVNRILFCQEITLMNEKNLLICLSPSLRIQAKVLSLILFHHDNLFDKFTTKYSLR
The following text describes a protein:
Function:
Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD1 may act as a transcription factor that exert a negative effect on the expression of several genes that are transcribed by RNA polymerase II.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, may also transiently localize to the nucleus.
Sequence:
MDQAKLARMQASVRIGTFCSFLWIFEVLESESVFSADGFQAHHLGNVIGKGTPRRKVKKVHKSSGADDKKLQTTLKKMNVQPIQAIEEVNMFKEDGNVIHFAAPKVHASVPSNTFALYGNGEEKELTELVPGILNQLGPDSLASLRKLAESYQNMQKQAGAEGKKDEDEDDIPDLVEGENFESNVE
The following text describes a protein:
Function:
Catalyzes the transfer of a 4'-phosphopantetheine moiety from coenzyme A to a serine residue of acceptor proteins, such as alpha-aminoadipate reductase. Necessary for alpha-aminoadipate reductase activity.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKQKVYRLLIDTQEAWPFERTRIPSFKKLSDSERQQIERYYFDMDAKMALASILIKRHLVSTALECSPNEVQISVTKAGRPYCQSAHCPPIIFDFNVSHYGGIVIVVGAWLPSDPSGMRPINIGVDIVECKPLAFEASWMEDFMSVFTPCEWKLIKSSISSIDVFFLLWTCKEAILKALGIGLSGNPLDIVVTFHKLNELLNSEEVSLRRAATAVYSGYSWDLEIHKLILHSSTFYVSVAFPQDCVIMDLNWETLNDL