TBC11_CAEEL
ID TBC11_CAEEL Reviewed; 934 AA.
AC H2KZZ6; A0A4V0IKC0; H2KZZ5; Q5LK42;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Rab GTPase-activating protein tbc-11 {ECO:0000303|PubMed:33826611};
DE Short=RabGAP tbc-11 {ECO:0000303|PubMed:33826611};
DE AltName: Full=TBC1 domain family member 11 {ECO:0000305};
GN Name=tbc-11 {ECO:0000303|PubMed:33826611, ECO:0000312|WormBase:F35H12.2b};
GN ORFNames=F35H12.2 {ECO:0000312|WormBase:F35H12.2b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 323-LYS--ILE-402 AND
RP SER-490.
RX PubMed=33826611; DOI=10.1371/journal.pgen.1009511;
RA Michaud P., Shah V.N., Adjibade P., Houle F., Quevillon Huberdeau M.,
RA Rioux R., Lavoie-Ouellet C., Gu W., Mazroui R., Simard M.J.;
RT "The RabGAP TBC-11 controls Argonaute localization for proper microRNA
RT function in C. elegans.";
RL PLoS Genet. 17:e1009511-e1009511(2021).
CC -!- FUNCTION: Rab GTPase activating protein for the small GTPases rab-6.1
CC and rab-6.2 (Probable). Probably acts through rab-6.1 and rab-6.2 to
CC play a role in microRNA-mediated gene silencing in different tissue
CC types (PubMed:33826611). Required for seam cell division and alae
CC formation (PubMed:33826611). {ECO:0000269|PubMed:33826611,
CC ECO:0000305|PubMed:33826611}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:F35H12.2b};
CC IsoId=H2KZZ6-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F35H12.2a};
CC IsoId=H2KZZ6-2; Sequence=VSP_061182;
CC Name=c {ECO:0000312|WormBase:F35H12.2c};
CC IsoId=H2KZZ6-3; Sequence=VSP_061180, VSP_061182;
CC Name=d {ECO:0000312|WormBase:F35H12.2d};
CC IsoId=H2KZZ6-4; Sequence=VSP_061181, VSP_061182;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC expression of the lin-41 protein, which is a target of the let-7
CC microRNA. {ECO:0000269|PubMed:33826611}.
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DR EMBL; BX284606; CCD70614.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD70615.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD70616.1; -; Genomic_DNA.
DR EMBL; BX284606; VTW47567.1; -; Genomic_DNA.
DR RefSeq; NP_508178.2; NM_075777.4.
DR AlphaFoldDB; H2KZZ6; -.
DR SMR; H2KZZ6; -.
DR STRING; 6239.F35H12.2b; -.
DR EPD; H2KZZ6; -.
DR PaxDb; H2KZZ6; -.
DR EnsemblMetazoa; F35H12.2a.1; F35H12.2a.1; WBGene00018075. [H2KZZ6-2]
DR EnsemblMetazoa; F35H12.2b.1; F35H12.2b.1; WBGene00018075. [H2KZZ6-1]
DR EnsemblMetazoa; F35H12.2c.1; F35H12.2c.1; WBGene00018075. [H2KZZ6-3]
DR EnsemblMetazoa; F35H12.2c.2; F35H12.2c.2; WBGene00018075. [H2KZZ6-3]
DR EnsemblMetazoa; F35H12.2c.3; F35H12.2c.3; WBGene00018075. [H2KZZ6-3]
DR EnsemblMetazoa; F35H12.2c.4; F35H12.2c.4; WBGene00018075. [H2KZZ6-3]
DR EnsemblMetazoa; F35H12.2d.1; F35H12.2d.1; WBGene00018075. [H2KZZ6-4]
DR GeneID; 180444; -.
DR UCSC; F35H12.2b; c. elegans.
DR CTD; 180444; -.
DR WormBase; F35H12.2a; CE30971; WBGene00018075; tbc-11. [H2KZZ6-2]
DR WormBase; F35H12.2b; CE30972; WBGene00018075; tbc-11. [H2KZZ6-1]
DR WormBase; F35H12.2c; CE37909; WBGene00018075; tbc-11. [H2KZZ6-3]
DR WormBase; F35H12.2d; CE53416; WBGene00018075; tbc-11. [H2KZZ6-4]
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000168693; -.
DR HOGENOM; CLU_007394_0_0_1; -.
DR InParanoid; H2KZZ6; -.
DR OMA; KPSQGDC; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; H2KZZ6; -.
DR Reactome; R-CEL-8854214; TBC/RABGAPs.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018075; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; H2KZZ6; baseline and differential.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; GTPase activation; Reference proteome.
FT CHAIN 1..934
FT /note="Rab GTPase-activating protein tbc-11"
FT /id="PRO_0000453576"
FT DOMAIN 16..134
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 422..612
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 337..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 727..800
FT /evidence="ECO:0000255"
FT COILED 861..895
FT /evidence="ECO:0000255"
FT COMPBIAS 337..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..359
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_061180"
FT VAR_SEQ 372
FT /note="E -> ESD (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061181"
FT VAR_SEQ 438..441
FT /note="Missing (in isoform a, isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061182"
FT MUTAGEN 323..402
FT /note="Missing: In ok257; Disrupts seam cell division and
FT alae formation. Reduces the total number of microRNAs and
FT reduces microRNA-mediated gene silencing. Disrupts the
FT localization of alg-1 to endomembranes. Increases the
FT expression of lin-41 protein, which is a target for the
FT let-7 microRNA. Increases the number of animals with a
FT burst vulva phenotype in a let-7 n2853 mutant background.
FT The seam cell division and alae formation defects are
FT suppressed in a rab-6.1 or rab-6.2 RNAi mutant background."
FT /evidence="ECO:0000269|PubMed:33826611"
FT MUTAGEN 490
FT /note="S->P: In qbc24; males are sterile. Disrupts seam
FT cell division and alae formation. Disrupts the localization
FT of alg-1 to endomembranes, and instead alg-1 accumulates in
FT the perinuclear region. Reduces the total number of
FT microRNAs and reduces microRNA-mediated gene silencing.
FT Specifically reduces the association of alg-1 with
FT microRNAs. Increases the expression of lin-41 protein,
FT which is a target for the let-7 microRNA. The seam cell
FT division and alae formation defects are suppressed in a
FT rab-6.1 or rab-6.2 RNAi mutant background. The localization
FT of alg-1 is restored in a rab-6.1 RNAi mutant background."
FT /evidence="ECO:0000269|PubMed:33826611"
SQ SEQUENCE 934 AA; 108279 MW; BD54B046526C970C CRC64;
MEDFKDFTEV TQFTNVQYLG CSQLVNNDND NEMKALMKVL DEQKGAQTIN VTLVVPHNIS
GTVKLIDAQG KVLSSFSLVN IRFCIRGESS TSQNNCFGIS FTHKISVGEH NSSDILHQCH
VFRTSKAETA AKALYSFSYA FSNKNVSSES NRLEFQFESI LEVKENDGTV EKPSWKLCPQ
HNGVFKVRRD REKKIVVQLR QIDGFLLNIK KCFGMLLAAG RNLRHSDLQL LEMDRNATGT
DSAVFVIEAN WDPRVHMFEV LNTETPRDTR VFMTVAIDVI VSEISEPIRF SMEAMSRVFH
EHERFYKTPQ TVVSEEFTLV LEKSCDQSDP NDRKLTFISL ESDSDRKRSK QNLGKSPSRM
PTQLLHPTGD DESDCDEPLL SGSGKVSQEC KEEHLEMWDQ LIENWDQQSD RPQKISELVL
DGIPDKLRGR VWQLLSNVRI LAIDQPDLVE KYHIFLSQPC PSEQVIMRDI HRTFPAHDYF
KESQGKGQQS LYKISKVYSL YDEEVSYCQG LSFLAASLLL HMPEEQAFCT LVKIMFNYGL
RDLFKLGFDN LHLRFFQLTA LLKDYIPDLS HHLEHIGIET HMYASQWFLT LFTAKFPLQM
VFFILDLFLS QGMNTIFHIS LALLDDAKTD LLQLDFEGTL KYFRVSLPRK YRTEASTKCL
IHKAVKFRLN HSKLEVYENE YKRIKELERE NEDPVLRMEK EIGRHQANTL RLERENDDLA
HELVTSKIEL RRKLDVAEDQ IETSANAIER LTRQNMDILE ENKNLMREYE QIKEMYRRDV
LRLEENGSRA EKLLAEYKKL FSERSKRAEN EREHFEVQKK AIIARISDCD KCWPAVCEWE
KNRSPVHSAS TPTGPDLLTK LEEREDHIKN LEIDLAQTKL SLVEAECRNQ DLTHQLMAQS
ESDGKKWFKK TITQLKEVGS SLKHHERSNS SVTP
