TB10A_MOUSE
ID TB10A_MOUSE Reviewed; 500 AA.
AC P58802;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=TBC1 domain family member 10A;
DE AltName: Full=EBP50-PDX interactor of 64 kDa;
DE Short=EPI64 protein;
GN Name=Tbc1d10a; Synonyms=Epi64, Tbc1d10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA Reczek D., Bretscher A.;
RT "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL J. Cell Biol. 153:191-206(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-40; SER-45 AND
RP THR-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as GTPase-activating protein for RAB27A. {ECO:0000250}.
CC -!- SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000250}.
CC Note=Localizes to the microvilli-rich region of the
CC syncytiotrophoblast. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, except for skeletal
CC muscle. {ECO:0000269|PubMed:11285285}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
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DR EMBL; BC018300; AAH18300.1; -; mRNA.
DR CCDS; CCDS56756.1; -.
DR RefSeq; NP_598784.1; NM_134023.1.
DR AlphaFoldDB; P58802; -.
DR SMR; P58802; -.
DR BioGRID; 222145; 4.
DR STRING; 10090.ENSMUSP00000036861; -.
DR iPTMnet; P58802; -.
DR PhosphoSitePlus; P58802; -.
DR CPTAC; non-CPTAC-3434; -.
DR EPD; P58802; -.
DR jPOST; P58802; -.
DR MaxQB; P58802; -.
DR PaxDb; P58802; -.
DR PeptideAtlas; P58802; -.
DR PRIDE; P58802; -.
DR ProteomicsDB; 263069; -.
DR DNASU; 103724; -.
DR Ensembl; ENSMUST00000180088; ENSMUSP00000136453; ENSMUSG00000034412.
DR GeneID; 103724; -.
DR KEGG; mmu:103724; -.
DR UCSC; uc007huq.1; mouse.
DR CTD; 83874; -.
DR MGI; MGI:2144164; Tbc1d10a.
DR VEuPathDB; HostDB:ENSMUSG00000034412; -.
DR eggNOG; KOG2221; Eukaryota.
DR GeneTree; ENSGT00940000157386; -.
DR HOGENOM; CLU_005350_2_0_1; -.
DR InParanoid; P58802; -.
DR OrthoDB; 976276at2759; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 103724; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tbc1d10a; mouse.
DR PRO; PR:P58802; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P58802; protein.
DR Bgee; ENSMUSG00000034412; Expressed in lip and 207 other tissues.
DR ExpressionAtlas; P58802; baseline and differential.
DR Genevisible; P58802; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Cell projection; GTPase activation; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..500
FT /note="TBC1 domain family member 10A"
FT /id="PRO_0000208036"
FT DOMAIN 111..299
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..500
FT /note="Binding to the PDZ domain of EBP50"
FT /evidence="ECO:0000250"
FT COMPBIAS 479..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 156
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXI6"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 500 AA; 56202 MW; 15954DB7A4E3A9B6 CRC64;
MAKSSRENGP REPAAGGSLS GTRESLAQGP DAATADELSS LGSDSEANGF AERRIDKFGF
IVGSQGAEGA LEEVPLEVLR QRESKWLDML NNWDKWMAKK HKKIRLRCQK GIPPSLRGRA
WQYLSGGKVK LQQNPGKFDE LDMSPGDPKW LDVIERDLHR QFPFHEMFVS RGGHGQQDLF
RVLKAYTLYR PEEGYCQAQA PIAAVLLMHM PAEQAFWCLV QVCEKYLPGY YSEKLEAIQL
DGEILFSLLQ KVSPVAHKHL SRQKIDPLLY MTEWFMCAFA RTLPWSSVLR VWDMFFCEGV
KIIFRVGLVL LKHALGSPEK LKACQGQYET IEQLRSLSPK IMQEAFLVQE VIELPVTERQ
IEREHLIQLR RWQETRGELE CRSLPRMHGA KAILDAEPGP RPALQPSPSI RLPPDAALLS
SKAKPHKQAQ KEQKRTKTSA QLDKSPGLSQ ATVVTAAGDA CPPQGVSPKD PVPQDPTPQN
LACHHSQESL TSQESEDTYL
