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TBC1 domain family member 10A (EBP50-PDX interactor of 64 kDa) (EPI64 protein)

 TB10A_MOUSE             Reviewed;         500 AA.
P58802;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 1.
10-MAY-2017, entry version 111.
RecName: Full=TBC1 domain family member 10A;
AltName: Full=EBP50-PDX interactor of 64 kDa;
Short=EPI64 protein;
Name=Tbc1d10a; Synonyms=Epi64, Tbc1d10;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
TISSUE SPECIFICITY.
PubMed=11285285; DOI=10.1083/jcb.153.1.191;
Reczek D., Bretscher A.;
"Identification of EPI64, a TBC/rabGAP domain-containing microvillar
protein that binds to the first PDZ domain of EBP50 and E3KARP.";
J. Cell Biol. 153:191-206(2001).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-40; SER-45 AND
THR-477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as GTPase-activating protein for RAB27A.
{ECO:0000250}.
-!- SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell projection, microvillus {ECO:0000250}.
Note=Localizes to the microvilli-rich region of the
syncytiotrophoblast. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in most tissues, except for skeletal
muscle. {ECO:0000269|PubMed:11285285}.
-!- DOMAIN: The arginine and glutamine fingers are critical for the
GTPase-activating mechanism, they pull out Rab's 'switch 2'
glutamine and insert in Rab's active site. {ECO:0000250}.
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EMBL; BC018300; AAH18300.1; -; mRNA.
CCDS; CCDS56756.1; -.
RefSeq; NP_598784.1; NM_134023.1.
UniGene; Mm.28140; -.
ProteinModelPortal; P58802; -.
SMR; P58802; -.
STRING; 10090.ENSMUSP00000136453; -.
iPTMnet; P58802; -.
PhosphoSitePlus; P58802; -.
EPD; P58802; -.
MaxQB; P58802; -.
PaxDb; P58802; -.
PeptideAtlas; P58802; -.
PRIDE; P58802; -.
Ensembl; ENSMUST00000180088; ENSMUSP00000136453; ENSMUSG00000034412.
GeneID; 103724; -.
KEGG; mmu:103724; -.
UCSC; uc007huq.1; mouse.
CTD; 83874; -.
MGI; MGI:2144164; Tbc1d10a.
eggNOG; KOG2221; Eukaryota.
eggNOG; ENOG410XPSR; LUCA.
GeneTree; ENSGT00860000133698; -.
HOVERGEN; HBG070028; -.
InParanoid; P58802; -.
KO; K19944; -.
Reactome; R-MMU-8854214; TBC/RABGAPs.
ChiTaRS; Tbc1d10a; mouse.
PRO; PR:P58802; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000034412; -.
CleanEx; MM_TBC1D10A; -.
ExpressionAtlas; P58802; baseline and differential.
Genevisible; P58802; MM.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0031338; P:regulation of vesicle fusion; IBA:GO_Central.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
InterPro; IPR000195; Rab-GTPase-TBC_dom.
Pfam; PF00566; RabGAP-TBC; 1.
SMART; SM00164; TBC; 1.
SUPFAM; SSF47923; SSF47923; 2.
PROSITE; PS50086; TBC_RABGAP; 1.
1: Evidence at protein level;
Cell projection; Complete proteome; GTPase activation;
Guanine-nucleotide releasing factor; Phosphoprotein;
Reference proteome.
CHAIN 1 500 TBC1 domain family member 10A.
/FTId=PRO_0000208036.
DOMAIN 111 299 Rab-GAP TBC. {ECO:0000255|PROSITE-
ProRule:PRU00163}.
REGION 497 500 Binding to the PDZ domain of EBP50.
{ECO:0000250}.
SITE 156 156 Arginine finger. {ECO:0000250}.
SITE 197 197 Glutamine finger. {ECO:0000250}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXI6}.
MOD_RES 477 477 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
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


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