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ARF GTPase-activating protein GIT2 (ARF GAP GIT2) (Cool-interacting tyrosine-phosphorylated protein 2) (CAT-2) (CAT2) (G protein-coupled receptor kinase-interactor 2) (GRK-interacting protein 2)

 GIT2_MOUSE              Reviewed;         708 AA.
Q9JLQ2; E9QPU7;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 144.
RecName: Full=ARF GTPase-activating protein GIT2;
Short=ARF GAP GIT2;
AltName: Full=Cool-interacting tyrosine-phosphorylated protein 2;
Short=CAT-2;
Short=CAT2;
AltName: Full=G protein-coupled receptor kinase-interactor 2;
AltName: Full=GRK-interacting protein 2;
Name=Git2;
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 [MRNA].
PubMed=10428811; DOI=10.1074/jbc.274.32.22393;
Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T.,
Taylor S.J., Cerione R.A.;
"A tyrosine-phosphorylated protein that binds to an important
regulatory region on the cool family of p21-activated kinase-binding
proteins.";
J. Biol. Chem. 274:22393-22400(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
INTERACTION WITH TGFB1I1.
PubMed=10330411; DOI=10.1083/jcb.145.4.851;
Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N.,
McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.;
"Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
repeat, ARF-GAP protein: a role in cytoskeletal remodeling.";
J. Cell Biol. 145:851-863(1999).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396 AND THR-400, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-396; SER-511;
SER-519; THR-536 AND SER-563, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
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: GTPase-activating protein for the ADP ribosylation
factor family. {ECO:0000250}.
-!- SUBUNIT: Interacts with G protein-coupled receptor kinases.
Associates with PXN. Also interacts with PIX exchange factors.
Identified in a complex with ARHGEF6 and BIN2 (By similarity).
Interacts with TGFB1I1. {ECO:0000250,
ECO:0000269|PubMed:10330411}.
-!- INTERACTION:
Q9ES28:Arhgef7; NbExp=6; IntAct=EBI-642860, EBI-642580;
-!- PTM: Tyrosine phosphorylated when coexpressed in cells with
PTK2/FAK1 and SRC.
-----------------------------------------------------------------------
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EMBL; AF148693; AAF61633.1; -; mRNA.
EMBL; AC087330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS19570.2; -.
RefSeq; NP_062808.3; NM_019834.3.
UniGene; Mm.195632; -.
ProteinModelPortal; Q9JLQ2; -.
SMR; Q9JLQ2; -.
BioGrid; 204983; 3.
IntAct; Q9JLQ2; 4.
MINT; MINT-1751173; -.
STRING; 10090.ENSMUSP00000107803; -.
iPTMnet; Q9JLQ2; -.
PhosphoSitePlus; Q9JLQ2; -.
EPD; Q9JLQ2; -.
MaxQB; Q9JLQ2; -.
PaxDb; Q9JLQ2; -.
PeptideAtlas; Q9JLQ2; -.
PRIDE; Q9JLQ2; -.
Ensembl; ENSMUST00000112185; ENSMUSP00000107803; ENSMUSG00000041890.
GeneID; 26431; -.
KEGG; mmu:26431; -.
UCSC; uc008yzz.1; mouse.
CTD; 9815; -.
MGI; MGI:1347053; Git2.
eggNOG; KOG0818; Eukaryota.
eggNOG; ENOG410XR8U; LUCA.
GeneTree; ENSGT00900000140990; -.
HOGENOM; HOG000232135; -.
HOVERGEN; HBG012506; -.
InParanoid; Q9JLQ2; -.
KO; K12487; -.
TreeFam; TF317762; -.
PMAP-CutDB; Q9JLQ2; -.
PRO; PR:Q9JLQ2; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000041890; -.
CleanEx; MM_GIT2; -.
ExpressionAtlas; Q9JLQ2; baseline and differential.
Genevisible; Q9JLQ2; MM.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032403; F:protein complex binding; IPI:MGI.
GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001164; ArfGAP.
InterPro; IPR037278; ARFGAP/RecO.
InterPro; IPR022018; GIT1_C.
InterPro; IPR013724; GIT_SHD.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01412; ArfGap; 1.
Pfam; PF12205; GIT1_C; 1.
Pfam; PF08518; GIT_SHD; 2.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00248; ANK; 3.
SMART; SM00105; ArfGap; 1.
SMART; SM00555; GIT; 2.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF57863; SSF57863; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
PROSITE; PS50115; ARFGAP; 1.
1: Evidence at protein level;
ANK repeat; Complete proteome; GTPase activation; Metal-binding;
Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
CHAIN 1 708 ARF GTPase-activating protein GIT2.
/FTId=PRO_0000074204.
DOMAIN 1 124 Arf-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
REPEAT 132 161 ANK 1.
REPEAT 166 195 ANK 2.
REPEAT 199 228 ANK 3.
ZN_FING 11 34 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 400 400 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q14161}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 536 536 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 188 188 V -> E (in Ref. 1; AAF61633).
{ECO:0000305}.
SEQUENCE 708 AA; 78766 MW; B84F4F684182D8CA CRC64;
MSKRLRSSDV CADCNGPDPS WASVNRGTFI CDECCSVHRS LGRHISQVRH LKHTAWPPTL
LQMVETLYNN GANSIWEHSL LDPASIMSGR RKANPQDKVH PNKAEFIRAK YQMLAFVHRL
PCREDDSVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGSTP LHVASKAGQI
LQAELLAVYG ADPGTQDSSG KTPVDYARQG GHHELAERLI EIQYELTDRL AFYLCGRKPD
HKSGQHFLIP QRADSLDLSE LAKAAKKKLQ SLSNHLFEEL AMDVYDEVDR RETDAVWLAT
QNHSTLVTET TVVPFLPVNP EYSSTRNQGR QKLARFNAHE FATLVIDILS DAKRRQQGSP
LSRSKDNVEL ILRTVSTQHS TESQDNDQPD YDSVASDEDT DVETRASKAN RQKLQTLQSE
NSSLRRQATA SACQVQTGSD HKDTASHSSL KRRPSARGSR PMSMYETGSG QKPYLPMGEA
SHPEESRTRL QPFPTHIGRS ALVTSSSSLP SFPSTLSWSR DESARRASRL EKQNSTPESD
YDNTACDPEP DDTGSTRKGR QRSMLWQGDG LLPDTAEPHS VPSPTLPSTE DVIRKTEQIT
KNIQELLRAA QENKHDSYIP CSERIHVAVT EMAALFPKKP KSDTVRTSLR LLTSSAYRLQ
SECRKALPGD SSLPTDVQLV TQQVIQCAYD IAKAAKQLVT ITTKENSS


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