GIT2_MOUSE
ID GIT2_MOUSE Reviewed; 708 AA.
AC Q9JLQ2; E9QPU7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ARF GTPase-activating protein GIT2;
DE Short=ARF GAP GIT2;
DE AltName: Full=Cool-interacting tyrosine-phosphorylated protein 2;
DE Short=CAT-2;
DE Short=CAT2;
DE AltName: Full=G protein-coupled receptor kinase-interactor 2;
DE AltName: Full=GRK-interacting protein 2;
GN Name=Git2;
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 [MRNA].
RX PubMed=10428811; DOI=10.1074/jbc.274.32.22393;
RA Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T.,
RA Taylor S.J., Cerione R.A.;
RT "A tyrosine-phosphorylated protein that binds to an important regulatory
RT region on the cool family of p21-activated kinase-binding proteins.";
RL J. Biol. Chem. 274:22393-22400(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH TGFB1I1.
RX PubMed=10330411; DOI=10.1083/jcb.145.4.851;
RA Turner C.E., Brown M.C., Perrotta J.A., Riedy M.C., Nikolopoulos S.N.,
RA McDonald A.R., Bagrodia S., Thomas S.M., Leventhal P.S.;
RT "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat,
RT ARF-GAP protein: a role in cytoskeletal remodeling.";
RL J. Cell Biol. 145:851-863(1999).
RN [4]
RP INTERACTION WITH EFNB1 AND NCK2, AND TISSUE SPECIFICITY.
RX PubMed=17310244; DOI=10.1038/nn1858;
RA Segura I., Essmann C.L., Weinges S., Acker-Palmer A.;
RT "Grb4 and GIT1 transduce ephrinB reverse signals modulating spine
RT morphogenesis and synapse formation.";
RL Nat. Neurosci. 10:301-310(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396 AND THR-400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-396; SER-511;
RP SER-519; THR-536 AND SER-563, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: GTPase-activating protein for ADP ribosylation factor family
CC members, including ARF1. {ECO:0000250|UniProtKB:Q14161}.
CC -!- SUBUNIT: May form heterooligomers with GIT1 (By similarity). Directly
CC interacts with protein Piccolo/PCLO (By similarity). Interacts with
CC PPFIA1 and PPFIA2 (By similarity). Interacts with ARHGEF7 (By
CC similarity). Identified in a complex with ARHGEF6 and BIN2 (By
CC similarity). Interacts with PAK3 (By similarity). Interacts with
CC PXN/paxillin (By similarity). Interacts with TGFB1I1 (PubMed:10330411).
CC Forms a complex with EFNB1 and GRB4/NCK2 (PubMed:17310244).
CC {ECO:0000250|UniProtKB:Q14161, ECO:0000250|UniProtKB:Q66H91,
CC ECO:0000269|PubMed:10330411, ECO:0000269|PubMed:17310244}.
CC -!- INTERACTION:
CC Q9JLQ2; Q9ES28: Arhgef7; NbExp=6; IntAct=EBI-642860, EBI-642580;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:17310244}.
CC -!- PTM: Tyrosine phosphorylated when coexpressed in cells with PTK2/FAK1
CC and SRC.
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DR EMBL; AF148693; AAF61633.1; -; mRNA.
DR EMBL; AC087330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS19570.2; -.
DR RefSeq; NP_062808.3; NM_019834.3.
DR PDB; 6JMT; X-ray; 2.80 A; A/B/C/D/E/F=1-359.
DR PDBsum; 6JMT; -.
DR AlphaFoldDB; Q9JLQ2; -.
DR SMR; Q9JLQ2; -.
DR BioGRID; 204983; 5.
DR IntAct; Q9JLQ2; 4.
DR MINT; Q9JLQ2; -.
DR STRING; 10090.ENSMUSP00000107803; -.
DR iPTMnet; Q9JLQ2; -.
DR PhosphoSitePlus; Q9JLQ2; -.
DR EPD; Q9JLQ2; -.
DR jPOST; Q9JLQ2; -.
DR MaxQB; Q9JLQ2; -.
DR PaxDb; Q9JLQ2; -.
DR PeptideAtlas; Q9JLQ2; -.
DR PRIDE; Q9JLQ2; -.
DR ProteomicsDB; 265750; -.
DR ABCD; Q9JLQ2; 1 sequenced antibody.
DR Antibodypedia; 30932; 320 antibodies from 35 providers.
DR DNASU; 26431; -.
DR Ensembl; ENSMUST00000112185; ENSMUSP00000107803; ENSMUSG00000041890.
DR GeneID; 26431; -.
DR KEGG; mmu:26431; -.
DR UCSC; uc008yzz.1; mouse.
DR CTD; 9815; -.
DR MGI; MGI:1347053; Git2.
DR VEuPathDB; HostDB:ENSMUSG00000041890; -.
DR eggNOG; KOG0818; Eukaryota.
DR GeneTree; ENSGT00940000156383; -.
DR InParanoid; Q9JLQ2; -.
DR OrthoDB; 349344at2759; -.
DR TreeFam; TF317762; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 26431; 4 hits in 60 CRISPR screens.
DR ChiTaRS; Git2; mouse.
DR PRO; PR:Q9JLQ2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JLQ2; protein.
DR Bgee; ENSMUSG00000041890; Expressed in placenta labyrinth and 253 other tissues.
DR ExpressionAtlas; Q9JLQ2; baseline and differential.
DR Genevisible; Q9JLQ2; MM.
DR GO; GO:0044305; C:calyx of Held; IMP:SynGO.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0036465; P:synaptic vesicle recycling; IBA:GO_Central.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; GTPase activation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="ARF GTPase-activating protein GIT2"
FT /id="PRO_0000074204"
FT DOMAIN 1..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 132..161
FT /note="ANK 1"
FT REPEAT 166..195
FT /note="ANK 2"
FT REPEAT 199..228
FT /note="ANK 3"
FT ZN_FING 11..34
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 376..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14161"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 536
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 188
FT /note="V -> E (in Ref. 1; AAF61633)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6JMT"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:6JMT"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6JMT"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6JMT"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6JMT"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 274..300
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6JMT"
FT HELIX 338..356
FT /evidence="ECO:0007829|PDB:6JMT"
SQ 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
