GIT2_RAT
ID GIT2_RAT Reviewed; 759 AA.
AC Q66H91;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP INTERACTION WITH GIT1 AND PCLO.
RX PubMed=12473661; DOI=10.1074/jbc.m212287200;
RA Kim S., Ko J., Shin H., Lee J.R., Lim C., Han J.H., Altrock W.D.,
RA Garner C.C., Gundelfinger E.D., Premont R.T., Kaang B.K., Kim E.;
RT "The GIT family of proteins forms multimers and associates with the
RT presynaptic cytomatrix protein Piccolo.";
RL J. Biol. Chem. 278:6291-6300(2003).
RN [4]
RP INTERACTION WITH PPFIA1 AND PPFIA2.
RX PubMed=12629171; DOI=10.1523/jneurosci.23-05-01667.2003;
RA Ko J., Kim S., Valtschanoff J.G., Shin H., Lee J.R., Sheng M.,
RA Premont R.T., Weinberg R.J., Kim E.;
RT "Interaction between liprin-alpha and GIT1 is required for AMPA receptor
RT targeting.";
RL J. Neurosci. 23:1667-1677(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (Probable). Directly
CC interacts with protein Piccolo/PCLO (PubMed:12473661). Interacts with
CC PPFIA1 and PPFIA2 (PubMed:12629171). 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 (By similarity).
CC Forms a complex with EFNB1 and GRB4/NCK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q14161, ECO:0000250|UniProtKB:Q9JLQ2,
CC ECO:0000269|PubMed:12473661, ECO:0000269|PubMed:12629171,
CC ECO:0000305|PubMed:12473661}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC095845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081967; AAH81967.1; -; mRNA.
DR RefSeq; NP_001005553.1; NM_001005553.1.
DR AlphaFoldDB; Q66H91; -.
DR SMR; Q66H91; -.
DR STRING; 10116.ENSRNOP00000048331; -.
DR PhosphoSitePlus; Q66H91; -.
DR jPOST; Q66H91; -.
DR PaxDb; Q66H91; -.
DR PRIDE; Q66H91; -.
DR ABCD; Q66H91; 1 sequenced antibody.
DR GeneID; 304546; -.
DR KEGG; rno:304546; -.
DR UCSC; RGD:1359708; rat.
DR CTD; 9815; -.
DR RGD; 1359708; Git2.
DR VEuPathDB; HostDB:ENSRNOG00000001190; -.
DR eggNOG; KOG0818; Eukaryota.
DR HOGENOM; CLU_009739_0_0_1; -.
DR InParanoid; Q66H91; -.
DR OMA; ELWMAMQ; -.
DR OrthoDB; 349344at2759; -.
DR PhylomeDB; Q66H91; -.
DR TreeFam; TF317762; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
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; ISO:RGD.
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; IPR032352; GIT1/2_CC.
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; PF16559; GIT_CC; 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 ANK repeat; Coiled coil; GTPase activation; Metal-binding;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..759
FT /note="ARF GTPase-activating protein GIT2"
FT /id="PRO_0000452577"
FT DOMAIN 1..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 132..161
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023"
FT REPEAT 166..198
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023"
FT REPEAT 199..228
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023"
FT ZN_FING 11..34
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 376..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..478
FT /evidence="ECO:0000255"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 84525 MW; 4FCA85ED7999B01F CRC64;
MSKRLRSNDV CADCSGPDPS WASVNRGTLI CDECCSVHRS LGRHISQVRH LKHTPWPPTL
LQMVETLYSN GANSIWEHSL LDPASVMSGR RKANPQDKVH PNKAEFIRAK YQMLAFVHRL
PCRDDDSVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGSTP LHVASKAGQI
LQAELLAVYG ADPGTHDSSG KTPVDYARQG GHRELAERLV EIQYELTDRL AFYLCGRKPD
HKNGQHFIIP QMADSSLDLS ELAKAAKKKL QSLSNHLFEE LAMDVYDEVD RRETDAVWLA
TQNHSTLVTE TTVVPFLPVN PEYSSTRNQG RQKLARFNAH EFATLVIDIL SDAKRRQQGS
PLSRSKDNVE LILRTVSNQH STESQDNDQP DYDSVASDED TDVETRASRT NRQKSLDSDL
SDGPVTVQEF MEVKHALVAS EAKRQQLMKV NNNLSGELRI MQKKLQTLQS ENSSLRRQAT
ASACQVQTAS DHKDTVSHSS LKRRPSARGS RPMSMYETGS GQKPYLPMGE ANHPEESRTR
LQPFPTHIGR SALVTSSSSL PSFPSTLSWS RDESTRRASR LEKQNSTPES DYDNTAYDPE
PDDTVSGRKG RQRSMLWQGD GPLPDTAEPH AVPSPALPST EDVIRKTEQI TKNIQELLRA
AQENKHDSYI PCSERIHAAV TEMAALFPKK PKSDTVRTSL RLLTASAYRL QSECRKALPG
DSSLPTDVQL VTQQVIQCAY DIAKAAKQLV TITTKENSS
