GDIR2_MOUSE
ID GDIR2_MOUSE Reviewed; 200 AA.
AC Q61599; Q3TEB3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Rho GDP-dissociation inhibitor 2;
DE Short=Rho GDI 2;
DE AltName: Full=D4;
DE AltName: Full=Rho-GDI beta;
GN Name=Arhgdib; Synonyms=Gdid4;
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], AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss;
RX PubMed=7512369; DOI=10.1002/gcc.2870080408;
RA Adra C.N., Ko J., Leonard D., Wirth L.J., Cerione R.A., Lim B.;
RT "Identification of a novel protein with GDP dissociation inhibitor activity
RT for the ras-like proteins CDC42Hs and rac I.";
RL Genes Chromosomes Cancer 8:253-261(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Regulates the GDP/GTP exchange reaction of the Rho proteins
CC by inhibiting the dissociation of GDP from them, and the subsequent
CC binding of GTP to them. Regulates reorganization of the actin
CC cytoskeleton mediated by Rho family members.
CC {ECO:0000250|UniProtKB:P52566}.
CC -!- SUBUNIT: Interacts with RHOA. Interacts with RAC1. Interacts with RAC2.
CC Interacts with CDC42. {ECO:0000250|UniProtKB:P52566}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P52566}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in hematopoietic cells.
CC {ECO:0000269|PubMed:7512369}.
CC -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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DR EMBL; L07918; AAA61613.1; -; mRNA.
DR EMBL; AK002516; BAB22155.1; -; mRNA.
DR EMBL; AK169733; BAE41335.1; -; mRNA.
DR EMBL; BC031763; AAH31763.1; -; mRNA.
DR CCDS; CCDS20661.1; -.
DR PIR; I49687; I49687.
DR RefSeq; NP_001288230.1; NM_001301301.1.
DR RefSeq; NP_001288232.1; NM_001301303.1.
DR RefSeq; NP_001288234.1; NM_001301305.1.
DR RefSeq; NP_001288237.1; NM_001301308.1.
DR RefSeq; NP_001288238.1; NM_001301309.1.
DR RefSeq; NP_031512.1; NM_007486.5.
DR RefSeq; XP_006505467.1; XM_006505404.3.
DR AlphaFoldDB; Q61599; -.
DR SMR; Q61599; -.
DR BioGRID; 198201; 6.
DR IntAct; Q61599; 2.
DR STRING; 10090.ENSMUSP00000032344; -.
DR iPTMnet; Q61599; -.
DR PhosphoSitePlus; Q61599; -.
DR SwissPalm; Q61599; -.
DR COMPLUYEAST-2DPAGE; Q61599; -.
DR CPTAC; non-CPTAC-3815; -.
DR EPD; Q61599; -.
DR jPOST; Q61599; -.
DR MaxQB; Q61599; -.
DR PaxDb; Q61599; -.
DR PeptideAtlas; Q61599; -.
DR PRIDE; Q61599; -.
DR ProteomicsDB; 266788; -.
DR TopDownProteomics; Q61599; -.
DR Antibodypedia; 12089; 540 antibodies from 39 providers.
DR DNASU; 11857; -.
DR Ensembl; ENSMUST00000032344; ENSMUSP00000032344; ENSMUSG00000030220.
DR Ensembl; ENSMUST00000111891; ENSMUSP00000107522; ENSMUSG00000030220.
DR Ensembl; ENSMUST00000111892; ENSMUSP00000107523; ENSMUSG00000030220.
DR GeneID; 11857; -.
DR KEGG; mmu:11857; -.
DR UCSC; uc009emo.2; mouse.
DR CTD; 397; -.
DR MGI; MGI:101940; Arhgdib.
DR VEuPathDB; HostDB:ENSMUSG00000030220; -.
DR eggNOG; KOG3205; Eukaryota.
DR GeneTree; ENSGT00390000006233; -.
DR HOGENOM; CLU_076228_1_1_1; -.
DR InParanoid; Q61599; -.
DR OMA; HLKFEWS; -.
DR OrthoDB; 1265661at2759; -.
DR PhylomeDB; Q61599; -.
DR TreeFam; TF105387; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 11857; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Arhgdib; mouse.
DR PRO; PR:Q61599; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61599; protein.
DR Bgee; ENSMUSG00000030220; Expressed in granulocyte and 190 other tissues.
DR ExpressionAtlas; Q61599; baseline and differential.
DR Genevisible; Q61599; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:1901164; P:negative regulation of trophoblast cell migration; ISO:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.70.50.30; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR PANTHER; PTHR10980; PTHR10980; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT CHAIN 2..200
FT /note="Rho GDP-dissociation inhibitor 2"
FT /id="PRO_0000219017"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 23
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
FT MOD_RES 174
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52566"
SQ SEQUENCE 200 AA; 22851 MW; EA78C965F1AB6F5C CRC64;
MTEKDAQPQL EEADDDLDSK LNYKPPPQKS LKELQEMDKD DESLTKYKKT LLGDVPVVAD
PTVPNVTVTR LSLVCDSAPG PITMDLTGDL EALKKDTFVL KEGIEYRVKI NFKVNKDIVS
GLKYVQHTYR TGMRVDKATF MVGSYGPRPE EYEFLTPVEE APKGMLARGT YHNKSFFTDD
DKQDHLTWEW NLAIKKDWTE
