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   24-JAN-2024, entry version 160.
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,
RC   Pancreas, 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; 7.
DR   IntAct; Q61599; 2.
DR   STRING; 10090.ENSMUSP00000032344; -.
DR   iPTMnet; Q61599; -.
DR   PhosphoSitePlus; Q61599; -.
DR   SwissPalm; Q61599; -.
DR   CPTAC; non-CPTAC-3815; -.
DR   EPD; Q61599; -.
DR   jPOST; Q61599; -.
DR   MaxQB; Q61599; -.
DR   PaxDb; 10090-ENSMUSP00000032344; -.
DR   PeptideAtlas; Q61599; -.
DR   ProteomicsDB; 266788; -.
DR   Pumba; Q61599; -.
DR   TopDownProteomics; Q61599; -.
DR   Antibodypedia; 12089; 572 antibodies from 39 providers.
DR   DNASU; 11857; -.
DR   Ensembl; ENSMUST00000032344.12; ENSMUSP00000032344.6; ENSMUSG00000030220.14.
DR   Ensembl; ENSMUST00000111891.4; ENSMUSP00000107522.2; ENSMUSG00000030220.14.
DR   Ensembl; ENSMUST00000111892.8; ENSMUSP00000107523.2; ENSMUSG00000030220.14.
DR   GeneID; 11857; -.
DR   KEGG; mmu:11857; -.
DR   UCSC; uc009emo.2; mouse.
DR   AGR; MGI:101940; -.
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; YKPTAAK; -.
DR   OrthoDB; 21211at2759; -.
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 81 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 193 other cell types or tissues.
DR   ExpressionAtlas; Q61599; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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: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; Coagulation Factor XIII, subunit A, domain 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR000406; Rho_GDI.
DR   InterPro; IPR024792; RhoGDI_dom_sf.
DR   PANTHER; PTHR10980; RHO GDP-DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR10980:SF15; RHO GDP-DISSOCIATION INHIBITOR 2; 1.
DR   Pfam; PF02115; Rho_GDI; 1.
DR   PRINTS; PR00492; RHOGDI.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   COMPLUYEAST-2DPAGE; Q61599; -.
DR   Genevisible; Q61599; MM.
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
//