GDIR3_HUMAN
ID GDIR3_HUMAN Reviewed; 225 AA.
AC Q99819; Q4TT69; Q96S29;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Rho GDP-dissociation inhibitor 3;
DE Short=Rho GDI 3;
DE AltName: Full=Rho-GDI gamma;
GN Name=ARHGDIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9113980; DOI=10.1073/pnas.94.9.4279;
RA Adra C.N., Manor D., Ko J.L., Zhu S., Horiuchi T., van Aelst L.,
RA Cerione R.A., Lim B.;
RT "RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with
RT preferential expression in brain and pancreas.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4279-4284(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9787082; DOI=10.1006/geno.1998.5482;
RA Adra C.N., Iyengar A.R., Syed F.A., Kanaan I.N., Rilo H.L.R., Yu W.,
RA Kheraj R., Lin S.R., Horiuchi T., Khan S., Weremowicz S., Lim B.,
RA Morton C.C., Higgs D.R.;
RT "Human ARHGDIG, a GDP-dissociation inhibitor for Rho proteins: genomic
RT structure, sequence, expression analysis, and mapping to chromosome
RT 16p13.3.";
RL Genomics 53:104-109(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T.,
RA Saito T.;
RT "A human polycistronic mRNA composed of ARHGDIG and PDIP.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
CC -!- FUNCTION: Inhibits GDP/GTP exchange reaction of RhoB. Interacts
CC specifically with the GDP- and GTP-bound forms of post-translationally
CC processed Rhob and Rhog proteins, both of which show a growth-regulated
CC expression in mammalian cells. Stimulates the release of the GDP-bound
CC but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange
CC of RhoB but shows less ability to inhibit the dissociation of prebound
CC GTP.
CC -!- INTERACTION:
CC Q99819; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-10295284, EBI-1012434;
CC Q99819; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-10295284, EBI-743488;
CC Q99819; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-10295284, EBI-739657;
CC Q99819; Q9BTT4: MED10; NbExp=3; IntAct=EBI-10295284, EBI-394354;
CC Q99819; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-10295284, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Primarily expressed in pancreas and brain.
CC -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000305}.
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DR EMBL; U82532; AAC33138.1; -; mRNA.
DR EMBL; AF080237; AAC72354.1; -; Genomic_DNA.
DR EMBL; AB127078; BAE48733.1; -; mRNA.
DR EMBL; AF498928; AAM21076.1; -; mRNA.
DR EMBL; AE006463; AAK61222.1; -; Genomic_DNA.
DR EMBL; Z69667; CAI95584.1; -; Genomic_DNA.
DR EMBL; BC047699; AAH47699.1; -; mRNA.
DR CCDS; CCDS10404.1; -.
DR RefSeq; NP_001167.2; NM_001176.3.
DR AlphaFoldDB; Q99819; -.
DR SMR; Q99819; -.
DR BioGRID; 106891; 16.
DR IntAct; Q99819; 7.
DR MINT; Q99819; -.
DR STRING; 9606.ENSP00000219409; -.
DR PhosphoSitePlus; Q99819; -.
DR BioMuta; ARHGDIG; -.
DR DMDM; 38258951; -.
DR MassIVE; Q99819; -.
DR PaxDb; Q99819; -.
DR PeptideAtlas; Q99819; -.
DR PRIDE; Q99819; -.
DR Antibodypedia; 34941; 173 antibodies from 35 providers.
DR DNASU; 398; -.
DR Ensembl; ENST00000219409.8; ENSP00000219409.3; ENSG00000242173.10.
DR GeneID; 398; -.
DR KEGG; hsa:398; -.
DR MANE-Select; ENST00000219409.8; ENSP00000219409.3; NM_001176.4; NP_001167.2.
DR UCSC; uc002cgm.2; human.
DR CTD; 398; -.
DR DisGeNET; 398; -.
DR GeneCards; ARHGDIG; -.
DR HGNC; HGNC:680; ARHGDIG.
DR HPA; ENSG00000242173; Group enriched (brain, pancreas).
DR MIM; 602844; gene.
DR neXtProt; NX_Q99819; -.
DR OpenTargets; ENSG00000242173; -.
DR PharmGKB; PA24965; -.
DR VEuPathDB; HostDB:ENSG00000242173; -.
DR eggNOG; KOG3205; Eukaryota.
DR GeneTree; ENSGT00390000006233; -.
DR InParanoid; Q99819; -.
DR OMA; EWGLCIK; -.
DR OrthoDB; 1265661at2759; -.
DR PhylomeDB; Q99819; -.
DR TreeFam; TF105387; -.
DR PathwayCommons; Q99819; -.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q99819; -.
DR BioGRID-ORCS; 398; 13 hits in 1071 CRISPR screens.
DR ChiTaRS; ARHGDIG; human.
DR GeneWiki; ARHGDIG; -.
DR GenomeRNAi; 398; -.
DR Pharos; Q99819; Tbio.
DR PRO; PR:Q99819; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q99819; protein.
DR Bgee; ENSG00000242173; Expressed in right hemisphere of cerebellum and 115 other tissues.
DR ExpressionAtlas; Q99819; baseline and differential.
DR Genevisible; Q99819; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
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 Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..225
FT /note="Rho GDP-dissociation inhibitor 3"
FT /id="PRO_0000219018"
FT CONFLICT 114
FT /note="D -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 25098 MW; AFC4576E6BE0E9BD CRC64;
MLGLDACELG AQLLELLRLA LCARVLLADK EGGPPAVDEV LDEAVPEYRA PGRKSLLEIR
QLDPDDRSLA KYKRVLLGPL PPAVDPSLPN VQVTRLTLLS EQAPGPVVMD LTGDLAVLKD
QVFVLKEGVD YRVKISFKVH REIVSGLKCL HHTYRRGLRV DKTVYMVGSY GPSAQEYEFV
TPVEEAPRGA LVRGPYLVVS LFTDDDRTHH LSWEWGLCIC QDWKD
