ID A0A2R9BA66_PANPA Unreviewed; 204 AA.
AC A0A2R9BA66;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000256|ARBA:ARBA00040620};
DE AltName: Full=Rho-GDI alpha {ECO:0000256|ARBA:ARBA00041559};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000025165.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000025165.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000025165.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP
CC exchange reaction of the Rho proteins by inhibiting the dissociation of
CC GDP from them, and the subsequent binding of GTP to them. Retains Rho
CC proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool,
CC regulating their stability and protecting them from degradation.
CC Actively involved in the recycling and distribution of activated Rho
CC GTPases in the cell, mediates extraction from membranes of both
CC inactive and activated molecules due its exceptionally high affinity
CC for prenylated forms. Through the modulation of Rho proteins, may play
CC a role in cell motility regulation. In glioma cells, inhibits cell
CC migration and invasion by mediating the signals of SEMA5A and PLXNB3
CC that lead to inactivation of RAC1. {ECO:0000256|ARBA:ARBA00037489}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Rho GDI family.
CC {ECO:0000256|ARBA:ARBA00009758}.
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DR EMBL; AJFE02109977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003831157.1; XM_003831109.1.
DR AlphaFoldDB; A0A2R9BA66; -.
DR SMR; A0A2R9BA66; -.
DR Ensembl; ENSPPAT00000047991.1; ENSPPAP00000025165.1; ENSPPAG00000035710.1.
DR GeneID; 100993463; -.
DR KEGG; pps:100993463; -.
DR CTD; 396; -.
DR GeneTree; ENSGT00390000006233; -.
DR OMA; YQQQTYR; -.
DR OrthoDB; 21211at2759; -.
DR Proteomes; UP000240080; Chromosome 17.
DR Bgee; ENSPPAG00000035710; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
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:SF9; RHO GDP-DISSOCIATION INHIBITOR 1; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080}.
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 23207 MW; 59CB6F42E3B3BCCA CRC64;
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA
VSADPNVPNV VVTGLTLVCS SAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PVEEAPKGML ARGSYSIKSR
FTDDDKTDHL SWEWNLTIKK DWKD
//
