ID A0A3L8S105_CHLGU Unreviewed; 319 AA.
AC A0A3L8S105;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000256|ARBA:ARBA00040620};
DE AltName: Full=Rho-GDI alpha {ECO:0000256|ARBA:ARBA00041559};
GN ORFNames=DV515_00013914 {ECO:0000313|EMBL:RLV92097.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV92097.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV92097.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV92097.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV92097.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV92097.1}.
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DR EMBL; QUSF01000104; RLV92097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8S105; -.
DR STRING; 44316.ENSEGOP00005015956; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd12680; RRM_THOC4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.70.50.30; Coagulation Factor XIII, subunit A, domain 1; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR InterPro; IPR000504; RRM_dom.
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 Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00492; RHOGDI.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 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:UP000276834};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 42..116
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 35740 MW; 5779C3AE1DBEF1C4 CRC64;
MARGGGRNRP APYSRPKQLP EKWQHDLFDS GFGTGAGVET GGKLLVSNLD FGVSDADIQE
LFAEFGTLKK AAVHYDRSGR SLGTADVHFE RKADALKAMK QYNGVPLDVW VTCARMAEQE
PTAEQLAQIA AENEEDEHSV NYKPPAQKSI QEIQELDKDD ESLRKYKEAL LGAVTVTADP
NAPNVVVTKL TLVCATAPGP LELDLTGDLD SYKKQAFVLK EGVEYRIKIS FRVNREIVSG
LKYIQHTFRK GVKIDKTEYM VGSYGPRAEE YEFLTPMEEA PKGMLARGSY NIKSKFTDDD
KTDHLSWEWN LTIKKDWKD
//
