ID   F7BAR0_CALJA            Unreviewed;       441 AA.
AC   F7BAR0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   Name=GDI1 {ECO:0000313|Ensembl:ENSCJAP00000042204.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000042204.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000042204.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000042204.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most RAB proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP. {ECO:0000256|RuleBase:RU363124}.
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP to them. Promotes the dissociation of GDP-bound Rab
CC       proteins from the membrane and inhibits their activation. Promotes the
CC       dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes.
CC       {ECO:0000256|ARBA:ARBA00037119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU363124}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000256|ARBA:ARBA00004601}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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DR   AlphaFoldDB; F7BAR0; -.
DR   STRING; 9483.ENSCJAP00000042204; -.
DR   Ensembl; ENSCJAT00000056075.4; ENSCJAP00000042204.4; ENSCJAG00000016910.5.
DR   GeneTree; ENSGT00950000182994; -.
DR   HOGENOM; CLU_021695_0_0_1; -.
DR   InParanoid; F7BAR0; -.
DR   Proteomes; UP000008225; Chromosome X.
DR   Bgee; ENSCJAG00000016910; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787:SF3; RAB GDP DISSOCIATION INHIBITOR ALPHA; 1.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU363124};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   GTPase activation {ECO:0000256|RuleBase:RU363124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
SQ   SEQUENCE   441 AA;  50180 MW;  C62F619130CF4C4A CRC64;
     MVLPSLQECI LSGIMSVNGK KVLHMDRNPY YGGESSSITP LEELYKRFQL LEGPPESMGR
     GRDWNVDLIP KFLMANGQLV KMLLYTEVTR YLDFKVVEGS FVYKGGKIYK VPSTETEALA
     SNLMGMFEKR RFRKFLVFVA NFDENDPKTF EGVDPQTTSM RDVYRKFDLG QDVIDFTGHA
     LALYRTDDYL DQPCLETINR IKLYSESLAR YGKSPYLYPL YGLGELPQGF ARLSAIYGGT
     YMLNKPVDDI IMENGKVVGV KSEGEVARCK QLICDPSYIP DRVRKAGQVI RIICILSHPI
     KNTNDANSCQ IIIPQNQVNR KSELFLWPDI YVCMISYAHN VAAQGKYIAI ASTTVETMDP
     EKEVEPALEL LEPIDQKFVA ISDFLSQPWL LVFCSCSYDA TTHFETTCND IKDIYKRMAG
     TAFDFENMKR KQNDVFGEAE Q
//