ID   GDIA_RAT                Reviewed;         447 AA.
AC   P50398; Q499U0; Q9R274;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Rab GDP dissociation inhibitor alpha;
DE            Short=Rab GDI alpha;
DE   AltName: Full=Guanosine diphosphate dissociation inhibitor 1;
DE            Short=GDI-1;
GN   Name=Gdi1; Synonyms=Rabgdia;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8188702; DOI=10.1016/s0021-9258(17)36773-x;
RA   Nishimura N., Nakamura H., Takai Y., Sano K.;
RT   "Molecular cloning and characterization of two rab GDI species from rat
RT   brain: brain-specific and ubiquitous types.";
RL   J. Biol. Chem. 269:14191-14198(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=7513052; DOI=10.1128/mcb.14.5.3459-3468.1994;
RA   Shisheva A., Suedhof T.C., Czech M.P.;
RT   "Cloning, characterization, and expression of a novel GDP dissociation
RT   inhibitor isoform from skeletal muscle.";
RL   Mol. Cell. Biol. 14:3459-3468(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 81-439.
RC   TISSUE=Pancreas;
RX   PubMed=10996854;
RX   DOI=10.1002/1097-4644(20001215)79:4<628::aid-jcb120>3.0.co;2-t;
RA   Caillol N., Pasqualini E., Lloubes R., Lombardo D.;
RT   "Impairment of bile salt-dependent lipase secretion in human pancreatic
RT   tumoral SOJ-6 cells.";
RL   J. Cell. Biochem. 79:628-647(2000).
RN   [5]
RP   PROTEIN SEQUENCE OF 80-98; 104-112; 143-156; 194-208; 211-218; 222-240 AND
RP   279-290, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL   Submitted (JUL-2007) 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 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:0000269|PubMed:7513052, ECO:0000269|PubMed:8188702}.
CC   -!- SUBUNIT: Interacts with RHOH (By similarity). Interacts with the non-
CC       phosphorylated forms of RAB1A, RAB3A, RAB5A, RAB5B, RAB5C, RAB8A,
CC       RAB8B, RAB10, RAB12, RAB35, and RAB43 (By similarity).
CC       {ECO:0000250|UniProtKB:P31150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: High expression in brain, lower in other tissues.
CC       {ECO:0000269|PubMed:8188702}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR   EMBL; X74402; CAA52413.1; -; mRNA.
DR   EMBL; U07952; AAB16909.1; -; mRNA.
DR   EMBL; BC099763; AAH99763.1; -; mRNA.
DR   EMBL; AF130987; AAD25536.1; -; mRNA.
DR   PIR; A54091; A54091.
DR   PIR; B56024; B56024.
DR   RefSeq; NP_058784.2; NM_017088.2.
DR   AlphaFoldDB; P50398; -.
DR   SMR; P50398; -.
DR   BioGRID; 247236; 2.
DR   CORUM; P50398; -.
DR   IntAct; P50398; 2.
DR   MINT; P50398; -.
DR   STRING; 10116.ENSRNOP00000053135; -.
DR   iPTMnet; P50398; -.
DR   PhosphoSitePlus; P50398; -.
DR   SwissPalm; P50398; -.
DR   World-2DPAGE; 0004:P50398; -.
DR   jPOST; P50398; -.
DR   PaxDb; P50398; -.
DR   PRIDE; P50398; -.
DR   Ensembl; ENSRNOT00000089814; ENSRNOP00000070171; ENSRNOG00000056870.
DR   GeneID; 25183; -.
DR   KEGG; rno:25183; -.
DR   CTD; 2664; -.
DR   RGD; 2676; Gdi1.
DR   eggNOG; KOG1439; Eukaryota.
DR   GeneTree; ENSGT00950000182994; -.
DR   HOGENOM; CLU_021695_0_0_1; -.
DR   InParanoid; P50398; -.
DR   OMA; DHYGGES; -.
DR   OrthoDB; 763627at2759; -.
DR   PhylomeDB; P50398; -.
DR   TreeFam; TF300449; -.
DR   Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:P50398; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000056870; Expressed in cerebellum and 20 other tissues.
DR   Genevisible; P50398; RN.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISO:RGD.
DR   GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA:RGD.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IDA:UniProtKB.
DR   GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0032482; P:Rab protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787; PTHR11787; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Golgi apparatus; GTPase activation;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Rab GDP dissociation inhibitor alpha"
FT                   /id="PRO_0000056676"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50396"
FT   CONFLICT        199
FT                   /note="D -> Y (in Ref. 1; CAA52413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="G -> S (in Ref. 2; AAB16909)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="S -> P (in Ref. 2; AAB16909)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50537 MW;  58384671991DF793 CRC64;
     MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE
     GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
     STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQTTSMRD VYRKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETA
     EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI
     YKRMAGSAFD FENMKRKQND VFGEADQ