GDIB_BOVIN
ID GDIB_BOVIN Reviewed; 445 AA.
AC P50397; A5D985; Q3MHL1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Rab GDP dissociation inhibitor beta;
DE Short=Rab GDI beta;
DE AltName: Full=Guanosine diphosphate dissociation inhibitor 2;
DE Short=GDI-2;
GN Name=GDI2; Synonyms=RABGDIB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GDP-dissociation inhibitor preventing the GDP to GTP exchange
CC of most Rab proteins. By keeping these small GTPases in their inactive
CC GDP-bound form regulates intracellular membrane trafficking. Negatively
CC regulates protein transport to the cilium and ciliogenesis through the
CC inhibition of RAB8A. {ECO:0000250|UniProtKB:P50395}.
CC -!- SUBUNIT: Interacts with RHOH. Interacts with the GDP-bound forms of
CC RAB3A, RAB3B, RAB3C, RAB5A, RAB5B, RAB5C, RAB8B, RAB10, RAB12, RAB35,
CC and RAB43; binds RAB3D to a lesser extent. Interacts with RAB8A (GDP-
CC bound inactive form); prevents RAB8A activation. Interacts with DZIP1;
CC negatively regulates the interaction of GDI2 with GDP-bound RAB8A.
CC {ECO:0000250|UniProtKB:P50395}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from mouse.
CC {ECO:0000305|PubMed:7513052}.
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DR EMBL; U07951; AAB16908.1; -; mRNA.
DR EMBL; BT030504; ABQ12944.1; -; mRNA.
DR EMBL; BC105197; AAI05198.1; -; mRNA.
DR PIR; A56024; A56024.
DR RefSeq; NP_001028934.1; NM_001033762.2.
DR AlphaFoldDB; P50397; -.
DR SMR; P50397; -.
DR STRING; 9913.ENSBTAP00000006992; -.
DR PaxDb; P50397; -.
DR PeptideAtlas; P50397; -.
DR PRIDE; P50397; -.
DR GeneID; 509832; -.
DR KEGG; bta:509832; -.
DR CTD; 2665; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; P50397; -.
DR OrthoDB; 763627at2759; -.
DR TreeFam; TF300449; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:1903565; P:negative regulation of protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..445
FT /note="Rab GDP dissociation inhibitor beta"
FT /id="PRO_0000056677"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P50395"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61598"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50395"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50399"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50395"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50395"
SQ SEQUENCE 445 AA; 50488 MW; CEEA4DE3CC17D5F7 CRC64;
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRFKIPG
APPASMGRGR DWNVDLIPKF LMANGQLVKM LLFTEVTRYL DFKVTEGSFV YKGGKIYKVP
STEAEALASS LMGLFEKRRF RKFLVYVANF DENDPRTFEG IDPKKTSMRE VYKKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCCETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPIEEIIM QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISSA HNVAAQGKYI AIASTTVETK
EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESQIFI SRTYDATTHF ETTCDDIKDI
YKRMMGSEFD FEEMKRKKND IYGEE
