ID   RAB3B_MESAU             Reviewed;         219 AA.
AC   Q5KTJ7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Ras-related protein Rab-3B;
GN   Name=RAB3B;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shinahara W., Nishimura N., Yamaguchi Y., Manabe S., Sasaki T.;
RT   "Hamster Rab3B.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RIMS1, RIMS2, RPH3A and RPH3AL. The GTP-bound
CC       form interacts with GAS8/DRC4 (via coiled-coil domains) (By
CC       similarity). Interacts with GDI2, CHM and CHML; phosphorylation at Thr-
CC       86 disrupts these interactions (By similarity). Interacts with MADD
CC       (via uDENN domain); the GTP-bound form is preferred for interaction (By
CC       similarity). {ECO:0000250|UniProtKB:P20337,
CC       ECO:0000250|UniProtKB:Q9CZT8}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9CZT8}. Note=Colocalizes with GAS8/DRC4 in the
CC       Golgi apparatus. {ECO:0000250|UniProtKB:Q9CZT8}.
CC   -!- PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including CHM,
CC       CHML and RAB GDP dissociation inhibitor GDI2.
CC       {ECO:0000250|UniProtKB:P20337}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AB158368; BAD83699.1; -; mRNA.
DR   AlphaFoldDB; Q5KTJ7; -.
DR   SMR; Q5KTJ7; -.
DR   STRING; 10036.XP_005072184.1; -.
DR   eggNOG; KOG0093; Eukaryota.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProt.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd01865; Rab3; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037872; Rab3.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   CHAIN           2..219
FT                   /note="Ras-related protein Rab-3B"
FT                   /id="PRO_0000270790"
FT   MOTIF           51..59
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   BINDING         48..54
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P63012"
FT   BINDING         77..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   BINDING         165..167
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95716"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P20337"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63941"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20337"
FT   MOD_RES         219
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           217
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           219
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  24725 MW;  102F615541A7670E CRC64;
     MASVTDGKTG VKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK
     VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI
     KTYSWDNAQV ILVGNKCDME EERVVPTEKG RLLAEQLGFD FFEASAKENI SVRQAFERLV
     DAICDKMSDS LDTDPSVLGA SKTTRLSDTP PLLQQNCSC