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RB39B_BOVIN
ID   RB39B_BOVIN             Reviewed;         213 AA.
AC   Q17QU4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ras-related protein Rab-39B;
GN   Name=RAB39B;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Small GTPases Rab involved in autophagy. The small GTPases
CC       Rab are key regulators of intracellular membrane trafficking, from the
CC       formation of transport vesicles to their fusion with membranes. Rabs
CC       cycle between an inactive GDP-bound form and an active GTP-bound form
CC       that is able to recruit to membranes different sets of downstream
CC       effectors directly responsible for vesicle formation, movement,
CC       tethering and fusion (By similarity). May regulate the homeostasis of
CC       SNCA/alpha-synuclein. Together with PICK1 proposed to ensure
CC       selectively GRIA2 exit from the endoplasmic reticulum to the Golgi and
CC       to regulate AMPAR compostion at the post-synapses and thus synaptic
CC       transmission (By similarity). {ECO:0000250|UniProtKB:Q8BHC1,
CC       ECO:0000250|UniProtKB:Q96DA2}.
CC   -!- SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ domain); a
CC       PICK1 homodimer may allow simultaneous association of RAB39B and GRIA2
CC       to PICK1 which is involved in GRIA2 trafficking (By similarity).
CC       Interacts with isoform c of RASSF1; the interaction is strong (By
CC       similarity). Interacts with isoform a of RASSF1; the interaction is
CC       weak (By similarity). Interacts with the DLG4/PSD-95 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8BHC1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96DA2};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q96DA2}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q96DA2}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q96DA2}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q96DA2}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q96DA2}. Note=Partial colocalization with
CC       markers that cycle from the cell surface to the trans-Golgi network.
CC       {ECO:0000250|UniProtKB:Q8BHC1}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; BC118177; AAI18178.1; -; mRNA.
DR   RefSeq; NP_001069563.1; NM_001076095.1.
DR   AlphaFoldDB; Q17QU4; -.
DR   SMR; Q17QU4; -.
DR   STRING; 9913.ENSBTAP00000026354; -.
DR   PaxDb; Q17QU4; -.
DR   PRIDE; Q17QU4; -.
DR   Ensembl; ENSBTAT00000026354; ENSBTAP00000026354; ENSBTAG00000019779.
DR   GeneID; 537560; -.
DR   KEGG; bta:537560; -.
DR   CTD; 116442; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019779; -.
DR   VGNC; VGNC:33648; RAB39B.
DR   eggNOG; KOG0091; Eukaryota.
DR   GeneTree; ENSGT00940000158132; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; Q17QU4; -.
DR   OMA; XSITRAY; -.
DR   OrthoDB; 1416096at2759; -.
DR   TreeFam; TF300032; -.
DR   Reactome; R-BTA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000019779; Expressed in occipital lobe and 61 other tissues.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0031489; F:myosin V binding; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR   CDD; cd04111; Rab39; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041818; Rab39.
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   Autophagy; Cell membrane; Cytoplasmic vesicle; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..213
FT                   /note="Ras-related protein Rab-39B"
FT                   /id="PRO_0000262917"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHC1"
FT   MOD_RES         213
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           211
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  24608 MW;  2B2C5A9EDCAFA88E CRC64;
     MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL
     QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL
     VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGDI
     TIQEGWEGVK SGFVPNVVHS SEEVVKSERR CLC
 
 
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