RAB1B_BOVIN
ID RAB1B_BOVIN Reviewed; 201 AA.
AC Q2HJH2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ras-related protein Rab-1B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=RAB1B;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion (By similarity). Plays a role
CC in the initial events of the autophagic vacuole development which take
CC place at specialized regions of the endoplasmic reticulum (By
CC similarity). Regulates vesicular transport between the endoplasmic
CC reticulum and successive Golgi compartments. Required to modulate the
CC compacted morphology of the Golgi. Promotes the recruitment of lipid
CC phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate
CC compartment (By similarity). {ECO:0000250|UniProtKB:P10536,
CC ECO:0000250|UniProtKB:Q9H0U4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P62820};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62820};
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). {ECO:0000305}.
CC -!- SUBUNIT: Interacts with MICAL1 and MICAL2. Interacts (in GTP-bound
CC form) with MICALCL, MICAL1 and MILCAL3. Interacts with GDI1; the
CC interaction requires the GDP-bound state. Interacts with CHM/REP1; the
CC interaction requires the GDP-bound form and is necessary for
CC prenylation by GGTase II. Interacts with RabGAP TBC1D20. Interacts (in
CC GDP-bound form) with lipid phosphatase MTMR6 (via GRAM domain); the
CC interaction regulates MTMR6 recruitment to the endoplasmic reticulum-
CC Golgi intermediate compartment (By similarity). Interacts (in GDP-bound
CC form) with lipid phosphatase MTMR7 (By similarity).
CC {ECO:0000250|UniProtKB:Q9D1G1, ECO:0000250|UniProtKB:Q9H0U4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10536}.
CC Membrane {ECO:0000250|UniProtKB:P10536}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10536}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P10536}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10536}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P10536}. Note=Targeted by REP1 to membranes of
CC specific subcellular compartments including endoplasmic reticulum,
CC Golgi apparatus, and intermediate vesicles between these two
CC compartments. In the GDP-form, colocalizes with GDI in the cytoplasm
CC (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum-
CC Golgi intermediate compartment and to the peri-Golgi region (By
CC similarity). {ECO:0000250|UniProtKB:P10536,
CC ECO:0000250|UniProtKB:Q9H0U4}.
CC -!- PTM: Prenylated; by GGTase II, only after interaction of the substrate
CC with Rab escort protein 1 (REP1). {ECO:0000250|UniProtKB:Q9H0U4}.
CC -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic GTPase
CC activity. {ECO:0000250|UniProtKB:Q9H0U4}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC105393; AAI05394.1; -; mRNA.
DR RefSeq; NP_001069701.1; NM_001076233.1.
DR AlphaFoldDB; Q2HJH2; -.
DR SMR; Q2HJH2; -.
DR STRING; 9913.ENSBTAP00000054670; -.
DR PaxDb; Q2HJH2; -.
DR PeptideAtlas; Q2HJH2; -.
DR PRIDE; Q2HJH2; -.
DR GeneID; 540685; -.
DR KEGG; bta:540685; -.
DR CTD; 81876; -.
DR eggNOG; KOG0084; Eukaryota.
DR InParanoid; Q2HJH2; -.
DR OrthoDB; 1149105at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
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; Autophagy; Cytoplasm; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-1B"
FT /id="PRO_0000236247"
FT REGION 64..83
FT /note="Switch 2 region; Required for interaction with
FT REP1/CHM"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT REGION 173..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT MOD_RES 201
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
SQ SEQUENCE 201 AA; 22202 MW; 9812FF4DAC34B30E CRC64;
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ
IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGIPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG
GERPNLKIDS TPVKQAGGGC C
