RB27B_BOVIN
ID RB27B_BOVIN Reviewed; 218 AA.
AC Q8HZJ5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ras-related protein Rab-27B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:O00194};
GN Name=RAB27B;
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], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14625374; DOI=10.1073/pnas.2436350100;
RA Chen Y., Guo X., Deng F.M., Liang F.X., Sun W., Ren M., Izumi T.,
RA Sabatini D.D., Sun T.T., Kreibich G.;
RT "Rab27b is associated with fusiform vesicles and may be involved in
RT targeting uroplakins to urothelial apical membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14012-14017(2003).
CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC inactive GDP-bound states. In its active state, binds to a variety of
CC effector proteins to regulate homeostasis of late endocytic pathway,
CC including endosomal positioning, maturation and secretion (By
CC similarity). Plays a role in NTRK2/TRKB axonal anterograde transport by
CC facilitating the association of NTRK2/TRKB with KLC1 (By similarity).
CC May be involved in targeting uroplakins to urothelial apical membranes
CC (PubMed:14625374). {ECO:0000250|UniProtKB:O00194,
CC ECO:0000250|UniProtKB:Q99P74, ECO:0000269|PubMed:14625374}.
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:O00194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:O00194};
CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase
CC activating proteins (GAPs) which increase the GTP hydrolysis activity,
CC and GDP dissociation inhibitors which inhibit the dissociation of the
CC nucleotide from the GTPase. Activated by GEFs such as DENND10.
CC {ECO:0000250|UniProtKB:O00194}.
CC -!- SUBUNIT: Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with
CC RPH3A and RPH3A (By similarity). Interacts (GDP-bound form
CC preferentially) with DENND10 (By similarity).
CC {ECO:0000250|UniProtKB:O00194, ECO:0000250|UniProtKB:Q99P58}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O00194}; Lipid-
CC anchor {ECO:0000250|UniProtKB:O00194}. Late endosome
CC {ECO:0000250|UniProtKB:O00194}.
CC -!- TISSUE SPECIFICITY: Expressed at an extraordinary high level (0.1% of
CC total protein) in urothelium. {ECO:0000269|PubMed:14625374}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY010899; AAG45503.1; -; mRNA.
DR RefSeq; NP_777163.1; NM_174738.2.
DR AlphaFoldDB; Q8HZJ5; -.
DR SMR; Q8HZJ5; -.
DR STRING; 9913.ENSBTAP00000003613; -.
DR PaxDb; Q8HZJ5; -.
DR PRIDE; Q8HZJ5; -.
DR Ensembl; ENSBTAT00000003613; ENSBTAP00000003613; ENSBTAG00000002788.
DR Ensembl; ENSBTAT00000067536; ENSBTAP00000064075; ENSBTAG00000002788.
DR Ensembl; ENSBTAT00000074685; ENSBTAP00000062295; ENSBTAG00000002788.
DR Ensembl; ENSBTAT00000078091; ENSBTAP00000070586; ENSBTAG00000002788.
DR GeneID; 282858; -.
DR KEGG; bta:282858; -.
DR CTD; 5874; -.
DR VEuPathDB; HostDB:ENSBTAG00000002788; -.
DR VGNC; VGNC:33634; RAB27B.
DR eggNOG; KOG0081; Eukaryota.
DR GeneTree; ENSGT00940000157449; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q8HZJ5; -.
DR OMA; IGWMRDI; -.
DR OrthoDB; 1190514at2759; -.
DR TreeFam; TF312895; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000002788; Expressed in semen and 101 other tissues.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:Ensembl.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04127; Rab27A; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041837; Rab27a/b.
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; Disulfide bond; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00194"
FT CHAIN 2..218
FT /note="Ras-related protein Rab-27B"
FT /id="PRO_0000244430"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 16..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:O00194"
FT MOD_RES 218
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 123..188
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 24612 MW; 092FD9ADCE21FBA9 CRC64;
MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR VAYNTQGPNG
PTGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD LTSQQSFLNV RNWMSQLQAN
AYCENPDIVL IGNKADLPDQ REVNERQARD LAEKYSIPYF ETSAATGQNV EKAVETLLDL
IMKRMEQCVE KTHIPDTVNG SSSGKLDGEK SAEKKCAC
