RB27B_MOUSE
ID RB27B_MOUSE Reviewed; 218 AA.
AC Q99P58; Q8CIX0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ras-related protein Rab-27B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:O00194};
GN Name=Rab27b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11178108; DOI=10.1186/1471-2156-2-2;
RA Ramalho J.S., Tolmachova T., Hume A.N., McGuigan A., Gregory-Evans C.Y.,
RA Huxley C., Seabra M.C.;
RT "Chromosomal mapping, gene structure and characterization of the human and
RT murine RAB27B gene.";
RL BMC Genet. 2:2-2(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CH3/HeSn;
RA Chen Y., Deng F.-M., Sun T.-T., Kreibich G.;
RT "Mouse Rab27b.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH SYTL4.
RX PubMed=11956164; DOI=10.1210/endo.143.5.8823;
RA Zhao S., Torii S., Yokota-Hashimoto H., Takeuchi T., Izumi T.;
RT "Involvement of Rab27b in the regulated secretion of pituitary hormones.";
RL Endocrinology 143:1817-1824(2002).
RN [5]
RP INTERACTION WITH MYRIP.
RX PubMed=12221080; DOI=10.1074/jbc.m203862200;
RA Fukuda M., Kuroda T.S.;
RT "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a
RT novel linker protein that interacts with Rab27, myosin Va/VIIa, and
RT actin.";
RL J. Biol. Chem. 277:43096-43103(2002).
RN [6]
RP INTERACTION WITH RPH3A AND RPH3AL.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH SYTL2.
RX PubMed=16716193; DOI=10.1111/j.1365-2443.2006.00964.x;
RA Saegusa C., Tanaka T., Tani S., Itohara S., Mikoshiba K., Fukuda M.;
RT "Decreased basal mucus secretion by Slp2-a-deficient gastric surface mucous
RT cells.";
RL Genes Cells 11:623-631(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-201 IN COMPLEX WITH GTP AND
RP MLPH, DISULFIDE BOND, AND MUTAGENESIS OF TYR-6; GLN-78 AND ASP-91.
RX PubMed=18940604; DOI=10.1016/j.str.2008.07.014;
RA Kukimoto-Niino M., Sakamoto A., Kanno E., Hanawa-Suetsugu K., Terada T.,
RA Shirouzu M., Fukuda M., Yokoyama S.;
RT "Structural basis for the exclusive specificity of Slac2-a/melanophilin for
RT the Rab27 GTPases.";
RL Structure 16:1478-1490(2008).
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 (By similarity). {ECO:0000250|UniProtKB:O00194,
CC ECO:0000250|UniProtKB:Q8HZJ5}.
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. Interacts (GDP-bound form preferentially) with DENND10
CC (By similarity). {ECO:0000250|UniProtKB:O00194,
CC ECO:0000269|PubMed:11956164, ECO:0000269|PubMed:12221080,
CC ECO:0000269|PubMed:12578829, ECO:0000269|PubMed:16716193,
CC ECO:0000269|PubMed:18940604}.
CC -!- INTERACTION:
CC Q99P58; Q91V27: Mlph; NbExp=2; IntAct=EBI-11565917, EBI-398308;
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 abundantly in the stomach and is
CC predominantly localized at the apical region of gastric-surface mucus
CC cells. Also expressed in the brain and spleen.
CC {ECO:0000269|PubMed:16716193}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AF328893; AAK11242.1; -; mRNA.
DR EMBL; AY010898; AAG45502.1; -; mRNA.
DR EMBL; BC032928; AAH32928.1; -; mRNA.
DR CCDS; CCDS29331.1; -.
DR RefSeq; NP_001076022.1; NM_001082553.2.
DR RefSeq; NP_001289727.1; NM_001302798.1.
DR RefSeq; NP_085031.3; NM_030554.4.
DR PDB; 2IEY; X-ray; 3.18 A; A/B=1-193.
DR PDB; 2IEZ; X-ray; 2.80 A; A/B/H/I=1-218.
DR PDB; 2IF0; X-ray; 2.80 A; A/B=1-198.
DR PDB; 2ZET; X-ray; 3.00 A; A/B=1-201.
DR PDBsum; 2IEY; -.
DR PDBsum; 2IEZ; -.
DR PDBsum; 2IF0; -.
DR PDBsum; 2ZET; -.
DR AlphaFoldDB; Q99P58; -.
DR SMR; Q99P58; -.
DR BioGRID; 219798; 2.
DR DIP; DIP-46237N; -.
DR IntAct; Q99P58; 8.
DR STRING; 10090.ENSMUSP00000114094; -.
DR PhosphoSitePlus; Q99P58; -.
DR EPD; Q99P58; -.
DR jPOST; Q99P58; -.
DR MaxQB; Q99P58; -.
DR PaxDb; Q99P58; -.
DR PRIDE; Q99P58; -.
DR ProteomicsDB; 300310; -.
DR Antibodypedia; 4487; 286 antibodies from 32 providers.
DR DNASU; 80718; -.
DR Ensembl; ENSMUST00000069749; ENSMUSP00000068349; ENSMUSG00000024511.
DR Ensembl; ENSMUST00000117692; ENSMUSP00000112807; ENSMUSG00000024511.
DR Ensembl; ENSMUST00000121693; ENSMUSP00000114094; ENSMUSG00000024511.
DR GeneID; 80718; -.
DR KEGG; mmu:80718; -.
DR UCSC; uc008fnz.2; mouse.
DR CTD; 5874; -.
DR MGI; MGI:1931295; Rab27b.
DR VEuPathDB; HostDB:ENSMUSG00000024511; -.
DR eggNOG; KOG0081; Eukaryota.
DR GeneTree; ENSGT00940000157449; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q99P58; -.
DR OMA; IGWMRDI; -.
DR OrthoDB; 1190514at2759; -.
DR PhylomeDB; Q99P58; -.
DR TreeFam; TF312895; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 80718; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rab27b; mouse.
DR EvolutionaryTrace; Q99P58; -.
DR PRO; PR:Q99P58; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q99P58; protein.
DR Bgee; ENSMUSG00000024511; Expressed in urinary bladder urothelium and 211 other tissues.
DR ExpressionAtlas; Q99P58; baseline and differential.
DR Genevisible; Q99P58; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0005795; C:Golgi stack; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISO:MGI.
DR GO; GO:0032585; C:multivesicular body membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; ISO:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:MGI.
DR GO; GO:0042589; C:zymogen granule membrane; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disulfide bond; Endosome; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW 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_0000121225"
FT REGION 194..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:0000269|PubMed:18940604"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18940604"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18940604"
FT BINDING 163..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18940604"
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:0000269|PubMed:18940604"
FT MUTAGEN 6
FT /note="Y->F: Abolishes the interaction with MLPH."
FT /evidence="ECO:0000269|PubMed:18940604"
FT MUTAGEN 78
FT /note="Q->L: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:18940604"
FT MUTAGEN 91
FT /note="D->G: Strongly reduces the interaction with MLPH."
FT /evidence="ECO:0000269|PubMed:18940604"
FT CONFLICT 57
FT /note="G -> R (in Ref. 2; AAG45502)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="G -> E (in Ref. 2; AAG45502)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="D -> V (in Ref. 2; AAG45502)"
FT /evidence="ECO:0000305"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:2IEZ"
FT STRAND 37..53
FT /evidence="ECO:0007829|PDB:2IEZ"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:2IEZ"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2IEZ"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2IEZ"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:2IEZ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2IEZ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2IEZ"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2IEZ"
FT HELIX 170..187
FT /evidence="ECO:0007829|PDB:2IEZ"
SQ SEQUENCE 218 AA; 24560 MW; 01DBC47275B4B955 CRC64;
MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR VVYDTQGADG
ASGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD LTSQQSFLNV RNWMSQLQAN
AYCENPDIVL IGNKADLPDQ REVNERQARE LAEKYGIPYF ETSAATGQNV EKSVETLLDL
IMKRMEKCVE KTQVPDTVNG GNSGKLDGEK PAEKKCAC
