RB27A_CANLF
ID RB27A_CANLF Reviewed; 221 AA.
AC Q1HE58;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ras-related protein Rab-27A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P51159};
GN Name=RAB27A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large Munsterlander; TISSUE=Skin;
RA Schmutz S.M., Berryere T.G., Philipp U., Dreger D., Leeb T.;
RT "Association of an MLPH allele with dilute coat colors in domestic dogs.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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. Plays a role
CC in cytotoxic granule exocytosis in lymphocytes. Required for both
CC granule maturation and granule docking and priming at the immunologic
CC synapse. {ECO:0000250|UniProtKB:P51159}.
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:P51159};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P51159};
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:P51159}.
CC -!- SUBUNIT: Binds SYTL1, SLAC2B, MYRIP, SYTL3, SYTL4 and SYTL5. Interacts
CC with RPH3A and RPH3A (By similarity). Binds MLPH and SYTL2. Interacts
CC with UNC13D. Does not interact with the BLOC-3 complex (heterodimer of
CC HPS1 and HPS4) (By similarity). Interacts (GDP-bound form
CC preferentially) with DENND10 (By similarity).
CC {ECO:0000250|UniProtKB:P51159, ECO:0000250|UniProtKB:Q9ERI2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P51159}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P51159}. Melanosome
CC {ECO:0000250|UniProtKB:P51159}. Late endosome
CC {ECO:0000250|UniProtKB:P51159}. Lysosome
CC {ECO:0000250|UniProtKB:P51159}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV. Localizes to endosomal
CC exocytic vesicles. {ECO:0000250|UniProtKB:P51159}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; DQ494380; ABF50191.1; -; mRNA.
DR RefSeq; NP_001041595.1; NM_001048130.1.
DR RefSeq; XP_005638237.1; XM_005638180.2.
DR RefSeq; XP_005638238.1; XM_005638181.2.
DR AlphaFoldDB; Q1HE58; -.
DR SMR; Q1HE58; -.
DR STRING; 9615.ENSCAFP00000023411; -.
DR PaxDb; Q1HE58; -.
DR Ensembl; ENSCAFT00030029077; ENSCAFP00030025349; ENSCAFG00030015797.
DR Ensembl; ENSCAFT00040047724; ENSCAFP00040041663; ENSCAFG00040025570.
DR Ensembl; ENSCAFT00845050349; ENSCAFP00845039475; ENSCAFG00845028531.
DR GeneID; 608699; -.
DR KEGG; cfa:608699; -.
DR CTD; 5873; -.
DR VEuPathDB; HostDB:ENSCAFG00845028531; -.
DR eggNOG; KOG0081; Eukaryota.
DR GeneTree; ENSGT00940000156218; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q1HE58; -.
DR OMA; CTGANIQ; -.
DR OrthoDB; 1190514at2759; -.
DR TreeFam; TF312895; -.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000002254; Chromosome 30.
DR Bgee; ENSCAFG00000015916; Expressed in granulocyte and 46 other tissues.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
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:0019882; P:antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; IEA:Ensembl.
DR GO; GO:0043316; P:cytotoxic T cell degranulation; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; IEA:Ensembl.
DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR GO; GO:0036257; P:multivesicular body organization; IEA:Ensembl.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0043320; P:natural killer cell degranulation; IEA:Ensembl.
DR GO; GO:1903435; P:positive regulation of constitutive secretory pathway; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:1903307; P:positive regulation of regulated secretory pathway; IEA:Ensembl.
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; Exocytosis; GTP-binding; Hydrolase;
KW Lipoprotein; Lysosome; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT CHAIN 2..221
FT /note="Ras-related protein Rab-27A"
FT /id="PRO_0000252359"
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-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51159"
FT MOD_RES 221
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 221
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 123..188
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24972 MW; F765097DC87C6D54 CRC64;
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRANGPDG
AIGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH
AYCENPDIVL CGNKSDLEDQ RVVKEEDARG LAEKYGIPYF ETSAANGTNI SQAIEMLLDL
IMKRMERCVD KSWIPEGVVR SNGHTSTDHL NEAKEKGICG C
