RB27A_PIG
ID RB27A_PIG Reviewed; 221 AA.
AC Q4LE85;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=16441305; DOI=10.1111/j.1365-2052.2005.01404.x;
RA Okumura N., Hayashi T., Sekikawa H., Matsumoto T., Mikawa A., Hamasima N.,
RA Awata T.;
RT "Sequencing, mapping and nucleotide variation of porcine coat color genes
RT EDNRB, MYO5A, KITLG, SLC45A2, RAB27A, SILV and MITF.";
RL Anim. Genet. 37:80-82(2006).
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; AB209958; BAE03308.1; -; mRNA.
DR RefSeq; NP_001027528.1; NM_001032357.1.
DR RefSeq; XP_005659637.1; XM_005659580.2.
DR RefSeq; XP_005659638.1; XM_005659581.2.
DR RefSeq; XP_005659639.1; XM_005659582.2.
DR RefSeq; XP_005659640.1; XM_005659583.2.
DR RefSeq; XP_005659641.1; XM_005659584.2.
DR RefSeq; XP_005659642.1; XM_005659585.2.
DR RefSeq; XP_013848417.1; XM_013992963.1.
DR RefSeq; XP_013848418.1; XM_013992964.1.
DR RefSeq; XP_013848419.1; XM_013992965.1.
DR RefSeq; XP_013848420.1; XM_013992966.1.
DR RefSeq; XP_013848422.1; XM_013992968.1.
DR AlphaFoldDB; Q4LE85; -.
DR SMR; Q4LE85; -.
DR STRING; 9823.ENSSSCP00000004969; -.
DR PaxDb; Q4LE85; -.
DR PeptideAtlas; Q4LE85; -.
DR PRIDE; Q4LE85; -.
DR Ensembl; ENSSSCT00000038357; ENSSSCP00000041641; ENSSSCG00000004612.
DR Ensembl; ENSSSCT00005058281; ENSSSCP00005035972; ENSSSCG00005036452.
DR Ensembl; ENSSSCT00015073554; ENSSSCP00015029547; ENSSSCG00015055155.
DR Ensembl; ENSSSCT00025039592; ENSSSCP00025016776; ENSSSCG00025029044.
DR Ensembl; ENSSSCT00030030675; ENSSSCP00030013758; ENSSSCG00030022112.
DR Ensembl; ENSSSCT00035088356; ENSSSCP00035036921; ENSSSCG00035065558.
DR Ensembl; ENSSSCT00040081693; ENSSSCP00040035522; ENSSSCG00040060006.
DR Ensembl; ENSSSCT00045060087; ENSSSCP00045042191; ENSSSCG00045034965.
DR Ensembl; ENSSSCT00050004561; ENSSSCP00050001816; ENSSSCG00050003397.
DR Ensembl; ENSSSCT00055005327; ENSSSCP00055004133; ENSSSCG00055002777.
DR Ensembl; ENSSSCT00060041337; ENSSSCP00060017516; ENSSSCG00060030599.
DR Ensembl; ENSSSCT00065064555; ENSSSCP00065027969; ENSSSCG00065047198.
DR Ensembl; ENSSSCT00070016409; ENSSSCP00070013583; ENSSSCG00070008420.
DR Ensembl; ENSSSCT00070016417; ENSSSCP00070013591; ENSSSCG00070008420.
DR Ensembl; ENSSSCT00070016422; ENSSSCP00070013596; ENSSSCG00070008420.
DR Ensembl; ENSSSCT00070016430; ENSSSCP00070013604; ENSSSCG00070008420.
DR Ensembl; ENSSSCT00070016445; ENSSSCP00070013617; ENSSSCG00070008420.
DR Ensembl; ENSSSCT00070016453; ENSSSCP00070013625; ENSSSCG00070008420.
DR GeneID; 606749; -.
DR KEGG; ssc:606749; -.
DR CTD; 5873; -.
DR VGNC; VGNC:98249; RAB27A.
DR eggNOG; KOG0081; Eukaryota.
DR GeneTree; ENSGT00940000156218; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; Q4LE85; -.
DR OMA; CTGANIQ; -.
DR OrthoDB; 1190514at2759; -.
DR TreeFam; TF312895; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004612; Expressed in pituitary gland and 41 other tissues.
DR ExpressionAtlas; Q4LE85; baseline and differential.
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_0000236243"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 24889 MW; 7A958EE0014657FC CRC64;
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRANGPDG
AIGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH
AYCENPDIVL CGNKSDLEDQ RVVKEEEARG LAEKYGIPYF ETSAANGTNV SLAIETLLDL
IMKRMERCVD KSWIPEGVVR SNGHTSADPL NEEKEKGSCG C
