RAB9A_CANLF
ID RAB9A_CANLF Reviewed; 201 AA.
AC P24408;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ras-related protein Rab-9A;
GN Name=RAB9A; Synonyms=RAB9;
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], AND FUNCTION.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8440258; DOI=10.1002/j.1460-2075.1993.tb05701.x;
RA Lombardi D., Soldati T., Riederer M.A., Goda Y., Zerial M., Pfeffer S.R.;
RT "Rab9 functions in transport between late endosomes and the trans Golgi
RT network.";
RL EMBO J. 12:677-682(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-201.
RC STRAIN=Cocker spaniel;
RX PubMed=2123294; DOI=10.1128/mcb.10.12.6578-6585.1990;
RA Chavrier P., Vingron M., Sander C., Simons K., Zerial M.;
RT "Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell
RT line.";
RL Mol. Cell. Biol. 10:6578-6585(1990).
RN [3]
RP INTERACTION WITH GCC2.
RX PubMed=16885419; DOI=10.1091/mbc.e06-02-0153;
RA Reddy J.V., Burguete A.S., Sridevi K., Ganley I.G., Nottingham R.M.,
RA Pfeffer S.R.;
RT "A functional role for the GCC185 golgin in mannose 6-phosphate receptor
RT recycling.";
RL Mol. Biol. Cell 17:4353-4363(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 1-174 IN COMPLEX WITH GDP ANALOG.
RX PubMed=15196914; DOI=10.1016/j.febslet.2004.05.004;
RA Wittmann J.G., Rudolph M.G.;
RT "Crystal structure of Rab9 complexed to GDP reveals a dimer with an active
RT conformation of switch II.";
RL FEBS Lett. 568:23-29(2004).
CC -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC and the trans-Golgi network (PubMed:8440258). Involved in the
CC recruitment of SGSM2 to melanosomes and is required for the proper
CC trafficking of melanogenic enzymes TYR, TYRP1 and DCT/TYRP2 to
CC melanosomes in melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q9R0M6, ECO:0000269|PubMed:8440258}.
CC -!- SUBUNIT: Interacts (preferentially in its GTP-bound form) with GCC2
CC (via its GRIP domain) (PubMed:16885419). Interacts (GTP-bound form)
CC with SGSM1; the GDP-bound form has much lower affinity for SGSM1.
CC Interacts with SGSM2. The GTP-bound form but not the GDP-bound form
CC interacts with HPS4 and the BLOC-3 complex (heterodimer of HPS1 and
CC HPS4) but does not interact with HPS1 alone (By similarity).
CC {ECO:0000250|UniProtKB:P51151, ECO:0000269|PubMed:16885419}.
CC -!- INTERACTION:
CC P24408; O94955: RHOBTB3; Xeno; NbExp=5; IntAct=EBI-1646050, EBI-2367123;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51151};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P51151}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P51151}. Late endosome
CC {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:P51151}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P51151}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9R0M6}. Melanosome
CC {ECO:0000250|UniProtKB:Q9R0M6}. Note=Colocalizes with OSBPL1A at the
CC late endosome. Recruited to phagosomes containing S.aureus or
CC M.tuberculosis. {ECO:0000250|UniProtKB:P51151}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X56386; CAA39797.1; -; mRNA.
DR PIR; S36187; S36187.
DR RefSeq; NP_001183960.1; NM_001197031.1.
DR RefSeq; XP_005641047.1; XM_005640990.2.
DR RefSeq; XP_013966791.1; XM_014111316.1.
DR PDB; 1S8F; X-ray; 1.77 A; A/B=1-174.
DR PDBsum; 1S8F; -.
DR AlphaFoldDB; P24408; -.
DR SMR; P24408; -.
DR IntAct; P24408; 2.
DR STRING; 9612.ENSCAFP00000017285; -.
DR PaxDb; P24408; -.
DR Ensembl; ENSCAFT00030017737; ENSCAFP00030015493; ENSCAFG00030009574.
DR Ensembl; ENSCAFT00040020233; ENSCAFP00040017553; ENSCAFG00040010945.
DR Ensembl; ENSCAFT00845050307; ENSCAFP00845039439; ENSCAFG00845028510.
DR GeneID; 403947; -.
DR KEGG; cfa:403947; -.
DR CTD; 9367; -.
DR VEuPathDB; HostDB:ENSCAFG00845028510; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000158619; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; P24408; -.
DR OMA; FQNLGNW; -.
DR OrthoDB; 1579101at2759; -.
DR TreeFam; TF326442; -.
DR Reactome; R-CFA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-CFA-8873719; RAB geranylgeranylation.
DR Reactome; R-CFA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-CFA-9706019; RHOBTB3 ATPase cycle.
DR EvolutionaryTrace; P24408; -.
DR Proteomes; UP000002254; Chromosome X.
DR Bgee; ENSCAFG00000011750; Expressed in spinal cord and 48 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd04116; Rab9; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041824; Rab9.
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; Cell membrane; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT CHAIN 2..201
FT /note="Ras-related protein Rab-9A"
FT /id="PRO_0000121138"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15196914,
FT ECO:0007744|PDB:1S8F"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15196914,
FT ECO:0007744|PDB:1S8F"
FT BINDING 155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:15196914,
FT ECO:0007744|PDB:1S8F"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:1S8F"
FT STRAND 38..51
FT /evidence="ECO:0007829|PDB:1S8F"
FT STRAND 54..63
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1S8F"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1S8F"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1S8F"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1S8F"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1S8F"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1S8F"
SQ SEQUENCE 201 AA; 22811 MW; 65B502C204BEDB72 CRC64;
MAGKSSLFKV ILLGDGGVGK SSLMNRYVTN KFDTQLFHTI GVEFLNKDLE VDGHFVTMQI
WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV
ILGNKIDISE RQVSTEEAQA WCRDNGDYPY FETSAKDATN VAAAFEEAVR RVLATEDRSD
HLIQTDTVSL HRKPKPSSSC C
