RAB9A_RAT
ID RAB9A_RAT Reviewed; 201 AA.
AC Q99P75; Q6NS34;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ras-related protein Rab-9A;
GN Name=Rab9a; Synonyms=Rab9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Bone;
RX PubMed=12051767; DOI=10.1016/s0006-291x(02)00326-1;
RA Zhao H., Ettala O., Vaananen H.K.;
RT "Intracellular membrane trafficking pathways in bone-resorbing osteoclasts
RT revealed by cloning and subcellular localization studies of small GTP-
RT binding rab proteins.";
RL Biochem. Biophys. Res. Commun. 293:1060-1065(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [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).
CC -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC and the trans-Golgi network. Involved in the recruitment of SGSM2 to
CC melanosomes and is required for the proper trafficking of melanogenic
CC enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes.
CC {ECO:0000250|UniProtKB:P24408, ECO:0000250|UniProtKB:Q9R0M6}.
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 -!- 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:0000269|PubMed:12051767}. 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; AF325692; AAG49586.1; -; mRNA.
DR EMBL; BC070502; AAH70502.1; -; mRNA.
DR RefSeq; NP_445910.1; NM_053458.1.
DR AlphaFoldDB; Q99P75; -.
DR SMR; Q99P75; -.
DR STRING; 10116.ENSRNOP00000050986; -.
DR jPOST; Q99P75; -.
DR PaxDb; Q99P75; -.
DR PRIDE; Q99P75; -.
DR Ensembl; ENSRNOT00000050018; ENSRNOP00000050986; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000101281; ENSRNOP00000092308; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000106763; ENSRNOP00000088630; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000109401; ENSRNOP00000089377; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000111202; ENSRNOP00000086590; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000118631; ENSRNOP00000080913; ENSRNOG00000030443.
DR Ensembl; ENSRNOT00000119653; ENSRNOP00000081896; ENSRNOG00000030443.
DR GeneID; 84589; -.
DR KEGG; rno:84589; -.
DR UCSC; RGD:619740; rat.
DR CTD; 9367; -.
DR RGD; 619740; Rab9a.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000158619; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q99P75; -.
DR OMA; EEAKQWC; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q99P75; -.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-RNO-9706019; RHOBTB3 ATPase cycle.
DR PRO; PR:Q99P75; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000030443; Expressed in liver and 20 other tissues.
DR Genevisible; Q99P75; RN.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
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; ISO:RGD.
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 Acetylation; Cell membrane; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW 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_0000121141"
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:0000250|UniProtKB:P51151"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT BINDING 155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0M6"
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 CONFLICT 29
FT /note="T -> A (in Ref. 1; AAG49586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22896 MW; 43F490EAA67CF7EA CRC64;
MAGKSSLFKI ILLGDGGVGK SSLMNRYVTN KFDSQLFHTI GVEFLNKDLE VDGHFVTMQI
WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV
ILGNKTDIKE RQVSTEEAQA WCKDNGDYPY FETSAKDSTN VAAAFEEAVR RILATEDRSD
HLIQTDTVNL HRKPKPNSSC C
