RAB9A_MOUSE
ID RAB9A_MOUSE Reviewed; 201 AA.
AC Q9R0M6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ras-related protein Rab-9A;
DE AltName: Full=Sid 99;
GN Name=Rab9a; Synonyms=Rab9, Sid99;
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].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse small GTP binding protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Head, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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 [5]
RP INTERACTION WITH HPS4.
RX PubMed=20048159; DOI=10.1074/jbc.m109.069088;
RA Kloer D.P., Rojas R., Ivan V., Moriyama K., van Vlijmen T., Murthy N.,
RA Ghirlando R., van der Sluijs P., Hurley J.H., Bonifacino J.S.;
RT "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-
RT 3) and its interaction with Rab9.";
RL J. Biol. Chem. 285:7794-7804(2010).
RN [6]
RP FUNCTION, INTERACTION WITH SGSM2 AND HPS4, AND SUBCELLULAR LOCATION.
RX PubMed=26620560; DOI=10.1074/jbc.m115.684043;
RA Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
RT "RUTBC1 functions as a GTPase-activating protein for Rab32/38 and regulates
RT melanogenic enzyme trafficking in melanocytes.";
RL J. Biol. Chem. 291:1427-1440(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-199 IN COMPLEX WITH GTP AND
RP SGSM1, AND SUBCELLULAR LOCATION.
RX PubMed=25220469; DOI=10.1016/j.str.2014.08.005;
RA Zhang Z., Wang S., Shen T., Chen J., Ding J.;
RT "Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular
RT basis for the binding specificity of Rab9A with RUTBC2.";
RL Structure 22:1408-1420(2014).
CC -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC and the trans-Golgi network (By similarity). 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 (PubMed:26620560).
CC {ECO:0000250|UniProtKB:P24408, ECO:0000269|PubMed:26620560}.
CC -!- SUBUNIT: Interacts (preferentially in its GTP-bound form) with GCC2
CC (via its GRIP domain) (By similarity). Interacts (GTP-bound form) with
CC SGSM1; the GDP-bound form has much lower affinity for SGSM1
CC (PubMed:25220469). Interacts with SGSM2 (PubMed:26620560). The GTP-
CC bound form but not the GDP-bound form interacts with HPS4
CC (PubMed:26620560, PubMed:20048159). The GTP-bound form but not the GDP-
CC bound form interacts with BLOC-3 complex (heterodimer of HPS1 and HPS4)
CC but does not interact with HPS1 alone (By similarity).
CC {ECO:0000250|UniProtKB:P51151, ECO:0000269|PubMed:20048159,
CC ECO:0000269|PubMed:25220469, ECO:0000269|PubMed:26620560}.
CC -!- INTERACTION:
CC Q9R0M6; Q9R0M6: Rab9a; NbExp=2; IntAct=EBI-6552247, EBI-6552247;
CC Q9R0M6; Q8BPQ7-1: Sgsm1; NbExp=8; IntAct=EBI-6552247, EBI-16121756;
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 Melanosome {ECO:0000269|PubMed:26620560}. Note=Colocalizes with OSBPL1A
CC at the 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; AB027290; BAA84709.1; -; mRNA.
DR EMBL; AK010710; BAB27135.1; -; mRNA.
DR EMBL; AK017301; BAB30681.1; -; mRNA.
DR EMBL; AK032133; BAC27720.1; -; mRNA.
DR EMBL; BC008160; AAH08160.1; -; mRNA.
DR CCDS; CCDS30527.1; -.
DR RefSeq; NP_062747.1; NM_019773.2.
DR RefSeq; XP_006528985.1; XM_006528922.1.
DR PDB; 1YZL; X-ray; 1.85 A; A=2-175.
DR PDB; 4QXA; X-ray; 2.30 A; A=1-199.
DR PDBsum; 1YZL; -.
DR PDBsum; 4QXA; -.
DR AlphaFoldDB; Q9R0M6; -.
DR SMR; Q9R0M6; -.
DR BioGRID; 207943; 1.
DR DIP; DIP-61068N; -.
DR IntAct; Q9R0M6; 4.
DR MINT; Q9R0M6; -.
DR STRING; 10090.ENSMUSP00000123325; -.
DR iPTMnet; Q9R0M6; -.
DR PhosphoSitePlus; Q9R0M6; -.
DR EPD; Q9R0M6; -.
DR jPOST; Q9R0M6; -.
DR MaxQB; Q9R0M6; -.
DR PaxDb; Q9R0M6; -.
DR PRIDE; Q9R0M6; -.
DR ProteomicsDB; 300291; -.
DR ABCD; Q9R0M6; 22 sequenced antibodies.
DR Antibodypedia; 513; 289 antibodies from 35 providers.
DR DNASU; 56382; -.
DR Ensembl; ENSMUST00000112091; ENSMUSP00000123325; ENSMUSG00000079316.
DR GeneID; 56382; -.
DR KEGG; mmu:56382; -.
DR UCSC; uc009uwu.2; mouse.
DR CTD; 56382; -.
DR MGI; MGI:1890695; Rab9.
DR VEuPathDB; HostDB:ENSMUSG00000079316; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000158619; -.
DR InParanoid; Q9R0M6; -.
DR OMA; FQNLGNW; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q9R0M6; -.
DR TreeFam; TF326442; -.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-MMU-9706019; RHOBTB3 ATPase cycle.
DR BioGRID-ORCS; 56382; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Rab9; mouse.
DR EvolutionaryTrace; Q9R0M6; -.
DR PRO; PR:Q9R0M6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R0M6; protein.
DR Bgee; ENSMUSG00000079316; Expressed in trigeminal ganglion and 243 other tissues.
DR ExpressionAtlas; Q9R0M6; baseline and differential.
DR Genevisible; Q9R0M6; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
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:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA: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; IPI:IntAct.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
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:MGI.
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_0000121140"
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:0000269|PubMed:25220469,
FT ECO:0007744|PDB:4QXA"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4QXA"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25220469,
FT ECO:0007744|PDB:4QXA"
FT BINDING 155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:4QXA"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51151"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 6..13
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:1YZL"
FT STRAND 43..62
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1YZL"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4QXA"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1YZL"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:1YZL"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1YZL"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1YZL"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1YZL"
SQ SEQUENCE 201 AA; 22910 MW; 43F490EAA67D2C9A CRC64;
MAGKSSLFKI ILLGDGGVGK SSLMNRYVTN KFDSQLFHTI GVEFLNKDLE VDGHFVTMQI
WDTAGQERFR SLRTPFYRGS DCCLLTFSVD DSQSFQNLSN WKKEFIYYAD VKEPESFPFV
ILGNKTDIKE RQVSTEEAQA WCKDNGDYPY FETSAKDSTN VAAAFEEAVR RILATEDRSE
HLIQTDTVNL HRKPKPNSSC C
