RAB9B_MOUSE
ID RAB9B_MOUSE Reviewed; 201 AA.
AC Q8BHH2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ras-related protein Rab-9B;
GN Name=Rab9b;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Spinal cord;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [3]
RP INTERACTION WITH SGSM1.
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. {ECO:0000250|UniProtKB:P24408}.
CC -!- SUBUNIT: Interacts (GTP-bound form) with SGSM1; the GDP-bound form has
CC much lower affinity for SGSM1 (PubMed:25220469). The GTP-bound form but
CC not the GDP-bound form interacts with HPS4 and the BLOC-3 complex
CC (heterodimer of HPS1 and HPS4) but does not interact with HPS1 alone
CC (By similarity). {ECO:0000250|UniProtKB:Q9NP90,
CC ECO:0000305|PubMed:25220469}.
CC -!- INTERACTION:
CC Q8BHH2; Q8BHH2: Rab9b; NbExp=2; IntAct=EBI-11568845, EBI-11568845;
CC Q8BHH2; Q8BPQ7-1: Sgsm1; NbExp=3; IntAct=EBI-11568845, EBI-16121756;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing
CC S.aureus or Mycobacterium. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK034442; BAC28710.1; -; mRNA.
DR EMBL; AK049693; BAC33876.1; -; mRNA.
DR CCDS; CCDS30425.1; -.
DR RefSeq; NP_795945.1; NM_176971.2.
DR AlphaFoldDB; Q8BHH2; -.
DR SMR; Q8BHH2; -.
DR DIP; DIP-61069N; -.
DR IntAct; Q8BHH2; 12.
DR STRING; 10090.ENSMUSP00000049739; -.
DR iPTMnet; Q8BHH2; -.
DR PhosphoSitePlus; Q8BHH2; -.
DR jPOST; Q8BHH2; -.
DR MaxQB; Q8BHH2; -.
DR PaxDb; Q8BHH2; -.
DR PRIDE; Q8BHH2; -.
DR ProteomicsDB; 253156; -.
DR ABCD; Q8BHH2; 22 sequenced antibodies.
DR Antibodypedia; 29164; 86 antibodies from 27 providers.
DR DNASU; 319642; -.
DR Ensembl; ENSMUST00000058814; ENSMUSP00000049739; ENSMUSG00000043463.
DR GeneID; 319642; -.
DR KEGG; mmu:319642; -.
DR UCSC; uc009uje.1; mouse.
DR CTD; 51209; -.
DR MGI; MGI:2442454; Rab9b.
DR VEuPathDB; HostDB:ENSMUSG00000043463; -.
DR eggNOG; KOG0394; Eukaryota.
DR GeneTree; ENSGT00940000160481; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q8BHH2; -.
DR OMA; NRKAPRS; -.
DR OrthoDB; 1172019at2759; -.
DR PhylomeDB; Q8BHH2; -.
DR TreeFam; TF326442; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
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; 319642; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rab9b; mouse.
DR PRO; PR:Q8BHH2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BHH2; protein.
DR Bgee; ENSMUSG00000043463; Expressed in ventromedial nucleus of hypothalamus and 80 other tissues.
DR ExpressionAtlas; Q8BHH2; baseline and differential.
DR Genevisible; Q8BHH2; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
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 Cell membrane; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-9B"
FT /id="PRO_0000121143"
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:Q9NP90"
FT BINDING 33..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT BINDING 38..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT BINDING 65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT BINDING 155..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 22704 MW; 1E28B18F8F8DDDFD CRC64;
MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE VDGRFVTLQI
WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN WQKEFIYYAD VKDPDHFPFV
VLGNKVDKED RQVTTEEAQA WCMENGNYPY LETSAKDDTN VTVAFEEAVR QVLAVEEQLE
HCMLGHTIDL NSGSKASSSC C
