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 30-NOV-2016, entry version 115. DE RecName: Full=Ras-related protein Rab-9B; GN Name=Rab9b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RP BY 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 RT 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 RT molecular 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 CC endosomes and the trans Golgi network. CC {ECO:0000250|UniProtKB:P24408}. CC -!- SUBUNIT: Interacts (GTP-bound form) with SGSM1; the GDP-bound form CC has much lower affinity for SGSM1 (PubMed:25220469). The GTP-bound CC form but not the GDP-bound form interacts with HPS4 and the BLOC-3 CC complex (heterodimer of HPS1 and HPS4) but does not interact with CC HPS1 alone (By similarity). {ECO:0000250|UniProtKB:Q9NP90, CC ECO:0000305|PubMed:25220469}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic CC vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to CC phagosomes containing S.aureus or Mycobacterium. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.44557; -. DR ProteinModelPortal; Q8BHH2; -. DR SMR; Q8BHH2; -. DR DIP; DIP-61069N; -. DR IntAct; Q8BHH2; 10. DR STRING; 10090.ENSMUSP00000049739; -. DR iPTMnet; Q8BHH2; -. DR PhosphoSitePlus; Q8BHH2; -. DR MaxQB; Q8BHH2; -. DR PaxDb; Q8BHH2; -. DR PRIDE; Q8BHH2; -. 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 eggNOG; KOG0394; Eukaryota. DR eggNOG; ENOG410XNZV; LUCA. DR GeneTree; ENSGT00760000119125; -. DR HOGENOM; HOG000233968; -. DR HOVERGEN; HBG009351; -. DR InParanoid; Q8BHH2; -. DR KO; K07900; -. DR OMA; LSNWQKE; -. DR OrthoDB; EOG091G0JIV; -. DR PhylomeDB; Q8BHH2; -. DR TreeFam; TF326442; -. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR PRO; PR:Q8BHH2; -. DR Proteomes; UP000000589; Chromosome X. DR Bgee; ENSMUSG00000043463; -. DR CleanEx; MM_RAB9B; -. DR ExpressionAtlas; Q8BHH2; baseline and differential. DR Genevisible; Q8BHH2; MM. DR GO; GO:0005829; C:cytosol; IEA:GOC. 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:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 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; Complete proteome; Cytoplasmic vesicle; GTP-binding; KW Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein; KW Prenylation; Protein transport; Reference proteome; Transport. FT CHAIN 1 201 Ras-related protein Rab-9B. FT /FTId=PRO_0000121143. FT NP_BIND 14 22 GTP. {ECO:0000250|UniProtKB:Q9NP90}. FT NP_BIND 33 34 GTP. {ECO:0000250|UniProtKB:Q9NP90}. FT NP_BIND 38 39 GTP. {ECO:0000250|UniProtKB:Q9NP90}. FT NP_BIND 124 127 GTP. {ECO:0000250|UniProtKB:Q9NP90}. FT NP_BIND 155 156 GTP. {ECO:0000250|UniProtKB:Q9NP90}. FT MOTIF 36 44 Effector region. {ECO:0000250}. FT BINDING 65 65 GTP; via amide nitrogen. FT {ECO:0000250|UniProtKB:Q9NP90}. FT MOD_RES 34 34 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT LIPID 200 200 S-geranylgeranyl cysteine. {ECO:0000250}. FT LIPID 201 201 S-geranylgeranyl cysteine. {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 //