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 23-FEB-2022, entry version 142. 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}. 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 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; 83 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; 1 hit in 64 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 133 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 NP_BIND 14..22 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9NP90" FT NP_BIND 33..34 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9NP90" FT NP_BIND 38..39 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9NP90" FT NP_BIND 124..127 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9NP90" FT NP_BIND 155..156 FT /note="GTP" FT /evidence="ECO:0000250|UniProtKB:Q9NP90" FT MOTIF 36..44 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 65 FT /note="GTP; via amide nitrogen" 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 //