RAB8B_MOUSE
ID RAB8B_MOUSE Reviewed; 207 AA.
AC P61028; Q3U1Z3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ras-related protein Rab-8B;
DE Flags: Precursor;
GN Name=Rab8b;
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=Heart;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 OTOF.
RX PubMed=18772196; DOI=10.1093/hmg/ddn279;
RA Heidrych P., Zimmermann U., Bress A., Pusch C.M., Ruth P., Pfister M.,
RA Knipper M., Blin N.;
RT "Rab8b GTPase, a protein transport regulator, is an interacting partner of
RT otoferlin, defective in a human autosomal recessive deafness form.";
RL Hum. Mol. Genet. 17:3814-3821(2008).
RN [4]
RP INTERACTION WITH MICALL2.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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 [7]
RP PHOSPHORYLATION AT THR-72.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different sets of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab may be involved in
CC polarized vesicular trafficking and neurotransmitter release. May
CC participate in cell junction dynamics in Sertoli cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Associated with actin, delta-catenin and alpha and beta
CC tubulins (By similarity). Interacts with OTOF (PubMed:18772196).
CC Interacts with PEX5R (By similarity). Interacts with RAB3IP (By
CC similarity). Interacts with VIM (By similarity). Interacts with CDH1
CC (By similarity). Interacts with MICALL2 (PubMed:18094055). Interacts
CC with GDI1, GDI2, CHML and CHM; phosphorylation at Thr-72 disrupts these
CC interactions (By similarity). {ECO:0000250|UniProtKB:P70550,
CC ECO:0000250|UniProtKB:Q92930, ECO:0000269|PubMed:18094055,
CC ECO:0000269|PubMed:18772196}.
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 -!- PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:Q92930}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK084650; BAC39239.1; -; mRNA.
DR EMBL; AK155621; BAE33350.1; -; mRNA.
DR EMBL; BC059208; AAH59208.1; -; mRNA.
DR CCDS; CCDS23309.1; -.
DR RefSeq; NP_775589.1; NM_173413.3.
DR AlphaFoldDB; P61028; -.
DR SMR; P61028; -.
DR BioGRID; 231663; 13.
DR IntAct; P61028; 9.
DR STRING; 10090.ENSMUSP00000041857; -.
DR iPTMnet; P61028; -.
DR PhosphoSitePlus; P61028; -.
DR SwissPalm; P61028; -.
DR EPD; P61028; -.
DR jPOST; P61028; -.
DR PaxDb; P61028; -.
DR PeptideAtlas; P61028; -.
DR PRIDE; P61028; -.
DR ProteomicsDB; 253155; -.
DR Antibodypedia; 25649; 262 antibodies from 31 providers.
DR DNASU; 235442; -.
DR Ensembl; ENSMUST00000041139; ENSMUSP00000041857; ENSMUSG00000036943.
DR GeneID; 235442; -.
DR KEGG; mmu:235442; -.
DR UCSC; uc009qfk.2; mouse.
DR CTD; 51762; -.
DR MGI; MGI:2442982; Rab8b.
DR VEuPathDB; HostDB:ENSMUSG00000036943; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000155363; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P61028; -.
DR OMA; IMENRSK; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P61028; -.
DR TreeFam; TF314097; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 235442; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Rab8b; mouse.
DR PRO; PR:P61028; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P61028; protein.
DR Bgee; ENSMUSG00000036943; Expressed in stroma of bone marrow and 235 other tissues.
DR ExpressionAtlas; P61028; baseline and differential.
DR Genevisible; P61028; MM.
DR GO; GO:0051286; C:cell tip; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0030911; F:TPR domain binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0150115; P:cell-substrate junction organization; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IBA:GO_Central.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; ISO:MGI.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
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 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 Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..204
FT /note="Ras-related protein Rab-8B"
FT /id="PRO_0000121135"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370801"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="Phosphothreonine; by LRRK2"
FT /evidence="ECO:0000269|PubMed:29125462"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 204
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23603 MW; 4A41AB26BF9DCAF4 CRC64;
MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI ELDGKKIKLQ
IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK NWIRNIEEHA SSDVERMILG
NKCDMNDKRQ VSKERGEKLA IDYGIKFLET SAKSSTNVEE AFFTLARDIM TKLNRKMNDS
NSSGAGGPVK ITESRSKKTS FFRCSLL
