RAB8B_RAT
ID RAB8B_RAT Reviewed; 207 AA.
AC P70550;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ras-related protein Rab-8B;
DE Flags: Precursor;
GN Name=Rab8b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8799816; DOI=10.1242/jcs.109.6.1265;
RA Armstrong J., Thompson N., Squire J.H., Smith J., Hayes B., Solari R.;
RT "Identification of a novel member of the Rab8 family from the rat
RT basophilic leukaemia cell line, RBL.2H3.";
RL J. Cell Sci. 109:1265-1274(1996).
RN [2]
RP INTERACTION WITH PEX5R.
RX PubMed=11278749; DOI=10.1074/jbc.m010798200;
RA Chen S., Liang M.C., Chia J.N., Ngsee J.K., Ting A.E.;
RT "Rab8b and its interacting partner TRIP8b are involved in regulated
RT secretion in AtT20 cells.";
RL J. Biol. Chem. 276:13209-13216(2001).
RN [3]
RP FUNCTION IN CELL JUNCTION DYNAMICS, ASSOCIATION WITH ACTIN; DELTA-CATENIN
RP AND ALPHA AND BETA TUBULINS, INTERACTION WITH VIM AND CDH1, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12639940; DOI=10.1210/en.2002-220893;
RA Lau A.S., Mruk D.D.;
RT "Rab8B GTPase and junction dynamics in the testis.";
RL Endocrinology 144:1549-1563(2003).
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.
CC {ECO:0000269|PubMed:12639940}.
CC -!- SUBUNIT: Associated with actin, delta-catenin and alpha and beta
CC tubulins (PubMed:12639940). Interacts with OTOF (By similarity).
CC Interacts with PEX5R (PubMed:11278749). Interacts with RAB3IP (By
CC similarity). Interacts with VIM (PubMed:12639940). Interacts with CDH1
CC (PubMed:12639940). Interacts with MICALL2 (By similarity). Interacts
CC with GDI1, GDI2 and CHM; phosphorylation at Thr-72 disrupts these
CC interactions (By similarity). {ECO:0000250|UniProtKB:P61028,
CC ECO:0000250|UniProtKB:Q92930, ECO:0000269|PubMed:11278749,
CC ECO:0000269|PubMed:12639940}.
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 (By similarity). Colocalizes with CDH1 in the
CC basal compartment. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Hight levels of expression in the spleen, heart,
CC kidney, testis and brain. Expression increases in Sertoli and germ
CC cells during their maturation. {ECO:0000269|PubMed:12639940}.
CC -!- DEVELOPMENTAL STAGE: Localizes in the basal compartment associating
CC with spermatocytes in all stages of the spermatogenic cycle. Detected
CC at the site of elongate spermatids in stages XII-XIV in addition to
CC being found in the basal compartment in these stages.
CC {ECO:0000269|PubMed:12639940}.
CC -!- PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM and
CC 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; U53475; AAA99782.1; -; mRNA.
DR RefSeq; NP_695229.1; NM_153317.1.
DR AlphaFoldDB; P70550; -.
DR SMR; P70550; -.
DR BioGRID; 251776; 1.
DR IntAct; P70550; 3.
DR STRING; 10116.ENSRNOP00000024287; -.
DR iPTMnet; P70550; -.
DR PhosphoSitePlus; P70550; -.
DR jPOST; P70550; -.
DR PaxDb; P70550; -.
DR PRIDE; P70550; -.
DR Ensembl; ENSRNOT00000024286; ENSRNOP00000024287; ENSRNOG00000018009.
DR GeneID; 266688; -.
DR KEGG; rno:266688; -.
DR UCSC; RGD:628764; rat.
DR CTD; 51762; -.
DR RGD; 628764; Rab8b.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000155363; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P70550; -.
DR OMA; IMENRSK; -.
DR OrthoDB; 1426655at2759; -.
DR PhylomeDB; P70550; -.
DR TreeFam; TF314097; -.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P70550; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000018009; Expressed in spleen and 20 other tissues.
DR ExpressionAtlas; P70550; baseline and differential.
DR Genevisible; P70550; RN.
DR GO; GO:0051286; C:cell tip; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
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:RGD.
DR GO; GO:0030911; F:TPR domain binding; IPI:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0150115; P:cell-substrate junction organization; IDA: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; IDA:RGD.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; IDA:RGD.
DR GO; GO:0045046; P:protein import into peroxisome membrane; ISO:RGD.
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_0000121136"
FT PROPEP 205..207
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370803"
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"
FT /evidence="ECO:0000250|UniProtKB:Q92930"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61028"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61028"
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
