RB11B_RAT
ID RB11B_RAT Reviewed; 218 AA.
AC O35509; Q9ET14;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ras-related protein Rab-11B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:Q15907};
DE Flags: Precursor;
GN Name=Rab11b;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Sakurada K., Aisaka K., Ito S., Takeyama Y., Hori Y., Takai Y.;
RT "A novel YPT1/SEC4 related gene from rat brain.";
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Bone;
RA Zhao H., Gao L., Vaananen K.H.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP FUNCTION IN EXOCYTOSIS, AND SUBCELLULAR LOCATION.
RX PubMed=14627637; DOI=10.1523/jneurosci.23-33-10531.2003;
RA Khvotchev M.V., Ren M., Takamori S., Jahn R., Suedhof T.C.;
RT "Divergent functions of neuronal Rab11b in Ca2+-regulated versus
RT constitutive exocytosis.";
RL J. Neurosci. 23:10531-10539(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 set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. The small Rab GTPase RAB11B
CC plays a role in endocytic recycling, regulating apical recycling of
CC several transmembrane proteins including cystic fibrosis transmembrane
CC conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium
CC voltage-gated channel, and voltage-dependent L-type calcium channel.
CC May also regulate constitutive and regulated secretion, like insulin
CC granule exocytosis. Required for melanosome transport and release from
CC melanocytes. Also regulates V-ATPase intracellular transport in
CC response to extracellular acidosis. {ECO:0000269|PubMed:14627637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:Q15907};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q15907};
CC -!- SUBUNIT: Interacts with KCNMA1 (By similarity). Interacts with
CC RAB11FIP1, RAB11FIP2, RAB11FIP3 and RAB11FIP4 (By similarity). May
CC interact with TBC1D14 (By similarity). Interacts with ATP6V1E (By
CC similarity)1. Interacts with PI4KB (By similarity). Interacts with
CC RELCH (By similarity). Interacts (in GTP-bound form) with TBC1D8B (via
CC domain Rab-GAP TBC) (By similarity). {ECO:0000250|UniProtKB:P46638,
CC ECO:0000250|UniProtKB:Q15907}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P46638}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P46638}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P46638}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000305|PubMed:14627637}; Lipid-anchor
CC {ECO:0000305|PubMed:14627637}; Cytoplasmic side
CC {ECO:0000305|PubMed:14627637}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:Q15907}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q15907}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15907}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P46638}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; D01046; BAA22522.1; -; mRNA.
DR EMBL; AF286534; AAG00542.1; -; mRNA.
DR EMBL; BC062041; AAH62041.1; -; mRNA.
DR RefSeq; NP_116006.1; NM_032617.2.
DR AlphaFoldDB; O35509; -.
DR SMR; O35509; -.
DR BioGRID; 249465; 2.
DR IntAct; O35509; 3.
DR STRING; 10116.ENSRNOP00000010197; -.
DR iPTMnet; O35509; -.
DR PhosphoSitePlus; O35509; -.
DR jPOST; O35509; -.
DR PaxDb; O35509; -.
DR PRIDE; O35509; -.
DR GeneID; 79434; -.
DR KEGG; rno:79434; -.
DR UCSC; RGD:68369; rat.
DR CTD; 9230; -.
DR RGD; 68369; Rab11b.
DR VEuPathDB; HostDB:ENSRNOG00000007648; -.
DR eggNOG; KOG0087; Eukaryota.
DR InParanoid; O35509; -.
DR OMA; PSSYENC; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; O35509; -.
DR TreeFam; TF300099; -.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:O35509; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007648; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; O35509; baseline and differential.
DR Genevisible; O35509; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; 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:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:RGD.
DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; ISS:UniProtKB.
DR GO; GO:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; 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 Acetylation; Citrullination; Cytoplasmic vesicle; Endosome; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-11B"
FT /id="PRO_0000121160"
FT PROPEP 216..218
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT /id="PRO_0000370817"
FT REGION 184..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT MOD_RES 4
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P46638"
FT MOD_RES 215
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q15907"
FT CONFLICT 120
FT /note="M -> L (in Ref. 1; BAA22522)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..137
FT /note="PTD -> CPLT (in Ref. 1; BAA22522)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..147
FT /note="KNN -> RH (in Ref. 1; BAA22522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24489 MW; 8DF146BA39EBD9FF CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ
IADRAAHDES PGNNVVDISV PPTTDGQKPN KLQCCQNL
