RB11B_DIPOM
ID RB11B_DIPOM Reviewed; 218 AA.
AC P22129;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ras-related protein Rab-11B;
DE AltName: Full=ORA3;
DE Flags: Precursor;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric lobe;
RX PubMed=1899244; DOI=10.1016/s0021-9258(18)52297-3;
RA Ngsee J.K., Elferink L.A., Scheller R.H.;
RT "A family of ras-like GTP-binding proteins expressed in electromotor
RT neurons.";
RL J. Biol. Chem. 266:2675-2680(1991).
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. That Rab plays a role in
CC endocytic recycling, regulating apical recycling of several
CC 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M38392; AAA49233.1; -; mRNA.
DR PIR; C38625; C38625.
DR AlphaFoldDB; P22129; -.
DR SMR; P22129; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR GO; GO:0045054; P:constitutive secretory pathway; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
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; ISS: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 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasmic vesicle; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-11B"
FT /id="PRO_0000121161"
FT PROPEP 216..218
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370818"
FT REGION 183..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 24556 MW; 1DF9E40CE29DFE8F CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADNNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ
ISDRSAHDES PGNNVVDISV PPTTDGQKSN KLQCCQNM
