RB11A_RAT
ID RB11A_RAT Reviewed; 216 AA.
AC P62494; P24410; Q9JLX1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ras-related protein Rab-11A {ECO:0000250|UniProtKB:P62492};
DE Short=Rab-11 {ECO:0000250|UniProtKB:P62492};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62491};
DE AltName: Full=24KG;
DE Flags: Precursor;
GN Name=Rab11a {ECO:0000312|RGD:619762};
GN Synonyms=Rab11 {ECO:0000250|UniProtKB:P62492};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=1711847; DOI=10.1016/0006-291x(91)90672-t;
RA Sakurada K., Uchida K., Yamaguchi K., Aisaka K., Ito S., Ohmori T.,
RA Takeyama Y., Ueda T., Hori Y., Ohyanagi H., Saitoh Y., Kaibuchi K.,
RA Takai Y.;
RT "Molecular cloning and characterization of a ras p21-like GTP-binding
RT protein (24KG) from rat liver.";
RL Biochem. Biophys. Res. Commun. 177:1224-1232(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 FUNCTION, AND INTERACTION WITH RAB11FIP5.
RX PubMed=11163216; DOI=10.1016/s1097-2765(00)00140-4;
RA Prekeris R., Klumperman J., Scheller R.H.;
RT "A Rab11/Rip11 protein complex regulates apical membrane trafficking via
RT recycling endosomes.";
RL Mol. Cell 6:1437-1448(2000).
RN [4]
RP INTERACTION WITH STXBP6.
RX PubMed=12145319; DOI=10.1074/jbc.m204929200;
RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.;
RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex
RT assembly.";
RL J. Biol. Chem. 277:28271-28279(2002).
RN [5]
RP INTERACTION WITH ZFYVE27.
RX PubMed=17082457; DOI=10.1126/science.1134027;
RA Shirane M., Nakayama K.I.;
RT "Protrudin induces neurite formation by directional membrane trafficking.";
RL Science 314:818-821(2006).
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 (By similarity). Rabs cycle between an inactive
CC GDP-bound form and an active GTP-bound form that is able to recruit to
CC membranes different set of downstream effectors directly responsible
CC for vesicle formation, movement, tethering and fusion (By similarity).
CC The small Rab GTPase RAB11A regulates endocytic recycling
CC (PubMed:11163216). Acts as a major regulator of membrane delivery
CC during cytokinesis. Together with MYO5B and RAB8A participates in
CC epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst
CC complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of
CC PODXL to the apical membrane initiation sites (AMIS), apical surface
CC formation and lumenogenesis. Together with MYO5B participates in CFTR
CC trafficking to the plasma membrane and TF (Transferrin) recycling in
CC nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for
CC the transport of NPC1L1 to the plasma membrane. Participates in the
CC sorting and basolateral transport of CDH1 from the Golgi apparatus to
CC the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc
CC region of monomeric Ig G) to basolateral membranes (By similarity). May
CC also play a role in melanosome transport and release from melanocytes
CC (By similarity). {ECO:0000250|UniProtKB:P62491,
CC ECO:0000250|UniProtKB:P62492, ECO:0000269|PubMed:11163216}.
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:P62491};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62491};
CC -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-
CC terminus) and RAB11FIP4 (By similarity). Interacts with EVI5; EVI5 and
CC RAB11FIP3 may be mutually exclusive and compete for binding RAB11A (By
CC similarity). Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39 (By
CC similarity). Interacts with EXOC6 in a GTP-dependent manner. Interacts
CC with RAB11FIP5 (PubMed:11163216). Interacts with STXBP6
CC (PubMed:12145319). Interacts (GDP-bound form) with ZFYVE27
CC (PubMed:17082457). Interacts with BIRC6/bruce (By similarity). May
CC interact with TBC1D14 (By similarity). Interacts with UNC119; in a cell
CC cycle-dependent manner (By similarity). GDP-bound and nucleotide-free
CC forms interact with SH3BP5 (By similarity). Interacts (GDP-bound form)
CC with KIF5A in a ZFYVE27-dependent manner (By similarity). Interacts
CC (GDP-bound form) with RELCH (By similarity). Found in a complex
CC composed of RELCH, OSBP1 and RAB11A (By similarity). Interacts with
CC TBC1D12 (By similarity). Interacts with DEF6 (By similarity).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62492,
CC ECO:0000269|PubMed:11163216, ECO:0000269|PubMed:12145319,
CC ECO:0000269|PubMed:17082457}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P62491};
CC Lipid-anchor {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P62491}; Lipid-anchor {ECO:0000305}. Cleavage
CC furrow {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P62491}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P62491}. Note=Translocates with RAB11FIP2 from
CC the vesicles of the endocytic recycling compartment (ERC) to the plasma
CC membrane. Localizes to the cleavage furrow. Colocalizes with PARD3,
CC PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites
CC (AMIS) during the generation of apical surface and lumenogenesis.
CC {ECO:0000250|UniProtKB:P62491}.
CC -!- TISSUE SPECIFICITY: Detected in various tissues, such as brain, testis,
CC spleen, and heart. {ECO:0000269|PubMed:1711847}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M75153; AAA42012.1; -; mRNA.
DR EMBL; BC085727; AAH85727.1; -; mRNA.
DR PIR; JN0056; JN0056.
DR RefSeq; NP_112414.1; NM_031152.2.
DR AlphaFoldDB; P62494; -.
DR SMR; P62494; -.
DR BioGRID; 249688; 1.
DR DIP; DIP-46857N; -.
DR IntAct; P62494; 7.
DR MINT; P62494; -.
DR STRING; 10116.ENSRNOP00000015598; -.
DR iPTMnet; P62494; -.
DR PhosphoSitePlus; P62494; -.
DR jPOST; P62494; -.
DR PaxDb; P62494; -.
DR PRIDE; P62494; -.
DR Ensembl; ENSRNOT00000015598; ENSRNOP00000015598; ENSRNOG00000011302.
DR GeneID; 81830; -.
DR KEGG; rno:81830; -.
DR UCSC; RGD:619762; rat.
DR CTD; 8766; -.
DR RGD; 619762; Rab11a.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000154914; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P62494; -.
DR OMA; SMKEDYY; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; P62494; -.
DR TreeFam; TF300099; -.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR PRO; PR:P62494; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000011302; Expressed in stomach and 20 other tissues.
DR Genevisible; P62494; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005771; C:multivesicular body; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0000922; C:spindle pole; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
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:0030953; P:astral microtubule organization; ISO:RGD.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:RGD.
DR GO; GO:0072594; P:establishment of protein localization to organelle; ISO:RGD.
DR GO; GO:0051650; P:establishment of vesicle localization; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1990182; P:exosomal secretion; ISO:RGD.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD.
DR GO; GO:0036258; P:multivesicular body assembly; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0010796; P:regulation of multivesicular body size; ISO:RGD.
DR GO; GO:0051223; P:regulation of protein transport; IMP:RGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
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; Cell cycle; Cell membrane; Cytoplasmic vesicle; Endosome;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT CHAIN 2..213
FT /note="Ras-related protein Rab-11A"
FT /id="PRO_0000121156"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370812"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 37..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MOD_RES 213
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
SQ SEQUENCE 216 AA; 24394 MW; 76FC1E113A29B269 CRC64;
MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ
MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI
