RB11A_PONAB
ID RB11A_PONAB Reviewed; 216 AA.
AC Q5R9M7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Flags: Precursor;
GN Name=RAB11A {ECO:0000250|UniProtKB:P62492};
GN Synonyms=RAB11 {ECO:0000250|UniProtKB:P62492};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 RAB11A
CC regulates endocytic recycling. Acts as a major regulator of membrane
CC delivery during cytokinesis. Together with MYO5B and RAB8A participates
CC in epithelial cell polarization. Together with RAB3IP, RAB8A, the
CC exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes
CC transcytosis of PODXL to the apical membrane initiation sites (AMIS),
CC apical surface formation and lumenogenesis. Together with MYO5B
CC participates in CFTR trafficking to the plasma membrane and TF
CC (Transferrin) recycling in nonpolarized cells. Required in a complex
CC with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma
CC membrane. Participates in the sorting and basolateral transport of CDH1
CC from the Golgi apparatus to the plasma membrane. Regulates the
CC recycling of FCGRT (receptor of Fc region of monomeric Ig G) to
CC basolateral membranes (By similarity). May also play a role in
CC melanosome transport and release from melanocytes (By similarity).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62492}.
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. Interacts with EVI5; EVI5 and RAB11FIP3 may be
CC mutually exclusive and compete for binding RAB11A. Interacts with
CC RAB11FIP5 (By similarity). Interacts with STXBP6 (By similarity).
CC Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39. Interacts with EXOC6 in
CC a GTP-dependent manner. Interacts (GDP-bound form) with ZFYVE27.
CC Interacts with BIRC6/bruce. May interact with TBC1D14. Interacts with
CC UNC119; in a cell cycle-dependent manner. GDP-bound and nucleotide-free
CC forms interact with SH3BP5. Interacts (GDP-bound form) with RELCH (By
CC similarity). Found in a complex composed of RELCH, OSBP1 and RAB11A (By
CC similarity). Interacts with DEF6 (By similarity).
CC {ECO:0000250|UniProtKB:P62491, ECO:0000250|UniProtKB:P62492,
CC ECO:0000250|UniProtKB:P62494}.
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; CR859359; CAH91533.1; -; mRNA.
DR RefSeq; NP_001127429.1; NM_001133957.1.
DR AlphaFoldDB; Q5R9M7; -.
DR SMR; Q5R9M7; -.
DR STRING; 9601.ENSPPYP00000007454; -.
DR Ensembl; ENSPPYT00000007758; ENSPPYP00000007454; ENSPPYG00000006573.
DR GeneID; 100174499; -.
DR KEGG; pon:100174499; -.
DR CTD; 8766; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000154914; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; Q5R9M7; -.
DR OMA; SMKEDYY; -.
DR OrthoDB; 1133775at2759; -.
DR TreeFam; TF300099; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0031489; F:myosin V binding; IEA:Ensembl.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IEA:Ensembl.
DR GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IEA:Ensembl.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IEA:Ensembl.
DR GO; GO:1990182; P:exosomal secretion; IEA:Ensembl.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0036258; P:multivesicular body assembly; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0010796; P:regulation of multivesicular body size; IEA:Ensembl.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:Ensembl.
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; 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_0000121154"
FT PROPEP 214..216
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370810"
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
