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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
 
 
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