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   24-JAN-2024, entry version 178.
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. Promotes Rabin8/RAB3IP preciliary
CC       vesicular trafficking to mother centriole by forming a ciliary
CC       targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and
CC       ARF4, thereby regulating ciliogenesis initiation. On the contrary, upon
CC       LPAR1 receptor signaling pathway activation, interaction with
CC       phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation
CC       and cilia growth (By similarity). {ECO:0000250|UniProtKB:Q15907,
CC       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). Forms a complex containing RAB11B,
CC       ASAP1, Rabin8/RAB3IP, RAP11FIP3 and ARF4. Interacts with WDR44 (By
CC       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; 10116-ENSRNOP00000010197; -.
DR   GeneID; 79434; -.
DR   KEGG; rno:79434; -.
DR   UCSC; RGD:68369; rat.
DR   AGR; RGD:68369; -.
DR   CTD; 9230; -.
DR   RGD; 68369; Rab11b.
DR   VEuPathDB; HostDB:ENSRNOG00000007648; -.
DR   eggNOG; KOG0087; Eukaryota.
DR   InParanoid; O35509; -.
DR   OrthoDB; 3487147at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; O35509; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
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:0030672; C:synaptic vesicle membrane; IDA:SynGO.
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: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:2001135; P:regulation of endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0044070; P:regulation of monoatomic anion transport; 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   CDD; cd01868; Rab11_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47979; DRAB11-RELATED; 1.
DR   PANTHER; PTHR47979:SF41; RAS-RELATED PROTEIN RAB-11B; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   Genevisible; O35509; RN.
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
//