RB11A_CAEEL
ID RB11A_CAEEL Reviewed; 211 AA.
AC O01803; I7EVK5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ras-related protein rab-11.1 {ECO:0000250|UniProtKB:P62491};
DE AltName: Full=Rab GTPase rab-11.1 {ECO:0000305};
GN Name=rab-11.1 {ECO:0000312|WormBase:F53G12.1};
GN ORFNames=F53G12.1 {ECO:0000312|WormBase:F53G12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD71701.1,
RC ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000312|EMBL:AFP33153.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-211.
RX PubMed=23185324; DOI=10.1371/journal.pone.0049387;
RA Gallegos M.E., Balakrishnan S., Chandramouli P., Arora S., Azameera A.,
RA Babushekar A., Bargoma E., Bokhari A., Chava S.K., Das P., Desai M.,
RA Decena D., Saramma S.D., Dey B., Doss A.L., Gor N., Gudiputi L., Guo C.,
RA Hande S., Jensen M., Jones S., Jones N., Jorgens D., Karamchedu P.,
RA Kamrani K., Kolora L.D., Kristensen L., Kwan K., Lau H., Maharaj P.,
RA Mander N., Mangipudi K., Menakuru H., Mody V., Mohanty S., Mukkamala S.,
RA Mundra S.A., Nagaraju S., Narayanaswamy R., Ndungu-Case C., Noorbakhsh M.,
RA Patel J., Patel P., Pendem S.V., Ponakala A., Rath M., Robles M.C.,
RA Rokkam D., Roth C., Sasidharan P., Shah S., Tandon S., Suprai J.,
RA Truong T.Q., Uthayaruban R., Varma A., Ved U., Wang Z., Yu Z.;
RT "The C. elegans Rab family: Identification, classification and toolkit
RT construction.";
RL PLoS ONE 7:E49387-E49387(2012).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18472420; DOI=10.1016/j.cub.2008.04.043;
RA Cheng H., Govindan J.A., Greenstein D.;
RT "Regulated trafficking of the MSP/Eph receptor during oocyte meiotic
RT maturation in C. elegans.";
RL Curr. Biol. 18:705-714(2008).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18354496; DOI=10.1038/emboj.2008.54;
RA Sato M., Sato K., Liou W., Pant S., Harada A., Grant B.D.;
RT "Regulation of endocytic recycling by C. elegans Rab35 and its regulator
RT RME-4, a coated-pit protein.";
RL EMBO J. 27:1183-1196(2008).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18765566; DOI=10.1242/jcs.034678;
RA Sato M., Grant B.D., Harada A., Sato K.;
RT "Rab11 is required for synchronous secretion of chondroitin proteoglycans
RT after fertilization in Caenorhabditis elegans.";
RL J. Cell Sci. 121:3177-3186(2008).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18385514; DOI=10.1091/mbc.e07-09-0862;
RA Zhang H., Squirrell J.M., White J.G.;
RT "RAB-11 permissively regulates spindle alignment by modulating metaphase
RT microtubule dynamics in Caenorhabditis elegans early embryos.";
RL Mol. Biol. Cell 19:2553-2565(2008).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=19158384; DOI=10.1091/mbc.e08-09-0917;
RA Ai E., Poole D.S., Skop A.R.;
RT "RACK-1 directs dynactin-dependent RAB-11 endosomal recycling during
RT mitosis in Caenorhabditis elegans.";
RL Mol. Biol. Cell 20:1629-1638(2009).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20116245; DOI=10.1016/j.cub.2009.12.045;
RA Bembenek J.N., White J.G., Zheng Y.;
RT "A role for separase in the regulation of RAB-11-positive vesicles at the
RT cleavage furrow and midbody.";
RL Curr. Biol. 20:259-264(2010).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21320697; DOI=10.1016/j.chom.2011.01.005;
RA Los F.C., Kao C.Y., Smitham J., McDonald K.L., Ha C., Peixoto C.A.,
RA Aroian R.V.;
RT "RAB-5- and RAB-11-dependent vesicle-trafficking pathways are required for
RT plasma membrane repair after attack by bacterial pore-forming toxin.";
RL Cell Host Microbe 9:147-157(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22992455; DOI=10.1242/jcs.116400;
RA Kimura K., Kimura A.;
RT "Rab6 is required for the exocytosis of cortical granules and the
RT recruitment of separase to the granules during the oocyte-to-embryo
RT transition in Caenorhabditis elegans.";
RL J. Cell Sci. 125:5897-5905(2012).
RN [11] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22634595; DOI=10.1038/ncb2508;
RA Winter J.F., Hoepfner S., Korn K., Farnung B.O., Bradshaw C.R., Marsico G.,
RA Volkmer M., Habermann B., Zerial M.;
RT "Caenorhabditis elegans screen reveals role of PAR-5 in RAB-11-recycling
RT endosome positioning and apicobasal cell polarity.";
RL Nat. Cell Biol. 14:666-676(2012).
RN [12] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24843160; DOI=10.1073/pnas.1400696111;
RA Szumowski S.C., Botts M.R., Popovich J.J., Smelkinson M.G., Troemel E.R.;
RT "The small GTPase RAB-11 directs polarized exocytosis of the intracellular
RT pathogen N. parisii for fecal-oral transmission from C. elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8215-8220(2014).
RN [13] {ECO:0000305}
RP FUNCTION, INTERACTION WITH REI-1 AND REI-2, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=26506309; DOI=10.1016/j.devcel.2015.09.013;
RA Sakaguchi A., Sato M., Sato K., Gengyo-Ando K., Yorimitsu T., Nakai J.,
RA Hara T., Sato K., Sato K.;
RT "REI-1 is a guanine nucleotide exchange factor regulating RAB-11
RT localization and function in C. elegans embryos.";
RL Dev. Cell 35:211-221(2015).
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 (PubMed:21320697, PubMed:24843160). Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form that is
CC able to recruit to membranes different set of downstream effectors
CC directly responsible for vesicle formation, movement, tethering and
CC fusion (PubMed:21320697, PubMed:24843160). Involved in regulating the
CC meiotic maturation of oocytes (PubMed:18472420). Plays a role in egg
CC shell formation, regulating exocytosis of chondroitin proteoglycans
CC following fertilization (PubMed:18765566, PubMed:26506309). Controls
CC cortical granule localization and targets them to the plasma membrane
CC for exocytosis (PubMed:18765566, PubMed:22992455). Acts as a major
CC regulator of membrane delivery during cytokinesis (PubMed:18765566,
CC PubMed:20116245, PubMed:26506309). Regulates the cytoskeleton by
CC facilitating astral microtubule elongation and organization during
CC metaphase to ensure proper spindle alignment and polarity in the first
CC embryonic cell division (PubMed:18385514). Maintains normal endoplasmic
CC reticulum morphology during metaphase (PubMed:18385514). Involved in
CC vesicle formation and plasma membrane repair following exposure to pore
CC forming toxins (PubMed:21320697). Regulates endocytic recycling
CC (PubMed:24843160). May play a role in yolk receptor endocytosis in
CC growing oocytes (PubMed:18354496, PubMed:26506309). Plays a role in the
CC shedding of pathogen spores from intestinal cells via its involvement
CC in spore fusion and endocytic trafficking (PubMed:24843160).
CC {ECO:0000269|PubMed:18354496, ECO:0000269|PubMed:18385514,
CC ECO:0000269|PubMed:18472420, ECO:0000269|PubMed:18765566,
CC ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:21320697,
CC ECO:0000269|PubMed:22992455, ECO:0000269|PubMed:24843160,
CC ECO:0000269|PubMed:26506309}.
CC -!- SUBUNIT: Interacts with rei-1 and rei-2. The GDP-form preferentially
CC binds to rei-1 and rei-2. {ECO:0000269|PubMed:26506309}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:20116245,
CC ECO:0000269|PubMed:22992455}. Endosome {ECO:0000269|PubMed:19158384}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18385514,
CC ECO:0000269|PubMed:19158384}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:18385514}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:19158384}. Apical cell
CC membrane {ECO:0000269|PubMed:24843160}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24843160}. Recycling endosome membrane
CC {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18472420,
CC ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:22634595,
CC ECO:0000269|PubMed:26506309}; Lipid-anchor {ECO:0000305}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:18765566,
CC ECO:0000269|PubMed:26506309}. Cytoplasmic granule
CC {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:26506309}.
CC Note=Expressed in endosomal vesicles which localize to the
CC pericentriolar region of embryos during prophase and metaphase
CC (PubMed:19158384). Localizes along the spindle in embryos during
CC anaphase (PubMed:19158384). Transiently accumulates on secretory
CC vesicles before their exocytosis (PubMed:18765566). Localizes to
CC recycling endosomes and Golgi apparatus membrane in growing oocytes
CC (PubMed:18765566, PubMed:26506309). Translocates to cytoplasmic
CC granules and extracellular matrix components in mature oocytes
CC (PubMed:26506309). Accumulates on ring-shaped structures in ovulating
CC oocytes and in early one-cell stage embryos (PubMed:18765566).
CC Redistributes to recycling endosomes and Golgi apparatus in embryos
CC (PubMed:26506309). Co-localizes with rei-1 at Golgi apparatus membrane
CC in embryos (PubMed:26506309). Reycling endosomes co-localize with the
CC endoplasmic reticulum in embryos (PubMed:18385514). Co-localizes with
CC rab-6.1-positive vesicles near the plasma membrane until vesicle
CC exocytosis in embryos (PubMed:22992455). Localizes to the cytosol
CC during the meront-stage of N.parisii infection and around the resulting
CC spores that are to be shed from intestinal cells (PubMed:24843160).
CC {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18765566,
CC ECO:0000269|PubMed:19158384, ECO:0000269|PubMed:22992455,
CC ECO:0000269|PubMed:24843160, ECO:0000269|PubMed:26506309}.
CC -!- TISSUE SPECIFICITY: Expressed weakly in sperm, but more predominantly
CC in oocytes (PubMed:18472420). Expressed in the intestine
CC (PubMed:24843160). {ECO:0000269|PubMed:18472420,
CC ECO:0000269|PubMed:24843160}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (PubMed:18385514,
CC PubMed:20116245, PubMed:26506309). Transiently expressed during
CC cytokinesis in embryos on the ingressing furrow and at the midbody
CC during early abscission (PubMed:20116245). Expressed during the L4
CC stage and young adult stage of development (PubMed:22634595).
CC {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:20116245,
CC ECO:0000269|PubMed:22634595, ECO:0000269|PubMed:26506309}.
CC -!- DISRUPTION PHENOTYPE: Zygotic lethal (PubMed:18765566). RNAi-mediated
CC knockdown results in a reduced meiotic maturation rate of oocytes
CC (PubMed:18472420). Embryos are multinucleated and osmotically sensitive
CC with permeable and therefore defective eggshells (PubMed:18765566,
CC PubMed:18385514). During the first cell cycle, 52% of embryos fail to
CC extrude polar bodies, 83% of embryos display no or minimal
CC pseudocleavage and the centrosomal-nuclear complex does not migrate to
CC the center of embryos (PubMed:18385514). Animals display mitotic
CC spindle alignment defects whereby in 73.9% of embryos, the P0 spindle
CC does not rotate to the anterior-posterior axis of the embryo during
CC anaphase, but during the metaphase to anaphase transition, the
CC movements of the spindle are more abrupt with the spindle migrating to
CC the posterior pole and then rebounding to the anterior-posterior axis
CC (PubMed:18385514). In 17.4% of embryos the centrosomes are unstable and
CC the spindle is displaced further towards the posterior pole
CC (PubMed:18385514). Impaired localization of proteins important for
CC establishing cell polarity such as par-2, par-3, gpr-1 and gpr-2
CC (PubMed:18385514). Altered microtubule organization and dynamics during
CC metaphase including a greater distance between the growing microtubule
CC plus ends and the posterior cortex, impeded microtubule growth with
CC fewer growing astral microtubules reaching the cortex, and a reduced
CC microtubule nucleation rate (PubMed:18385514). Slight defect in
CC endoplasmic reticulum morphology whereby the large endoplasmic
CC reticulum aggregates that normally form during metaphase and persist
CC during anaphase, form, but do not persist during anaphase and disperse
CC (PubMed:18385514). Mild endocytosis defect with an accumulation of the
CC yolk protein vitellogenin in the pseudocoelom (PubMed:18354496).
CC Impaired cortical granule (secretory vesicle) localization with
CC granules abnormally clustered around the nuclear envelope of proximal
CC oocytes, irregulary dispersed in the cytoplasm of oocytes and retained
CC in the embryo following entry into the uterus (PubMed:18765566).
CC Cortical granule exocytosis defects whereby cav-1-positive cortical
CC granules are not tethered to the plasma membrane, but are distributed
CC throughout the cytoplasm and accumulate around the nucleus in embryos
CC following fertilization (PubMed:22992455). Disrupted fusion of spores,
CC containing intracellular pathogen N.parisii, with the apical cell
CC membrane and thus disrupted clearance from intestinal cells
CC (PubMed:24843160). RNAi-mediated knockdown in RNAi-sensitive mutants
CC exposed to bacterial pore-forming toxin Cry5B results in intoxification
CC and impaired plasma membrane repair (PubMed:21320697). RNAi-mediated
CC knockdown in the intestine results in reduced survival upon exposure to
CC Cry5B (PubMed:21320697). {ECO:0000269|PubMed:18354496,
CC ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:18472420,
CC ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:21320697,
CC ECO:0000269|PubMed:22992455, ECO:0000269|PubMed:24843160}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000255|RuleBase:RU003315}.
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DR EMBL; JQ235189; AFP33153.1; -; mRNA.
DR EMBL; BX284601; CCD71701.1; -; Genomic_DNA.
DR PIR; T29035; T29035.
DR RefSeq; NP_490675.1; NM_058274.3.
DR AlphaFoldDB; O01803; -.
DR SMR; O01803; -.
DR DIP; DIP-24288N; -.
DR IntAct; O01803; 1.
DR STRING; 6239.F53G12.1.1; -.
DR EPD; O01803; -.
DR PaxDb; O01803; -.
DR PeptideAtlas; O01803; -.
DR EnsemblMetazoa; F53G12.1.1; F53G12.1.1; WBGene00004274.
DR GeneID; 171601; -.
DR KEGG; cel:CELE_F53G12.1; -.
DR UCSC; F53G12.1; c. elegans.
DR CTD; 171601; -.
DR WormBase; F53G12.1; CE11006; WBGene00004274; rab-11.1.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000161659; -.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; O01803; -.
DR OMA; SMKEDYY; -.
DR OrthoDB; 1133775at2759; -.
DR PhylomeDB; O01803; -.
DR Reactome; R-CEL-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-CEL-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-CEL-8854214; TBC/RABGAPs.
DR Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR PRO; PR:O01803; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004274; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990676; C:Golgi trans cisterna membrane; IDA:WormBase.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IDA:WormBase.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060471; P:cortical granule exocytosis; IMP:WormBase.
DR GO; GO:0030703; P:eggshell formation; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0061796; P:membrane addition at site of mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 Cell membrane; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..211
FT /note="Ras-related protein rab-11.1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435682"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 18..26
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 LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62491"
SQ SEQUENCE 211 AA; 23429 MW; B0FD2837E42BE574 CRC64;
MGSRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSISVEGKTV
KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHVTYE NVERWLKELR DHADQNIVIM
LVGNKSDLRH LRAVPTDEAK IYAERNQLSF IETSALDSTN VEAAFTNILT EIYKSVSNKH
VGTDRQGYGG GSGTIIPSPA SDPPKKQCCI P
