RAB6A_CAEEL
ID RAB6A_CAEEL Reviewed; 205 AA.
AC P34213;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ras-related protein rab-6.1;
GN Name=rab-6.1 {ECO:0000312|WormBase:F59B2.7};
GN ORFNames=F59B2.7 {ECO:0000312|WormBase:F59B2.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP INTERACTION WITH VPS-52, AND SUBCELLULAR LOCATION.
RX PubMed=21613545; DOI=10.1091/mbc.e10-06-0493;
RA Luo L., Hannemann M., Koenig S., Hegermann J., Ailion M., Cho M.K.,
RA Sasidharan N., Zweckstetter M., Rensing S.A., Eimer S.;
RT "The Caenorhabditis elegans GARP complex contains the conserved Vps51
RT subunit and is required to maintain lysosomal morphology.";
RL Mol. Biol. Cell 22:2564-2578(2011).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP THR-25 AND GLN-70.
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF THR-25.
RX PubMed=26891225; DOI=10.1371/journal.pone.0149314;
RA Zhang D., Dubey J., Koushika S.P., Rongo C.;
RT "RAB-6.1 and RAB-6.2 Promote Retrograde Transport in C. elegans.";
RL PLoS ONE 11:e0149314-e0149314(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33826611; DOI=10.1371/journal.pgen.1009511;
RA Michaud P., Shah V.N., Adjibade P., Houle F., Quevillon Huberdeau M.,
RA Rioux R., Lavoie-Ouellet C., Gu W., Mazroui R., Simard M.J.;
RT "The RabGAP TBC-11 controls Argonaute localization for proper microRNA
RT function in C. elegans.";
RL PLoS Genet. 17:e1009511-e1009511(2021).
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:22992455, PubMed:26891225). 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:22992455, PubMed:26891225). In its active GTP-bound
CC form, acts redundantly with rab-6.2 (in its active GTP-bound form) to
CC positively regulate the retrograde trafficking of cargo molecules from
CC endosomes to Golgi structures (PubMed:26891225). Required for the
CC retrograde trafficking of glr-1, a subunit of AMPA-type glutamate
CC receptors (AMPRs), out of early endosomes and into the Golgi
CC compartment in neurons (PubMed:26891225). Together with rab-6.2,
CC promotes the retrograde trafficking of mig-14 from endosomes to Golgi
CC structures in the intestine (PubMed:26891225). In oocytes, in its
CC active GTP-bound form, involved in the membrane fusion and exocytosis
CC of secretory vesicles (cortical granules) to play a role in the
CC remodeling of the embryo surface following fertilization
CC (PubMed:22992455). Recruits sep-1 to cortical granules (derived from
CC the Golgi complex) for exocytosis during the oocyte-to-embryo
CC transition (PubMed:22992455). Required for seam cell division and alae
CC formation (PubMed:33826611). Promotes spontaneous reversals in
CC locomotion (PubMed:26891225). {ECO:0000269|PubMed:22992455,
CC ECO:0000269|PubMed:26891225, ECO:0000269|PubMed:33826611}.
CC -!- SUBUNIT: Interacts with GARP complex component vps-52.
CC {ECO:0000269|PubMed:21613545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22992455};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
CC projection, dendrite {ECO:0000269|PubMed:26891225}. Perikaryon
CC {ECO:0000269|PubMed:26891225}. Golgi apparatus
CC {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:26891225}. Cytoplasmic
CC vesicle, secretory vesicle {ECO:0000269|PubMed:22992455}.
CC Note=Following fertilization, localizes to cav-1-positive vesicles
CC tethered to the plasma membrane (PubMed:22992455). Localization becomes
CC dispersed throughout the cytoplasm once the vesicles fuse with the
CC plasma membrane during meiotic anaphase I (PubMed:22992455).
CC Temporarily co-localizes with sep-1 in the cortical granules prior to
CC membrane fusion (PubMed:22992455). Co-localizes with rab-11.1-positive
CC vesicles near the plasma membrane until vesicle exocytosis in embryos
CC (PubMed:22992455). Co-localizes with rab-6.2 at vesicular structures
CC throughout the oocyte cytoplasm (PubMed:22992455). Co-localizes with
CC rab-6.2 in neuronal cell bodies and dendrites and in Golgi structures
CC in neurons and the intestine (PubMed:26891225). Co-localizes with vps-
CC 52 at Golgi structures (PubMed:21613545). {ECO:0000269|PubMed:21613545,
CC ECO:0000269|PubMed:22992455, ECO:0000269|PubMed:26891225}.
CC -!- TISSUE SPECIFICITY: Highly expressed in body wall muscle, intestine,
CC somatic gonad, distal tip cells, vulva, and neurons including AVB, AVD,
CC RIG, and PVC (at protein level) (PubMed:26891225). Not expressed in AVA
CC and RMDV neurons (PubMed:26891225). {ECO:0000269|PubMed:26891225}.
CC -!- DISRUPTION PHENOTYPE: Sterile with fertilized embryos failing to
CC develop in the gonad (PubMed:26891225, PubMed:22992455). This may be
CC due to cytokinesis defects in embryos and increased permeability of the
CC embryonic surface to exogenous small molecules (PubMed:22992455).
CC Furthermore, the exocytosis of cortical granules following
CC fertilization is delayed and only partially occurs (PubMed:22992455).
CC Another study suggested that sterility may be due to abnormalities in
CC the hermaphrodite sperm (PubMed:26891225). Lowers rate of spontaneous
CC reversals in locomotion (PubMed:26891225). Decreases the number of mig-
CC 14-positive puncta in the intestine and results in mig-14 accumulation
CC in early endosome, late endosome and lysosome structures which are
CC adjacent to Golgi structures (PubMed:26891225). Decreases the number of
CC glr-1-positive puncta along the ventral nerve cord, indicative of
CC defective glr-1 trafficking (PubMed:26891225). RNAi-mediated knockdown
CC results in cytokinesis defects in embryos and increases the
CC permeability of the embryonic surface to exogenous small molecules
CC (PubMed:22992455). RNAi-mediated knockdown impairs incorporation of
CC cav-1 into the cytoplasm of cortical granules and abolishes the
CC recruitment of sep-1 to cortical granules in embryos resulting in
CC defective exocytosis of cortical granules following fertilization
CC (PubMed:22992455). RNAi-mediated knockdown results in the accumulation
CC of unsecreted cav-1-positive cortical granules near the plasma membrane
CC of the embryo following fertilization (PubMed:22992455). RNAi-mediated
CC knockdown disrupts seam cell division and alae formation
CC (PubMed:33826611). RNAi-mediated knockdown suppresses the seam cell
CC division and alae formation defects in the tbc-11 ok2576 mutant
CC (PubMed:33826611). RNAi-mediated knockdown in glr-1 expressing neurons
CC further reduces the number of glr-1-positive puncta in a rab-6.2 tm2254
CC mutant background (PubMed:26891225). {ECO:0000269|PubMed:22992455,
CC ECO:0000269|PubMed:26891225, ECO:0000269|PubMed:33826611}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CAA77590.1; -; Genomic_DNA.
DR PIR; S31127; S31127.
DR RefSeq; NP_498993.1; NM_066592.4.
DR AlphaFoldDB; P34213; -.
DR SMR; P34213; -.
DR BioGRID; 41474; 1.
DR IntAct; P34213; 1.
DR STRING; 6239.F59B2.7; -.
DR EPD; P34213; -.
DR PaxDb; P34213; -.
DR EnsemblMetazoa; F59B2.7.1; F59B2.7.1; WBGene00004269.
DR GeneID; 176275; -.
DR KEGG; cel:CELE_F59B2.7; -.
DR UCSC; F59B2.7.1; c. elegans.
DR CTD; 176275; -.
DR WormBase; F59B2.7; CE00234; WBGene00004269; rab-6.1.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000154769; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P34213; -.
DR OMA; PNIVIMN; -.
DR OrthoDB; 1277051at2759; -.
DR PhylomeDB; P34213; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-CEL-6811438; Intra-Golgi traffic.
DR Reactome; R-CEL-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-CEL-8854214; TBC/RABGAPs.
DR Reactome; R-CEL-8873719; RAB geranylgeranylation.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P34213; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004269; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0060473; C:cortical granule; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031985; C:Golgi cisterna; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060471; P:cortical granule exocytosis; IMP:WormBase.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; 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; Cell projection; Cytoplasmic vesicle; Golgi apparatus;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..205
FT /note="Ras-related protein rab-6.1"
FT /id="PRO_0000121118"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 25
FT /note="T->N: Constitutively inactive (GDP-locked form).
FT Diffusely localized. Fails to localize to the cortical
FT granules in oocytes. Does not recruit sep-1 to cortical
FT granules in embryos following fertilization. In glr-1
FT expressing neurons reduces the number of glr-1-positive
FT puncta in a rab-6.2 tm2254 mutant background."
FT /evidence="ECO:0000269|PubMed:22992455,
FT ECO:0000269|PubMed:26891225"
FT MUTAGEN 70
FT /note="Q->L: Constitutively active (GTP-locked form).
FT Localizes to the cortical granules in oocytes. Recruits
FT sep-1 to cortical granules in embryos following
FT fertilization."
FT /evidence="ECO:0000269|PubMed:22992455"
SQ SEQUENCE 205 AA; 23259 MW; A8A0876CF8E456C3 CRC64;
MADFTNNALK KFKLVFLGEQ SVGKTSIITR FMYDSFDNTY QATIGIDFLS KTMYLEDRTI
RLQLWDTAGQ ERFRSLIPSY IRDSSVAVVV YDITNANSFH QTTKWVDDVR NERGCDVIIV
LVGNKTDLAD KRQVSTEDGE KKARDLNVMF IETSAKAGYN VKQLFRKIAT ALPGIVQEET
PEQPNIVIMN PPKDAEESQG RQCPC
