VPS11_CAEEL
ID VPS11_CAEEL Reviewed; 980 AA.
AC Q09600;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Vacuolar protein sorting-associated protein 11 homolog;
GN Name=vps-11 {ECO:0000312|WormBase:R06F6.2};
GN ORFNames=R06F6.2 {ECO:0000312|WormBase:R06F6.2};
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=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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18923146; DOI=10.1091/mbc.e08-04-0441;
RA Xiao H., Chen D., Fang Z., Xu J., Sun X., Song S., Liu J., Yang C.;
RT "Lysosome biogenesis mediated by vps-18 affects apoptotic cell degradation
RT in Caenorhabditis elegans.";
RL Mol. Biol. Cell 20:21-32(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24501423; DOI=10.1091/mbc.e13-09-0521;
RA Delahaye J.L., Foster O.K., Vine A., Saxton D.S., Curtin T.P., Somhegyi H.,
RA Salesky R., Hermann G.J.;
RT "Caenorhabditis elegans HOPS and CCZ-1 mediate trafficking to lysosome-
RT related organelles independently of RAB-7 and SAND-1.";
RL Mol. Biol. Cell 25:1073-1096(2014).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25273556; DOI=10.1091/mbc.e13-12-0710;
RA Solinger J.A., Spang A.;
RT "Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a
RT block in endosome maturation in Caenorhabditis elegans.";
RL Mol. Biol. Cell 25:3909-3925(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26783301; DOI=10.1083/jcb.201506081;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Negative regulation of phosphatidylinositol 3-phosphate levels in early-
RT to-late endosome conversion.";
RL J. Cell Biol. 212:181-198(2016).
RN [7]
RP ERRATUM OF PUBMED:26783301.
RX PubMed=26975852; DOI=10.1083/jcb.20150608103012016c;
RA Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y., Xu J.,
RA Jing Y., Mitani S., He S., Yang C.;
RT "Correction: Negative regulation of phosphatidylinositol 3-phosphate levels
RT in early-to-late endosome conversion.";
RL J. Cell Biol. 212:739-739(2016).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport
CC pathways (PubMed:26783301). Believed to act as a core component of the
CC putative HOPS and CORVET endosomal tethering complexes which are
CC proposed to be involved in the rab-5-to-rab-7 endosome conversion
CC probably implicating sand-1, and via binding SNAREs and SNARE complexes
CC to mediate tethering and docking events during SNARE-mediated membrane
CC fusion (By similarity). The HOPS complex is proposed to be recruited to
CC Rab7 on the late endosomal membrane and to regulate late endocytic,
CC phagocytic and autophagic traffic towards lysosomes (By similarity).
CC Within the HOPS complex, contributes to the normal development of gut
CC granules in embryonic and adult intestinal cells (PubMed:24501423,
CC PubMed:25273556). The CORVET complex is proposed to function as a Rab5
CC effector to mediate early endosome fusion probably in specific endosome
CC subpopulations (By similarity). Required for fusion of endosomes and
CC autophagosomes with lysosomes (PubMed:25273556). Involved in cargo
CC transport from early to late endosomes and required for the transition
CC from early to late endosomes (By similarity). Possibly has a role in
CC clearance of apoptotic cells during programmed cell death
CC (PubMed:18425118, PubMed:18923146). {ECO:0000250|UniProtKB:Q9H270,
CC ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:18923146,
CC ECO:0000269|PubMed:24501423, ECO:0000269|PubMed:25273556,
CC ECO:0000269|PubMed:26783301}.
CC -!- SUBUNIT: Probable core component of at least two putative endosomal
CC tethering complexes, the homotypic fusion and vacuole protein sorting
CC (HOPS) complex and the class C core vacuole/endosome tethering (CORVET)
CC complex. Their common core is composed of the class C Vps proteins vps-
CC 11, vps-16 and vps-18, which in HOPS further associates with vps-33.1,
CC vps-39 and vps-41 and in CORVET with vps-8 and vps-33.2.
CC {ECO:0000250|UniProtKB:Q9H270}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H270}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H270}.
CC -!- DISRUPTION PHENOTYPE: Increased numbers of germ cell corpses
CC (PubMed:18425118, PubMed:18923146). Reduced number of gut granules in
CC the adult intestine (PubMed:24501423). Endosome/lysosome fusion defects
CC in coelomocytes (PubMed:26783301). Double knockout with either sorf-1
CC or sorf-2 results in larger endosomes and larger lysosomes and thus
CC suppresses the endosome/lysosome fusion defects in coelomocytes in the
CC vps-11 single mutant (PubMed:26783301). RNAi-mediated knockdown results
CC in a reduced number of gut granules in embryonic intestinal cells
CC (PubMed:24501423). RNAi-mediated knockdown results in defective
CC endosome maturation with the accumulation of small vesicles near the
CC gut lumen and large endosomes/lysosomes on the basal side of the cell
CC (PubMed:25273556). {ECO:0000269|PubMed:18425118,
CC ECO:0000269|PubMed:18923146, ECO:0000269|PubMed:24501423,
CC ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:26783301}.
CC -!- SIMILARITY: Belongs to the VPS11 family. {ECO:0000305}.
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DR EMBL; Z46794; CAA86774.2; -; Genomic_DNA.
DR PIR; T23975; T23975.
DR RefSeq; NP_496322.2; NM_063921.4.
DR AlphaFoldDB; Q09600; -.
DR BioGRID; 39974; 4.
DR ComplexPortal; CPX-1136; HOPS complex.
DR ComplexPortal; CPX-1137; CORVET complex.
DR STRING; 6239.R06F6.2; -.
DR EPD; Q09600; -.
DR PaxDb; Q09600; -.
DR PeptideAtlas; Q09600; -.
DR EnsemblMetazoa; R06F6.2.1; R06F6.2.1; WBGene00011067.
DR GeneID; 174661; -.
DR KEGG; cel:CELE_R06F6.2; -.
DR UCSC; R06F6.2; c. elegans.
DR CTD; 174661; -.
DR WormBase; R06F6.2; CE43323; WBGene00011067; vps-11.
DR eggNOG; KOG2114; Eukaryota.
DR GeneTree; ENSGT00940000153635; -.
DR HOGENOM; CLU_001287_0_1_1; -.
DR InParanoid; Q09600; -.
DR OMA; MRPQSTM; -.
DR OrthoDB; 429638at2759; -.
DR PhylomeDB; Q09600; -.
DR PRO; PR:Q09600; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011067; Expressed in adult organism and 5 other tissues.
DR GO; GO:0033263; C:CORVET complex; IC:ComplexPortal.
DR GO; GO:0031901; C:early endosome membrane; IC:ComplexPortal.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0030897; C:HOPS complex; ISS:WormBase.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IC:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IC:ComplexPortal.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR016528; VPS11.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323:SF24; PTHR23323:SF24; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR PIRSF; PIRSF007860; VPS11; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endosome; Lysosome; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..980
FT /note="Vacuolar protein sorting-associated protein 11
FT homolog"
FT /id="PRO_0000056326"
FT REPEAT 407..554
FT /note="CHCR"
FT ZN_FING 803..843
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 886..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 112009 MW; 9397243BFB2D9BD8 CRC64;
MTEFGWRRFN FFDRSVVFDK DDPKQKFMGL KDVAVDCWCS SGGSVYLGEA KGGVFQLTNQ
FSEYYWKAYQ KSLASLHSAD KYLFSIGEDD ETVNTLLKIW DPERVEKNTP HVMRTIRMSP
LNPTSSSPAC SIAVHSSLQS VVVGYTDGTV LFYQGDVLHD KSLNSRWIKV RDSSVGEGSV
TGLAIAVLPA SKTVVFVITQ KHVHSYVLEN GRTVIAHKKH DANGATADCW TFDESTGQLI
VASREMLFFY DADQCIDMDG GEVGRCLQLG RGHEKLQLVA SGQYLALLTK HHSLIQKERD
SEFMTMLSVY DIKGQYVGFS CSLPNLCRLF IAGSTMLVLS HDGLLSELIE KNLATKLDIL
VKKSMFDVAV LIAKNSRDGG DYLKGIHAKY GNYLYGKGDY ENAIQQYKET IGMLEPSYVM
KRYLDSSKIK ELCIYLECLH DAKRDNEHQT KILMNAYAKQ GEKKKLMEFV NKITDGTRVS
RMRDVFEILL KWNYLAEASL LATKFQMHED ALNVIIHHMH KYTMGVTYIS KMPIESVIEM
TGKFGRDLLI HARDDLMHML WEKIQENTDA KKNNFMRIFD IFMGDMDASR VFLSYIENQT
NEHDEFIIPI LECQMRLFKV NSDWSQERLE EDIYRFINKK NEDAALQMAQ LFDCTPVIEH
ILMRCHKSKE LMMYHQKKRD LEAIIRLCQS CSKEEKRRLW LDALSFIGKH ATARDELIII
DLLKEIEASE QIHPLVVLEL LAKNEHLTIS SVRDYIIAWL RKQQIIIEED RNTIKENNKA
MGELDGTVES LKFNAQIMQV TKCSACDTPL QLPTVHFLCK HAYHVHCFES YNMDGSDKCP
ACQTTRDTTR DEEISYHKFQ KELAEASNGM ELIAMYLQRG LFDEKTKKTK KSEAKKDPFS
TGRASTTTNP FDDDEVTTIS RTMSTVSSNM ATPSRQRSIT RKDDDSTNPF FNSDSGTRLS
TYDESKNPFG APAPSTNPFD
