VPS16_CAEEL
ID VPS16_CAEEL Reviewed; 852 AA.
AC Q11182;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Vacuolar protein sorting-associated protein 16 homolog;
GN Name=vps-16 {ECO:0000312|WormBase:C05D11.2};
GN ORFNames=C05D11.2 {ECO:0000312|WormBase:C05D11.2};
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=15843430; DOI=10.1091/mbc.e05-01-0060;
RA Hermann G.J., Schroeder L.K., Hieb C.A., Kershner A.M., Rabbitts B.M.,
RA Fonarev P., Grant B.D., Priess J.R.;
RT "Genetic analysis of lysosomal trafficking in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:3273-3288(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 rab-7 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 the adult intestine (PubMed:15843430, PubMed:24501423,
CC PubMed:25273556). The CORVET complex is proposed to function as a rab-5
CC effector to mediate early endosome fusion probably in specific endosome
CC subpopulations (By similarity). Required for recruitment of vps-33.1 to
CC the HOPS complex (By similarity). Required for fusion of endosomes and
CC autophagosomes with lysosomes; the function is dependent on its
CC association with vps-33.1 but not vps-33.2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H269, ECO:0000269|PubMed:15843430,
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:Q9H269}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H269}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9H269}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H269}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H269}. Note=Cytoplasmic, peripheral membrane
CC protein associated with late endosomes/lysosomes.
CC {ECO:0000250|UniProtKB:Q9H269}.
CC -!- DISRUPTION PHENOTYPE: Viable with a reduced number of gut granules in
CC the adult intestine (PubMed:15843430, PubMed:24501423). Embryos of
CC these adults arrest in early development and lack gut granules
CC (PubMed:15843430). Endosome/lysosome fusion defects in coelomocytes
CC (PubMed:26783301). RNAi-mediated knockdown results in a reduced number
CC of gut granules in embryonic intestinal cells (PubMed:24501423). RNAi-
CC mediated knockdown results in defective endosome maturation with the
CC accumulation of small vesicles near the gut lumen and large
CC endosomes/lysosomes on the basal side of the cell (PubMed:25273556).
CC {ECO:0000269|PubMed:15843430, ECO:0000269|PubMed:24501423,
CC ECO:0000269|PubMed:25273556, ECO:0000269|PubMed:26783301}.
CC -!- SIMILARITY: Belongs to the VPS16 family. {ECO:0000305}.
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DR EMBL; FO080365; CCD63191.1; -; Genomic_DNA.
DR PIR; H88482; H88482.
DR RefSeq; NP_498411.1; NM_066010.3.
DR AlphaFoldDB; Q11182; -.
DR SMR; Q11182; -.
DR BioGRID; 41131; 4.
DR ComplexPortal; CPX-1136; HOPS complex.
DR ComplexPortal; CPX-1137; CORVET complex.
DR STRING; 6239.C05D11.2; -.
DR EPD; Q11182; -.
DR PaxDb; Q11182; -.
DR PeptideAtlas; Q11182; -.
DR EnsemblMetazoa; C05D11.2.1; C05D11.2.1; WBGene00006516.
DR GeneID; 175913; -.
DR KEGG; cel:CELE_C05D11.2; -.
DR UCSC; C05D11.2.1; c. elegans.
DR CTD; 175913; -.
DR WormBase; C05D11.2; CE24785; WBGene00006516; vps-16.
DR eggNOG; KOG2280; Eukaryota.
DR GeneTree; ENSGT00390000003896; -.
DR HOGENOM; CLU_335015_0_0_1; -.
DR InParanoid; Q11182; -.
DR OMA; YVTFWYP; -.
DR OrthoDB; 1258856at2759; -.
DR PhylomeDB; Q11182; -.
DR PRO; PR:Q11182; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006516; Expressed in germ line (C elegans) and 4 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; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IC:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IBA:GO_Central.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR016534; VPS16.
DR InterPro; IPR006925; Vps16_C.
DR InterPro; IPR006926; Vps16_N.
DR PANTHER; PTHR12811; PTHR12811; 1.
DR Pfam; PF04840; Vps16_C; 1.
DR Pfam; PF04841; Vps16_N; 1.
DR PIRSF; PIRSF007949; VPS16; 1.
PE 3: Inferred from homology;
KW Endosome; Lysosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..852
FT /note="Vacuolar protein sorting-associated protein 16
FT homolog"
FT /id="PRO_0000065147"
SQ SEQUENCE 852 AA; 95843 MW; 659BB5D773A7155C CRC64;
MGESHAPSKP KLDGELCLRP SSSVFLGDQQ LYFTQEYLRT NSLNLKYVVY FTACQFSGPI
AVAYSPRPAS WYIWIRTISG RILKRDMAFN EPVFMEWTRA HCLLVLNKAG RAHIFSSLGE
KISEVIFDSQ MSDVHECRTF ATSRGDSGIA VMDVDGQVSV VNSVSEPVIW SMKPPYSEMP
TAWTAFQPHS QLTHILLIFE AVFLMGCQGE SLREQSHAAS WVDSNTKYVK CVVDDARSRI
AMMTESGKIQ IVSIDLSTCF CTVEITDHDI AKCINFGWVG NSAVFVQMSP SLIVFVNVSA
RRKPGDEVQI YEKMTANAKI SIEPDGIRLF ESTQVEFVEA ASREKIAVLN RNPNEDGAHL
YKAAQEMSQG TGHNSFAAST VIQDLYKAID DCISTACDTW QPEEQKLLLK AARFGMAYTN
TTPDTTKLMR AIKEIRVLNE LRMVRTGIPL THRQFRAIGE TCVINRLIDM GSYSVAIKVA
QWLGGETSEN VDRVLLEWVR RSISKVSKSN MKMDQPALEA LDEKISAKLL QFPHVSIADA
ARRAIEAKLP ELARLFIRRE TDDANHVAVL LQLNDVSAAL QKASASQRPQ LIHQVVRHLM
NSESRSSYEL AISRIPLAQC LYQDLVRQEG ETRGASSRQM LALLEQASDF ERQTLFHFDV
AETERNPDER LNALRRAKDA AKSMGDKAIE EILNDVSAFA PLQIQRGQAD MSVRDTVIEM
AHDTAKVAQL KQQARLTDKQ VLLWTIEGLA KKGKMEQLFD LAQKRSPIGY APFVKACVRY
KRLDEIKKYF AKVNGYPDLV AAHLAMKNYV EAAKLAYDRR DRDVLHAVHM KSHEDPTQCP
RVGQFLRSLD QN
