ID   VPS16_CAEBR             Reviewed;         858 AA.
AC   Q60V75; A8XW56;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Vacuolar protein sorting-associated protein 16 homolog;
GN   Name=vps-16 {ECO:0000250|UniProtKB:Q11182}; ORFNames=CBG19671;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC       lysosomal compartments including the endocytic membrane transport
CC       pathways. Believed to act as a core component of the putative HOPS and
CC       CORVET endosomal tethering complexes which are proposed to be involved
CC       in the rab-5-to-rab-7 endosome conversion probably implicating sand-1,
CC       and via binding SNAREs and SNARE complexes to mediate tethering and
CC       docking events during SNARE-mediated membrane fusion. The HOPS complex
CC       is proposed to be recruited to rab-7 on the late endosomal membrane and
CC       to regulate late endocytic, phagocytic and autophagic traffic towards
CC       lysosomes. Within the HOPS complex, contributes to the normal
CC       development of gut granules in the adult intestine. The CORVET complex
CC       is proposed to function as a rab-5 effector to mediate early endosome
CC       fusion probably in specific endosome subpopulations. Required for
CC       recruitment of vps-33.1 to the HOPS complex. Required for fusion of
CC       endosomes and autophagosomes with lysosomes; the function is dependent
CC       on its association with vps-33.1 but not vps-33.2.
CC       {ECO:0000250|UniProtKB:Q11182, ECO:0000250|UniProtKB:Q9H269}.
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   -!- SIMILARITY: Belongs to the VPS16 family. {ECO:0000255}.
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DR   EMBL; HE600934; CAP36875.1; -; Genomic_DNA.
DR   RefSeq; XP_002634685.1; XM_002634639.1.
DR   AlphaFoldDB; Q60V75; -.
DR   SMR; Q60V75; -.
DR   STRING; 6238.CBG19671; -.
DR   GeneID; 8576678; -.
DR   KEGG; cbr:CBG_19671; -.
DR   CTD; 8576678; -.
DR   WormBase; CBG19671; CBP41531; WBGene00038846; Cbr-vps-16.
DR   eggNOG; KOG2280; Eukaryota.
DR   HOGENOM; CLU_335015_0_0_1; -.
DR   InParanoid; Q60V75; -.
DR   OMA; YVTFWYP; -.
DR   OrthoDB; 1258856at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IBA:GO_Central.
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..858
FT                   /note="Vacuolar protein sorting-associated protein 16
FT                   homolog"
FT                   /id="PRO_0000278179"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  96378 MW;  80BB84F7F32A6291 CRC64;
     MKESTRTSTP SSGAKPKGDR EICLRPSSSV FLGDQQLYFT QEYLATNSLN MKYVVYFAAC
     QFSGPIAVIY AAPKSWFIWI RTISGRILKR DLPCTDPVFI DWTRAHCLLV LSKNGRAQVL
     SSIGEKVSEV FFDNQVSDVH ECRTFATSRG DSGIAVMDVD GQVAVVNSVS EPVIWSMRPP
     YSELPTAWTA FQPHSQLTHI LLIFEAVFLM GCQGESLQVQ NHASVWVDSS TKYVKCVVDD
     ARSRIAMMTE NGKIQIVSID LSTCFCTVEV TEHEIGKCIN FGWVGNSVVF VQMSSSLTVF
     VNVSARRKPG DEVRFMSIKM TANARISVEP DGIRLFESTR VEFVEAASRE KIAVLNRSLN
     EDGAYLYKAA QEMEQGTGHN SFAASTVIQD MYKAIDDCIS TACDTWQPEE QKLLLKAARF
     GMAYTNTTPD TTKLMRAIKE IRVLNELRMV RTGIPLTHRQ YRIIGDTCII NRLIDMGSYS
     VAIKVAQWLG GENCESVDRV LLEWVRRSIS KVSRSNMKMD QPALEALDEK ISAKLLQFPH
     VSMADAARRA IEAKLPELAR LFIRRETDDE SHVAVLLQLN DVSAALTKAA ASQRPQLIHQ
     VVRHLMTSES RSSYELAISR IPLAQCLYQD LVRQEGETRG ISSRQMLALL EQASDFERQT
     LFHFDVAEIE RNPSERLNAL RRAKDAAKSM GDKAIEEILN DVSAFAPLQI QRGQADMSVR
     DTIIEIADDT AKVAQLKQQA RLNDKQVLLW TIEGLAKKGK MEQLFDLAQK RSPIGYAPFV
     KACVRYKRNE EVNKYFAKAN GYSDLVAANL AKKNYVDAAK LAYDRRDREV LHAIHMKSHD
     DPVQCPRVKQ LLNSMDQA