ID   VPS16_YEAST             Reviewed;         798 AA.
AC   Q03308; D6W3W9; Q03078;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Vacuolar protein sorting-associated protein 16;
DE   AltName: Full=Vacuolar morphogenesis protein 9;
DE   AltName: Full=Vacuolar protein-targeting protein 16;
GN   Name=VPS16; Synonyms=VAM9, VPT16; OrderedLocusNames=YPL045W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444873; DOI=10.1016/s0021-9258(18)53488-8;
RA   Horazdovsky B.F., Emr S.D.;
RT   "The VPS16 gene product associates with a sedimentable protein complex and
RT   is essential for vacuolar protein sorting in yeast.";
RL   J. Biol. Chem. 268:4953-4962(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   IDENTIFICATION IN THE HOPS COMPLEX, FUNCTION OF THE HOPS COMPLEX, AND
RP   INTERACTION WITH VAM7.
RX   PubMed=16601699; DOI=10.1038/sj.emboj.7601051;
RA   Stroupe C., Collins K.M., Fratti R.A., Wickner W.;
RT   "Purification of active HOPS complex reveals its affinities for
RT   phosphoinositides and the SNARE Vam7p.";
RL   EMBO J. 25:1579-1589(2006).
CC   -!- FUNCTION: Essential for vacuolar protein sorting. Required for vacuole
CC       biogenesis, stability and to maintain vacuole morphology. Required for
CC       growth at elevated temperatures. Acts as a component of the HOPS
CC       complex that acts during the docking stage of vacuole fusion. HOPS is
CC       an effector for the vacuolar Rab GTPase YPT7 and is required for
CC       vacuolar SNARE complex assembly. It remains bound to SNARE complexes
CC       after vacuole fusion. {ECO:0000269|PubMed:16601699}.
CC   -!- SUBUNIT: Component of the HOPS complex which is composed of PEP5,
CC       VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with
CC       phosphoinositides and the PX domain of VAM7. Interacts with VAM7.
CC       {ECO:0000269|PubMed:16601699}.
CC   -!- INTERACTION:
CC       Q03308; P20795: VPS33; NbExp=5; IntAct=EBI-20355, EBI-20395;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Vacuole.
CC   -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VPS16 family. {ECO:0000305}.
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DR   EMBL; L07327; AAA35215.1; -; Genomic_DNA.
DR   EMBL; U44030; AAB68176.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11385.1; -; Genomic_DNA.
DR   PIR; S62031; S62031.
DR   RefSeq; NP_015280.1; NM_001183859.1.
DR   PDB; 7ZU0; EM; 4.40 A; B=1-798.
DR   PDBsum; 7ZU0; -.
DR   AlphaFoldDB; Q03308; -.
DR   EMDB; EMD-14964; -.
DR   EMDB; EMD-2280; -.
DR   SMR; Q03308; -.
DR   BioGRID; 36135; 66.
DR   ComplexPortal; CPX-1625; HOPS complex.
DR   ComplexPortal; CPX-1626; CORVET complex.
DR   DIP; DIP-6691N; -.
DR   IntAct; Q03308; 13.
DR   MINT; Q03308; -.
DR   STRING; 4932.YPL045W; -.
DR   MaxQB; Q03308; -.
DR   PaxDb; 4932-YPL045W; -.
DR   PeptideAtlas; Q03308; -.
DR   EnsemblFungi; YPL045W_mRNA; YPL045W; YPL045W.
DR   GeneID; 856062; -.
DR   KEGG; sce:YPL045W; -.
DR   AGR; SGD:S000005966; -.
DR   SGD; S000005966; VPS16.
DR   VEuPathDB; FungiDB:YPL045W; -.
DR   eggNOG; KOG2280; Eukaryota.
DR   GeneTree; ENSGT00390000003896; -.
DR   HOGENOM; CLU_008909_1_0_1; -.
DR   InParanoid; Q03308; -.
DR   OMA; YVTFWYP; -.
DR   OrthoDB; 1110811at2759; -.
DR   BioCyc; YEAST:G3O-33958-MONOMER; -.
DR   BioGRID-ORCS; 856062; 2 hits in 10 CRISPR screens.
DR   PRO; PR:Q03308; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q03308; Protein.
DR   GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0030897; C:HOPS complex; IPI:SGD.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; IDA:SGD.
DR   GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:ComplexPortal.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR   GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR   GO; GO:0099022; P:vesicle tethering; IDA:SGD.
DR   Gene3D; 1.10.150.780; Vps16, C-terminal region; 1.
DR   InterPro; IPR016534; VPS16.
DR   InterPro; IPR006925; Vps16_C.
DR   InterPro; IPR038132; Vps16_C_sf.
DR   InterPro; IPR006926; Vps16_N.
DR   PANTHER; PTHR12811; VACUOLAR PROTEIN SORTING VPS16; 1.
DR   PANTHER; PTHR12811:SF0; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 16 HOMOLOG; 1.
DR   Pfam; PF04840; Vps16_C; 1.
DR   Pfam; PF04841; Vps16_N; 1.
DR   PIRSF; PIRSF007949; VPS16; 1.
DR   SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Vacuole.
FT   CHAIN           1..798
FT                   /note="Vacuolar protein sorting-associated protein 16"
FT                   /id="PRO_0000065891"
FT   CONFLICT        100
FT                   /note="L -> R (in Ref. 1; AAA35215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="V -> I (in Ref. 1; AAA35215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326..340
FT                   /note="AIEILKNFVLEKGVL -> QLNIKEFCLREGCT (in Ref. 1;
FT                   AAA35215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   798 AA;  92741 MW;  6AE1ED43DB234137 CRC64;
     MKNPSFDWER LKDVFYRSRA IGELKWPTQY EEFKCALSLT VIAVEIQDFI QVYNYFGQLL
     GKINLQRIHE DIIKFEFDKD EKLILVTKSS IKIVKGWSPL TIESVPLQDP TIDTIWDYHN
     GIMLLAKSRD IYKLNGNEWE LLYENKDKKY NLLTKNHWSC NDDSIILLDV DHVYQVSTSN
     GALLKLITDS SWHKVTISSR GFICLYNMKD NKLQIFRDPA RILMEHNLDS TPDDICWCGN
     DTVACSFEDE IKLYGPDGLY VTFWYPFTVT NLRAEVDGLK VITTEKIYFL SRVQPQTSNI
     FRIGSTEPGA MLVDSFSLLE DHAPKAIEIL KNFVLEKGVL DCIAAAIDEF EPKLQKMLLN
     AASYGKASLQ YKSFDASIFV NACNTIKLLN CFRSFGIFLT VEEYRCISLK GVIDRLLKYH
     RYYECIQICK LANERFLLGY VFTEWAKDKI KGSPDMEDDE LLDKIKSRLS VIDMTDTLQM
     VAVAKVAYLE GRFQLSRNLA LLEKNEEARI EQLYNLDDDS IALKECIKVQ NYSLTISLLI
     ALSKKLTNSQ LTKLLIIDMF NNPLYLYYMR MDKAYLYDFY RQTDRFIDLA HVLLQQGKEQ
     QSLHSFLPQI KDLYSQVQNS EVVNNTIEQL QRQEKLWIYQ ESLGKRFAIS FTNMTLDQTL
     SKLIETGQDK QVKEIVKKFK ISEKKLYHLK CKTLVEAKKF DELLQFAQSR KSPIGYMPFY
     TYLKSRGHMD KASPYVNMIP GLSYQEKKKL YVECRGFRDA IQLAGKEKDI PGLKEIYNII
     PPNEPELKAL ANETMSRI
//