VPS16_YEAST
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 03-AUG-2022, entry version 170.
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 component of the HOPS complex
CC that acts during the docking stage of vacuole fusion. HOPS is an
CC effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar
CC SNARE complex assembly. It remains bound to SNARE complexes after
CC 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 AlphaFoldDB; Q03308; -.
DR SMR; Q03308; -.
DR BioGRID; 36135; 63.
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; Q03308; -.
DR PRIDE; Q03308; -.
DR EnsemblFungi; YPL045W_mRNA; YPL045W; YPL045W.
DR GeneID; 856062; -.
DR KEGG; sce:YPL045W; -.
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 BioCyc; YEAST:G3O-33958-MON; -.
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: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; -; 1.
DR InterPro; IPR016534; VPS16.
DR InterPro; IPR006925; Vps16_C.
DR InterPro; IPR038132; Vps16_C_sf.
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 1: Evidence at protein level;
KW Cytoplasm; Protein transport; Reference proteome; Transport; 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
