VAC17_YEAST
ID VAC17_YEAST Reviewed; 423 AA.
AC P25591; D6VQV5; P25590;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=vacuole-related protein 17;
DE AltName: Full=Vacuole-specific MYO2 receptor VAC17;
GN Name=VAC17; OrderedLocusNames=YCL063W; ORFNames=YCL63W/YCL62W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, AND INTERACTION WITH MYO2 AND VAC8.
RX PubMed=12642614; DOI=10.1083/jcb.200210139;
RA Ishikawa K., Catlett N.L., Novak J.L., Tang F., Nau J.J., Weisman L.S.;
RT "Identification of an organelle-specific myosin V receptor.";
RL J. Cell Biol. 160:887-897(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAINS, AND INTERACTION WITH MYO2 AND
RP VAC8.
RX PubMed=12594460; DOI=10.1038/nature01453;
RA Tang F., Kauffman E.J., Novak J.L., Nau J.J., Catlett N.L., Weisman L.S.;
RT "Regulated degradation of a class V myosin receptor directs movement of the
RT yeast vacuole.";
RL Nature 422:87-92(2003).
RN [6]
RP INTERACTION WITH MYO2.
RX PubMed=15821138; DOI=10.1128/ec.4.4.787-798.2005;
RA Pashkova N., Catlett N.L., Novak J.L., Weisman L.S.;
RT "A point mutation in the cargo-binding domain of myosin V affects its
RT interaction with multiple cargoes.";
RL Eukaryot. Cell 4:787-798(2005).
RN [7]
RP INTERACTION WITH MYO2.
RX PubMed=15684027; DOI=10.1083/jcb.200407146;
RA Pashkova N., Catlett N.L., Novak J.L., Wu G., Lu R., Cohen R.E.,
RA Weisman L.S.;
RT "Myosin V attachment to cargo requires the tight association of two
RT functional subdomains.";
RL J. Cell Biol. 168:359-364(2005).
RN [8]
RP INTERACTION WITH VAC8.
RX PubMed=16824055; DOI=10.1111/j.1600-0854.2006.00458.x;
RA Tang F., Peng Y., Nau J.J., Kauffman E.J., Weisman L.S.;
RT "Vac8p, an armadillo repeat protein, coordinates vacuole inheritance with
RT multiple vacuolar processes.";
RL Traffic 7:1368-1377(2006).
RN [9]
RP INTERACTION WITH ATG18.
RX PubMed=17699591; DOI=10.1091/mbc.e07-04-0301;
RA Efe J.A., Botelho R.J., Emr S.D.;
RT "Atg18 regulates organelle morphology and Fab1 kinase activity independent
RT of its membrane recruitment by phosphatidylinositol 3,5-bisphosphate.";
RL Mol. Biol. Cell 18:4232-4244(2007).
RN [10]
RP PHOSPHORYLATION AT SER-119; THR-149; SER-178 AND THR-248, INTERACTION WITH
RP MYO2, FUNCTION, AND MUTAGENESIS OF SER-119; THR-149; SER-178; PHE-225 AND
RP THR-248.
RX PubMed=18804442; DOI=10.1016/j.devcel.2008.07.007;
RA Peng Y., Weisman L.S.;
RT "The cyclin-dependent kinase Cdk1 directly regulates vacuole inheritance.";
RL Dev. Cell 15:478-485(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Vacuole-specific MYO2 receptor required for vacuole
CC inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar
CC membrane protein, forming a transport complex which moves the attached
CC vacuole membrane along actin cables into the bud. Once the vacuole
CC arrives in the bud, VAC17 is degraded, depositing the vacuole in its
CC correct location. {ECO:0000269|PubMed:12594460,
CC ECO:0000269|PubMed:12642614, ECO:0000269|PubMed:18804442}.
CC -!- SUBUNIT: Interacts with MYO2 and VAC8. Interacts with ATG18.
CC {ECO:0000269|PubMed:12594460, ECO:0000269|PubMed:12642614,
CC ECO:0000269|PubMed:15684027, ECO:0000269|PubMed:15821138,
CC ECO:0000269|PubMed:16824055, ECO:0000269|PubMed:17699591,
CC ECO:0000269|PubMed:18804442}.
CC -!- INTERACTION:
CC P25591; P19524: MYO2; NbExp=7; IntAct=EBI-21800, EBI-11659;
CC P25591; P39968: VAC8; NbExp=3; IntAct=EBI-21800, EBI-20212;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12594460};
CC Peripheral membrane protein {ECO:0000269|PubMed:12594460}; Cytoplasmic
CC side {ECO:0000269|PubMed:12594460}.
CC -!- SIMILARITY: Belongs to the VAC17 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42404.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07424.1; -; Genomic_DNA.
DR PIR; S74278; S74278.
DR RefSeq; NP_009870.1; NM_001178705.1.
DR AlphaFoldDB; P25591; -.
DR SMR; P25591; -.
DR BioGRID; 30925; 89.
DR ComplexPortal; CPX-1304; MYO2-VAC17-VAC8 transport complex.
DR DIP; DIP-2065N; -.
DR IntAct; P25591; 10.
DR MINT; P25591; -.
DR STRING; 4932.YCL063W; -.
DR iPTMnet; P25591; -.
DR PaxDb; P25591; -.
DR PRIDE; P25591; -.
DR EnsemblFungi; YCL063W_mRNA; YCL063W; YCL063W.
DR GeneID; 850296; -.
DR KEGG; sce:YCL063W; -.
DR SGD; S000000568; VAC17.
DR VEuPathDB; FungiDB:YCL063W; -.
DR eggNOG; ENOG502RZF2; Eukaryota.
DR HOGENOM; CLU_571186_0_0_1; -.
DR InParanoid; P25591; -.
DR OMA; LQLDLWI; -.
DR BioCyc; YEAST:G3O-29312-MON; -.
DR PRO; PR:P25591; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25591; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0071563; C:Myo2p-Vac17p-Vac8p transport complex; IPI:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IPI:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IDA:ComplexPortal.
DR InterPro; IPR035293; Vac17.
DR Pfam; PF17321; Vac17; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..423
FT /note="vacuole-related protein 17"
FT /id="PRO_0000202554"
FT REGION 109..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..170
FT /note="MYO2-binding"
FT REGION 150..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..380
FT /note="VAC8-binding"
FT COMPBIAS 112..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18804442"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18804442"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18804442"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18804442"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 119
FT /note="S->A: Impairs phosphorylation; when associated with
FT A-149; A-178 and A-248."
FT /evidence="ECO:0000269|PubMed:18804442"
FT MUTAGEN 149
FT /note="T->A: Impairs phosphorylation; when associated with
FT A-119; A-178 and A-248."
FT /evidence="ECO:0000269|PubMed:18804442"
FT MUTAGEN 178
FT /note="S->A: Impairs phosphorylation; when associated with
FT A-119; A-149 and A-248."
FT /evidence="ECO:0000269|PubMed:18804442"
FT MUTAGEN 225
FT /note="F->S: Stabilizes VAC17 whose protein levels are
FT about 10-fold higher than wild-type."
FT /evidence="ECO:0000269|PubMed:18804442"
FT MUTAGEN 248
FT /note="T->A: Impairs phosphorylation; when associated with
FT A-119; A-149 and A-178."
FT /evidence="ECO:0000269|PubMed:18804442"
SQ SEQUENCE 423 AA; 47843 MW; 7F14A3A0BFE9571B CRC64;
MATQALEDIT ERLLIRSQEA ILQLDLWIQR QQRSSICQTT DQESLDKLSQ QYNQYMSQLN
SLYVRSESVR DKLSKEQQRR LITEDNEHQR IEDLVREFQD ITLRLNELAT VPNEAPNDSP
QSQSTRSSLG SFQPRPLKII ERQRLCMVTP SKPPKKSVGF NPINEVDCPS KTNSLPCSPK
KQPARNRTLR AAKSHDTGLN KSKKPSSSDT YESFFKNRQR LSLTFFDEMD DEDFDSDQDT
IILPNISTPP HVGVTAKGAE FEPLRRYNSH ESILSNKPAP SKSLNLGSFS ASFFRPSNPT
FGTSISNVQV NCHPTVAATM APSRNGPRIS SSKALLSSFI ARSDTHTVKE NNTNLKHASF
MDKFNSSLST ISESFQSKRG RKNKGMNEER ISNHNVAQEQ KNNMDISVSI EELQDALNTE
LLF
