VAC8_YEAST
ID VAC8_YEAST Reviewed; 578 AA.
AC P39968; D3DLN6; Q549T0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Vacuolar protein 8;
GN Name=VAC8; Synonyms=YEB3; OrderedLocusNames=YEL013W;
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 [MRNA].
RA Fischer R.;
RT "New members of the plakoglobin/armadillo/beta-catenin family characterized
RT by armadillo repeats.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 FUNCTION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4; CYS-5 AND
RP CYS-7, MUTAGENESIS OF 4-CYS--CYS-7, AND SUBCELLULAR LOCATION.
RX PubMed=9490720; DOI=10.1083/jcb.140.5.1063;
RA Wang Y.-X., Catlett N.L., Weisman L.S.;
RT "Vac8p, a vacuolar protein with armadillo repeats, functions in both
RT vacuole inheritance and protein targeting from the cytoplasm to vacuole.";
RL J. Cell Biol. 140:1063-1074(1998).
RN [5]
RP PHOSPHORYLATION, AND INTERACTION WITH ATG13.
RX PubMed=10837477; DOI=10.1074/jbc.m002813200;
RA Scott S.V., Nice D.C. III, Nau J.J., Weisman L.S., Kamada Y.,
RA Keizer-Gunnink I., Funakoshi T., Veenhuis M., Ohsumi Y., Klionsky D.J.;
RT "Apg13p and Vac8p are part of a complex of phosphoproteins that are
RT required for cytoplasm to vacuole targeting.";
RL J. Biol. Chem. 275:25840-25849(2000).
RN [6]
RP PALMITOYLATION.
RX PubMed=11406591; DOI=10.1093/emboj/20.12.3145;
RA Veit M., Laage R., Dietrich L., Wang L., Ungermann C.;
RT "Vac8p release from the SNARE complex and its palmitoylation are coupled
RT and essential for vacuole fusion.";
RL EMBO J. 20:3145-3155(2001).
RN [7]
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 [8]
RP PALMITOYLATION.
RX PubMed=16186255; DOI=10.1083/jcb.200507048;
RA Smotrys J.E., Schoenfish M.J., Stutz M.A., Linder M.E.;
RT "The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for
RT Vac8p.";
RL J. Cell Biol. 170:1091-1099(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-16, AND
RP IDENTIFICATION BY 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77 AND LYS-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Functions in both vacuole inheritance and protein targeting
CC from the cytoplasm to vacuole. {ECO:0000269|PubMed:9490720}.
CC -!- INTERACTION:
CC P39968; Q06628: ATG13; NbExp=7; IntAct=EBI-20212, EBI-36188;
CC P39968; P38881: NVJ1; NbExp=10; IntAct=EBI-20212, EBI-24885;
CC P39968; P40003: VAB2; NbExp=3; IntAct=EBI-20212, EBI-22275;
CC P39968; P25591: VAC17; NbExp=3; IntAct=EBI-20212, EBI-21800;
CC P39968; P39968: VAC8; NbExp=2; IntAct=EBI-20212, EBI-20212;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:9490720};
CC Lipid-anchor {ECO:0000269|PubMed:9490720}.
CC -!- PTM: Palmitoylated on one or more of its N-terminal cysteine residues
CC by PFA3, which is required for vacuole fusion.
CC {ECO:0000269|PubMed:11406591, ECO:0000269|PubMed:16186255,
CC ECO:0000269|PubMed:9490720}.
CC -!- MISCELLANEOUS: Present with 5680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AF005267; AAQ13402.1; -; mRNA.
DR EMBL; U18530; AAB64490.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07640.1; -; Genomic_DNA.
DR PIR; S50446; S50446.
DR RefSeq; NP_010903.3; NM_001178828.3.
DR PDB; 5XJG; X-ray; 2.40 A; A/C=10-515.
DR PDB; 6KBM; X-ray; 2.90 A; A=10-515.
DR PDB; 6KBN; X-ray; 3.20 A; A/C=1-578.
DR PDBsum; 5XJG; -.
DR PDBsum; 6KBM; -.
DR PDBsum; 6KBN; -.
DR AlphaFoldDB; P39968; -.
DR SMR; P39968; -.
DR BioGRID; 36717; 339.
DR ComplexPortal; CPX-1304; MYO2-VAC17-VAC8 transport complex.
DR ComplexPortal; CPX-1381; NVJ1-VAC8 nucleus-vacuole junction complex.
DR DIP; DIP-5121N; -.
DR IntAct; P39968; 29.
DR MINT; P39968; -.
DR STRING; 4932.YEL013W; -.
DR iPTMnet; P39968; -.
DR SwissPalm; P39968; -.
DR MaxQB; P39968; -.
DR PaxDb; P39968; -.
DR PRIDE; P39968; -.
DR EnsemblFungi; YEL013W_mRNA; YEL013W; YEL013W.
DR GeneID; 856702; -.
DR KEGG; sce:YEL013W; -.
DR SGD; S000000739; VAC8.
DR VEuPathDB; FungiDB:YEL013W; -.
DR eggNOG; KOG4224; Eukaryota.
DR GeneTree; ENSGT00940000167949; -.
DR HOGENOM; CLU_021483_0_0_1; -.
DR InParanoid; P39968; -.
DR OMA; VWDKPDG; -.
DR BioCyc; YEAST:G3O-30139-MON; -.
DR PRO; PR:P39968; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39968; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0045121; C:membrane raft; IDA:SGD.
DR GO; GO:0071563; C:Myo2p-Vac17p-Vac8p transport complex; IDA:SGD.
DR GO; GO:0005640; C:nuclear outer membrane; IC:ComplexPortal.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IMP:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0071255; P:Cvt vesicle assembly; IMP:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0071562; P:nucleus-vacuole junction assembly; IMP:SGD.
DR GO; GO:0000425; P:pexophagy; IDA:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:1903044; P:protein localization to membrane raft; IMP:SGD.
DR GO; GO:0034517; P:ribophagy; IDA:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IDA:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045156; Vac8.
DR PANTHER; PTHR47249; PTHR47249; 1.
DR Pfam; PF00514; Arm; 8.
DR SMART; SM00185; ARM; 9.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Lipoprotein; Membrane; Myristate; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..578
FT /note="Vacuolar protein 8"
FT /id="PRO_0000064302"
FT REPEAT 37..75
FT /note="ARM 1"
FT REPEAT 76..114
FT /note="ARM 2"
FT REPEAT 116..155
FT /note="ARM 3"
FT REPEAT 157..196
FT /note="ARM 4"
FT REPEAT 198..237
FT /note="ARM 5"
FT REPEAT 239..280
FT /note="ARM 6"
FT REPEAT 282..321
FT /note="ARM 7"
FT REPEAT 323..363
FT /note="ARM 8"
FT REPEAT 407..446
FT /note="ARM 9"
FT REGION 527..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:9490720"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:9490720"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:9490720"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:9490720"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 4..7
FT /note="CCSC->GTSS: In VAC8-3; not palmitoylated."
FT /evidence="ECO:0000269|PubMed:9490720"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:6KBM"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:5XJG"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6KBM"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:5XJG"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:6KBM"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6KBN"
FT HELIX 464..474
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 478..493
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:5XJG"
FT HELIX 506..511
FT /evidence="ECO:0007829|PDB:5XJG"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:6KBN"
FT HELIX 562..574
FT /evidence="ECO:0007829|PDB:6KBN"
SQ SEQUENCE 578 AA; 63208 MW; B2E75774B47E5933 CRC64;
MGSCCSCLKD SSDEASVSPI ADNEREAVTL LLGYLEDKDQ LDFYSGGPLK ALTTLVYSDN
LNLQRSAALA FAEITEKYVR QVSREVLEPI LILLQSQDPQ IQVAACAALG NLAVNNENKL
LIVEMGGLEP LINQMMGDNV EVQCNAVGCI TNLATRDDNK HKIATSGALI PLTKLAKSKH
IRVQRNATGA LLNMTHSEEN RKELVNAGAV PVLVSLLSST DPDVQYYCTT ALSNIAVDEA
NRKKLAQTEP RLVSKLVSLM DSPSSRVKCQ ATLALRNLAS DTSYQLEIVR AGGLPHLVKL
IQSDSIPLVL ASVACIRNIS IHPLNEGLIV DAGFLKPLVR LLDYKDSEEI QCHAVSTLRN
LAASSEKNRK EFFESGAVEK CKELALDSPV SVQSEISACF AILALADVSK LDLLEANILD
ALIPMTFSQN QEVSGNAAAA LANLCSRVNN YTKIIEAWDR PNEGIRGFLI RFLKSDYATF
EHIALWTILQ LLESHNDKVE DLVKNDDDII NGVRKMADVT FERLQRSGID VKNPGSNNNP
SSNDNNSNNN DTGSEHQPVE DASLELYNIT QQILQFLH
