IVY1_YEAST
ID IVY1_YEAST Reviewed; 453 AA.
AC Q04934; D6VSL1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein IVY1;
DE AltName: Full=Interaction with VPS33 and YPT7 protein 1;
GN Name=IVY1; OrderedLocusNames=YDR229W; ORFNames=YD9934.14;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS33 AND YPT7.
RX PubMed=12553664; DOI=10.1078/0171-9335-00290;
RA Lazar T., Scheglmann D., Gallwitz D.;
RT "A novel phospholipid-binding protein from the yeast Saccharomyces
RT cerevisiae with dual binding specificities for the transport GTPase Ypt7p
RT and the Sec1-related Vps33p.";
RL Eur. J. Cell Biol. 81:635-646(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84 AND SER-85, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: May be required for vacuolar fusion. Overexpression leads to
CC fragmentation of vacuoles, missorting of the vacuolar enzyme
CC carboxypeptidase Y (CPY) to the exterior of the cell and accumulation
CC of multivesicular bodies inside the cell.
CC {ECO:0000269|PubMed:12553664}.
CC -!- SUBUNIT: Homomultimer. Interacts with YPT7 and VPS33.
CC {ECO:0000269|PubMed:12553664}.
CC -!- INTERACTION:
CC Q04934; Q04934: IVY1; NbExp=2; IntAct=EBI-35255, EBI-35255;
CC Q04934; P20795: VPS33; NbExp=3; IntAct=EBI-35255, EBI-20395;
CC Q04934; P32939: YPT7; NbExp=3; IntAct=EBI-35255, EBI-29509;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12553664};
CC Peripheral membrane protein {ECO:0000269|PubMed:12553664}. Note=Binds
CC to various phospholipids.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48612; CAA88509.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12071.1; -; Genomic_DNA.
DR PIR; S59436; S59436.
DR RefSeq; NP_010515.3; NM_001180537.3.
DR AlphaFoldDB; Q04934; -.
DR SMR; Q04934; -.
DR BioGRID; 32281; 119.
DR DIP; DIP-2957N; -.
DR IntAct; Q04934; 14.
DR MINT; Q04934; -.
DR STRING; 4932.YDR229W; -.
DR iPTMnet; Q04934; -.
DR MaxQB; Q04934; -.
DR PaxDb; Q04934; -.
DR PRIDE; Q04934; -.
DR EnsemblFungi; YDR229W_mRNA; YDR229W; YDR229W.
DR GeneID; 851815; -.
DR KEGG; sce:YDR229W; -.
DR SGD; S000002637; IVY1.
DR VEuPathDB; FungiDB:YDR229W; -.
DR eggNOG; ENOG502QTA6; Eukaryota.
DR HOGENOM; CLU_034174_1_0_1; -.
DR InParanoid; Q04934; -.
DR OMA; RLKGCND; -.
DR BioCyc; YEAST:G3O-29808-MON; -.
DR PRO; PR:Q04934; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04934; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037470; IVY1.
DR PANTHER; PTHR38407; PTHR38407; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Phosphoprotein; Reference proteome; Vacuole.
FT CHAIN 1..453
FT /note="Protein IVY1"
FT /id="PRO_0000084277"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 102..122
FT /evidence="ECO:0000255"
FT COILED 230..257
FT /evidence="ECO:0000255"
FT COMPBIAS 353..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 453 AA; 49976 MW; 2DB24DD88BED4522 CRC64;
MPDNNTEQLQ GSPSSDQRLR VDWDNGNHFD VSPDRYAPHL SEFYPIVNSK RPVASSAGSE
NNDHLDDMNH LRSSKVYSKA RRASSITSGT STINDLQTLI TKRDVKETQE ALSTLLRNSN
AYSDSLLKTS QNGAEIAHSL ENIAKLKGCN DETAEKLLSA SGLFYLLSNH QLIMSKYFND
LLGDNLIDDI DEFELQTKIM ENKFKAQSKE QSLKLKLQER HNFDISKRKI RNLISYRESL
SSLQARLDQL ETLKHDFYMD SYELVENTCN KVLSKVATVS RAQVEISENI ARKGWSGGGL
DELLCDADDP FSKKADGPYG TIGGDGETAG EAYNSDEETG GNDVVLNELL EGTSQPSTSK
TSLPKSKGSS TVSTPNHSQS SSNKDGVRNN GGGKNGEDED TDNLMGTENS FSLPPTRNSA
EETTQTFKQL SIKEDNDNHS SDTDGMQDQS SNI
