SVL3_YEAST
ID SVL3_YEAST Reviewed; 825 AA.
AC Q03088; D6W3Y1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Styryl dye vacuolar localization protein 3;
GN Name=SVL3; OrderedLocusNames=YPL032C; ORFNames=P7102.17;
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=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 [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.
RX PubMed=9751732; DOI=10.1073/pnas.95.20.11721;
RA Zheng B., Wu J.N., Schober W., Lewis D.E., Vida T.;
RT "Isolation of yeast mutants defective for localization of vacuolar vital
RT dyes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11721-11726(1998).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 AND SER-551, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; THR-496; SER-551;
RP SER-662; THR-739; THR-756 AND SER-757, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May have a vacuolar function. {ECO:0000269|PubMed:9751732}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Bud
CC {ECO:0000269|PubMed:14562095}. Bud neck {ECO:0000269|PubMed:14562095}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:14562095}. Note=And found in
CC the cell periphery.
CC -!- MISCELLANEOUS: Present with 2180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PAM1/SVL3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44030; AAB68187.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11397.1; -; Genomic_DNA.
DR PIR; S62042; S62042.
DR RefSeq; NP_015293.1; NM_001183846.1.
DR AlphaFoldDB; Q03088; -.
DR SMR; Q03088; -.
DR BioGRID; 36146; 172.
DR DIP; DIP-2723N; -.
DR IntAct; Q03088; 23.
DR MINT; Q03088; -.
DR STRING; 4932.YPL032C; -.
DR iPTMnet; Q03088; -.
DR MaxQB; Q03088; -.
DR PaxDb; Q03088; -.
DR PRIDE; Q03088; -.
DR EnsemblFungi; YPL032C_mRNA; YPL032C; YPL032C.
DR GeneID; 856075; -.
DR KEGG; sce:YPL032C; -.
DR SGD; S000005953; SVL3.
DR VEuPathDB; FungiDB:YPL032C; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR GeneTree; ENSGT00940000176320; -.
DR HOGENOM; CLU_010717_0_0_1; -.
DR InParanoid; Q03088; -.
DR OMA; RENAYDY; -.
DR BioCyc; YEAST:G3O-33947-MON; -.
DR PRO; PR:Q03088; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03088; protein.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..825
FT /note="Styryl dye vacuolar localization protein 3"
FT /id="PRO_0000072340"
FT REGION 472..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..423
FT /evidence="ECO:0000255"
FT COMPBIAS 484..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 756
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 825 AA; 92144 MW; 1658119E0A436B11 CRC64;
MSSSSLRVLA IGNNPNILFY TSRFQLAKNI DLYHVNDSKS CQFEIETEYY GKDRFELENH
FTSIEHLTEA LSSKSSEAVF DIIIMSAPSL QELSSLASKL TSIIDSNTKI FLESSGFIQL
EPFVKLSMES PHVNVFSILT DLDIRQIGPN HFKHFPSTAK ENTIYLGESK SSTEKYSSGV
ITLLTTFEKL FAKLFSNIKI NLCNFSSIEF LSQQWKLAIS RICFDPLLIM FEQENPSDLD
QQIIAKPLIS GLVTEIITVA KTMGARLNSS HDNENSLLSL WKNSYHSTNK PPALVYHFIH
QTTPLNIDIL LLQTILLADD FGIKTPYLEF LYSVLSQFER LNSGKSKWFI RSDEKTQILQ
SLQKSQKNES ALQTQITSLQ GQISKLRQEL LMQAKQHEME TNELKEKHQV ALKAQAQAQA
QAQSQAQTSI EALTPTEATN QSDTNEYKAT GTPNLRDIED MALYSVNYGD SPVRSPPPVV
SSQPQMNSPL SSHSQTFGEN NGTNDKLLQE RELQLRKKEL ELQERELEFQ KRALQQQRFN
NSNNSIPRKP SFPQLQQSAN VRSNSRGMHG TNGAMSQPAS AGNFVDPISS SIAAYDPQQP
PSLPLQQPQQ SVQVQPFHSH SIKPTSRKNR NSNMPNIGNP SSINMSDFGR PPNNSSQTRL
NSMPTHSIVN QNRLRSQQSK NKLNMPHATN PNNTFNQVPA PSLNNHVPTQ RQFSSSTMIE
VTNNNNKVNN SSSNPDISTN SVVHNAMQFT NTNNNTSSTV DINDPKNIAP PPTTSVSAPS
TPTLSSSSQM ANMASPSTDN GDNEEKNGGK KKRFGLFKKK NKSKK
