YL413_YEAST
ID YL413_YEAST Reviewed; 675 AA.
AC Q06689; D6VZ50;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cell membrane protein YLR413W;
DE Flags: Precursor;
GN OrderedLocusNames=YLR413W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INDUCTION.
RX PubMed=10601195; DOI=10.1128/jb.181.24.7409-7413.1999;
RA ter Linde J.J.M., Liang H., Davis R.W., Steensma H.Y., van Dijken J.P.,
RA Pronk J.T.;
RT "Genome-wide transcriptional analysis of aerobic and anaerobic chemostat
RT cultures of Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:7409-7413(1999).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, 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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654 AND SER-665, 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 [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-671, AND IDENTIFICATION BY
RP 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By anaerobic conditions. {ECO:0000269|PubMed:10601195}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; U20162; AAB67494.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09716.1; -; Genomic_DNA.
DR PIR; S59379; S59379.
DR RefSeq; NP_013517.1; NM_001182301.1.
DR AlphaFoldDB; Q06689; -.
DR BioGRID; 31672; 113.
DR DIP; DIP-5075N; -.
DR IntAct; Q06689; 20.
DR MINT; Q06689; -.
DR STRING; 4932.YLR413W; -.
DR iPTMnet; Q06689; -.
DR MaxQB; Q06689; -.
DR PaxDb; Q06689; -.
DR PRIDE; Q06689; -.
DR EnsemblFungi; YLR413W_mRNA; YLR413W; YLR413W.
DR GeneID; 851131; -.
DR KEGG; sce:YLR413W; -.
DR SGD; S000004405; YLR413W.
DR VEuPathDB; FungiDB:YLR413W; -.
DR eggNOG; ENOG502QVQ9; Eukaryota.
DR GeneTree; ENSGT00940000176595; -.
DR HOGENOM; CLU_402815_0_0_1; -.
DR InParanoid; Q06689; -.
DR OMA; SDFKPYM; -.
DR BioCyc; YEAST:G3O-32475-MON; -.
DR PRO; PR:Q06689; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06689; protein.
DR GO; GO:0051285; C:cell cortex of cell tip; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR Pfam; PF06687; SUR7; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..675
FT /note="Cell membrane protein YLR413W"
FT /id="PRO_0000247220"
FT TOPO_DOM 29..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..610
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 632..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 671
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 675 AA; 72698 MW; 92E23436DC857E95 CRC64;
MNFKILLPIC ALLTLTTFLL TIIATAGSTS NYKPITNIYI GDADISKINV TKVMPQVGPI
LTVLGSALTA PNTTVDTIFG ALKAIASTEA LSPLLHLLSN AANTSATLSS LTQLAPMALL
GTNTATTTTF SALDELLTTS KNTTELLDGF STLMSSMSTN TSSTSASLEN TVLTLLVDST
NPIGTTESLI TLNNMTTEEK TKLSPVFELF ASSKNITATC DALETIMNST IPTSTVSSLF
SSLKTSLAEG GNATETIMQL GSLVPSSLKP AVQAVVTLFD ETTSQNVTLS VLSTMIAENI
TQSSSAKAAM GALTDLLNYT TNQTELLTSV ESLALSKEAA SSTNQLVALD EILSASANAS
TVVSIIPTLE SQLANNTVLL KYVPYLFSLL AASSDPVSSF SSLVNITKWA ETNAATFMPM
LKILNSAVNM TTITPEQLKE MTPSILEYLH IPVIYRLSIF TMCRAHLNRT MYSCSKSHAV
QNMDFRSIVY NNIEGSDFKP YMDALNIGKD DLHLDGELQD RQHMYVPAVK AALAMNLMCI
ITSFFLMVFL LLLSRRSVVS QKLWLALGFI SCWICIFSGL GSTIFSVILN MMKSGSKKDN
YDVIISGSSP FYGLMWSGFV FAVLVFLCIA YCWWSSRKGA AIVEAEKAVQ ESDSTTSRII
EEHESPIDAE KNFAR
