ECM30_YEAST
ID ECM30_YEAST Reviewed; 1274 AA.
AC Q06673; D6VZ70;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein ECM30;
DE AltName: Full=Extracellular mutant protein 30;
GN Name=ECM30; OrderedLocusNames=YLR436C;
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 IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
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-1065, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, 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-635 AND SER-1065, 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).
CC -!- FUNCTION: Seems to be involved in cell wall organization and
CC biogenesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U21094; AAB67519.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09736.1; -; Genomic_DNA.
DR PIR; S59405; S59405.
DR RefSeq; NP_013540.1; NM_001182324.1.
DR AlphaFoldDB; Q06673; -.
DR SMR; Q06673; -.
DR BioGRID; 31694; 110.
DR DIP; DIP-2932N; -.
DR IntAct; Q06673; 5.
DR MINT; Q06673; -.
DR STRING; 4932.YLR436C; -.
DR iPTMnet; Q06673; -.
DR MaxQB; Q06673; -.
DR PaxDb; Q06673; -.
DR PRIDE; Q06673; -.
DR EnsemblFungi; YLR436C_mRNA; YLR436C; YLR436C.
DR GeneID; 851156; -.
DR KEGG; sce:YLR436C; -.
DR SGD; S000004428; ECM30.
DR VEuPathDB; FungiDB:YLR436C; -.
DR eggNOG; KOG2226; Eukaryota.
DR HOGENOM; CLU_003989_0_0_1; -.
DR InParanoid; Q06673; -.
DR OMA; TYRDFAI; -.
DR BioCyc; YEAST:G3O-32493-MON; -.
DR PRO; PR:Q06673; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06673; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IBA:GO_Central.
DR GO; GO:0000138; C:Golgi trans cisterna; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR026705; Hid-1/Ecm30.
DR PANTHER; PTHR21575; PTHR21575; 1.
DR Pfam; PF12722; Hid1; 2.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1274
FT /note="Protein ECM30"
FT /id="PRO_0000086919"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1274 AA; 145052 MW; AAA9659F3373BB39 CRC64;
MGNTDSKSSS ILLNHCIALV RPEDADASSP SRTSSPSPSL SVDADPLSLN LSIFKLDSGP
DVEALFSDKP NVPLDTVFND FYLDFISVDV QDFSINSSFK KILHIISSLN PPNFNNLIVF
LSLYIILSAN SLPASRTGLH SSRLINAIKT LSILIPIYFD RVKSSTQDHY DVFWATQHEI
EGLPLQNIPL GERLLLAILK LAFQDNFTTA VTAHPSELWE IGILTNSNKY RSLLNMHHQW
HLFANRLLLL RLLAALFSSD LYTSGGKQDI NMFLVYWCTQ MPKDKSIQFT SSLLNCTMRF
ILNNNKDFQS LKANFFSSDA TASNWQTLYF QFVQSCLHVL NLSMSYKAQD NVITIFLTQL
QREYDLKLIL SSFIKIFKYP IDLAIEQESN IFNFTNNKHI DASRRRAVST SSHDNSSSSH
ASLPSSSSAA YHTKPQTKPQ LPEIHPLLIP MTILMTNLID CNKCFQNYFA DKFASRFIIF
SIYYLKYYDY SSLSSSSSTT RSNSSTTSNG TSNDTSNERS IVELNENSVS QILLPLLNHL
LLILTSKKLV LFKMLQTFNL NYYTNNLPNF YKLSNINGDI NNLTFRDFTV IQLSNLILDN
IKFNLQPNPI FYELIYNLLP INDEILTSSH KNDDSHDDLI LLSAKKKSAS PSAATSSHTS
SSKLSYNAAM SLLYVLSKSS NKVYLTTYAT PVFKTKDIPY MISPGFKMDL LALLLRSITI
FFTLYFDDAE NLLFAMVRHQ SITHQINDSI NSISKALDMN PNLNSHIMTL KQMGFNRKVQ
WKDFYQFEEI TDLPQVNLYS SANQQHQNQQ QGQNDNRGQN QNEDPGQENE SPTPYLLFNP
ASLENETPGT VKHFSSTNHD KNYQVIAFID FKSDSNLNLQ HQLEYWPHRP QWPTPLTFTH
KCKNPKYENF NEVWSGTVYL QILLRVIKQI LSKVPEIPRI KSVQYFETLS KLSALRSDIL
TTIHPRLPLD VRRLTTFQPL SMHTNDKLLM WFHIATWANI FTQTSFKYEE TFSHELRQFE
SLLDISIDEC EGNTISKPTT DRLGYIRRSR GQSSVSLERT ISAGSGVSTP TMALNRTKSN
GSGNLMNYFF QNTAQNHFQH LRSSSSSSSI TLEKTTSNSS SIRTRPNSHH VAPETNNNNS
TNGNSNNSSN GGFSFFKWKW GGNNSNGGSD DTKASQRDPN VSTSIITDNL NSYMFEEEIS
PGVVNNIIEN NIWVGTDIRL FKIANFRKES FSFLEMTSSF FKKFKFINSD NDNYNNNEFD
DNTQLRYTSR GLYR
