ADD37_YEAST
ID ADD37_YEAST Reviewed; 198 AA.
AC Q03233; D6W008;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha1-proteinase inhibitor-degradation deficient protein 37;
GN Name=ADD37; OrderedLocusNames=YMR184W; ORFNames=YM8010.14;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=12711700; DOI=10.1242/jcs.00439;
RA Palmer E.A., Kruse K.B., Fewell S.W., Buchanan S.M., Brodsky J.L.,
RA McCracken A.A.;
RT "Differential requirements of novel A1PiZ degradation deficient (ADD) genes
RT in ER-associated protein degradation.";
RL J. Cell Sci. 116:2361-2373(2003).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, 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 INDUCTION.
RX PubMed=17351896; DOI=10.1002/yea.1446;
RA Lee M.-W., Kim B.-J., Choi H.-K., Ryu M.-J., Kim S.-B., Kang K.-M.,
RA Cho E.-J., Youn H.-D., Huh W.-K., Kim S.-T.;
RT "Global protein expression profiling of budding yeast in response to DNA
RT damage.";
RL Yeast 24:145-154(2007).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP 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: Involved in ER-associated protein degradation (ERAD).
CC {ECO:0000269|PubMed:12711700}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: In response to the DNA-damaging agent MMS.
CC {ECO:0000269|PubMed:17351896}.
CC -!- MISCELLANEOUS: Present with 1270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49808; CAA89917.1; -; Genomic_DNA.
DR EMBL; AY557970; AAS56296.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10082.1; -; Genomic_DNA.
DR PIR; S55131; S55131.
DR RefSeq; NP_013909.1; NM_001182690.1.
DR AlphaFoldDB; Q03233; -.
DR BioGRID; 35362; 69.
DR DIP; DIP-3848N; -.
DR IntAct; Q03233; 2.
DR MINT; Q03233; -.
DR STRING; 4932.YMR184W; -.
DR iPTMnet; Q03233; -.
DR MaxQB; Q03233; -.
DR PaxDb; Q03233; -.
DR PRIDE; Q03233; -.
DR EnsemblFungi; YMR184W_mRNA; YMR184W; YMR184W.
DR GeneID; 855222; -.
DR KEGG; sce:YMR184W; -.
DR SGD; S000004796; ADD37.
DR VEuPathDB; FungiDB:YMR184W; -.
DR eggNOG; ENOG502S4DB; Eukaryota.
DR HOGENOM; CLU_1496199_0_0_1; -.
DR InParanoid; Q03233; -.
DR OMA; PGYNDCP; -.
DR BioCyc; YEAST:G3O-32872-MON; -.
DR PRO; PR:Q03233; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03233; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..198
FT /note="Alpha1-proteinase inhibitor-degradation deficient
FT protein 37"
FT /id="PRO_0000203321"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 198 AA; 22110 MW; 2716B90391A82092 CRC64;
MAIKPTKSFQ NCLEAEVPGY NDCPTVLFSI DPNSGPRSKS KQRTKSKRCV SGRLATEVLD
LYGNTKTATT PPPVLRRPSV TAAQQESACE GVLVKDQGDR QLQPILCSKE ELVAKINDLC
VCGSKLSSKE LEFYKKKLDS NITKILQNEH TKTVLSQIFN EKDKNMAVKT IKHWMVTDTT
ISNWCPAFLK IFENAMPN
