ID   ECM21_YEAST             Reviewed;        1117 AA.
AC   P38167; D6VPQ2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Protein ECM21;
DE   AltName: Full=Extracellular mutant protein 21;
GN   Name=ECM21; OrderedLocusNames=YBL101C; ORFNames=YBL0814;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7502586; DOI=10.1002/yea.320111112;
RA   Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT   "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT   cerevisiae chromosome II.";
RL   Yeast 11:1103-1112(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
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   [4]
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   [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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577; LYS-651; LYS-712;
RP   LYS-794; LYS-807 AND LYS-1024, AND IDENTIFICATION BY 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   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA   Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT   "A subset of membrane-associated proteins is ubiquitinated in response to
RT   mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-527 AND SER-775, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-286 AND SER-550, AND
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-115; SER-775 AND
RP   SER-1035, AND 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   [12]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191 AND LYS-794, AND
RP   IDENTIFICATION BY 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   -!- FUNCTION: May be involved in cell wall organization and biogenesis.
CC   -!- INTERACTION:
CC       P38167; P39940: RSP5; NbExp=2; IntAct=EBI-21359, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CSR2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA55995.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB39760.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X79489; CAA55995.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z35862; CAB39760.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006936; DAA07022.1; -; Genomic_DNA.
DR   PIR; S45395; S45395.
DR   RefSeq; NP_009449.1; NM_001178341.1.
DR   PDB; 7QQY; X-ray; 1.26 A; B=2-8.
DR   PDBsum; 7QQY; -.
DR   AlphaFoldDB; P38167; -.
DR   SMR; P38167; -.
DR   BioGRID; 32602; 131.
DR   DIP; DIP-791N; -.
DR   IntAct; P38167; 7.
DR   MINT; P38167; -.
DR   STRING; 4932.YBL101C; -.
DR   GlyGen; P38167; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P38167; -.
DR   MaxQB; P38167; -.
DR   PaxDb; 4932-YBL101C; -.
DR   PeptideAtlas; P38167; -.
DR   TopDownProteomics; P38167; -.
DR   EnsemblFungi; YBL101C_mRNA; YBL101C; YBL101C.
DR   GeneID; 852173; -.
DR   KEGG; sce:YBL101C; -.
DR   AGR; SGD:S000000197; -.
DR   SGD; S000000197; ECM21.
DR   VEuPathDB; FungiDB:YBL101C; -.
DR   eggNOG; KOG3780; Eukaryota.
DR   GeneTree; ENSGT00940000176445; -.
DR   HOGENOM; CLU_006239_0_0_1; -.
DR   InParanoid; P38167; -.
DR   OMA; NMELPTY; -.
DR   OrthoDB; 2056731at2759; -.
DR   BioCyc; YEAST:G3O-28985-MONOMER; -.
DR   BioGRID-ORCS; 852173; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P38167; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38167; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   PANTHER; PTHR11188; ARRESTIN DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11188:SF182; PROTEIN ECM21-RELATED; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   SMART; SM01017; Arrestin_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Cytoplasm; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..1117
FT                   /note="Protein ECM21"
FT                   /id="PRO_0000086917"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          63..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1079..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1062
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         775
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1035
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        577
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131,
FT                   ECO:0000269|PubMed:14557538"
FT   CROSSLNK        651
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        712
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        794
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        807
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        1024
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CONFLICT        964..967
FT                   /note="PSGY -> HPDT (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1117 AA;  123610 MW;  7DE365C1625B8BA9 CRC64;
     MPFITSRPVA KNSSHSLSET DLNQSKGQPF QPSPTKKLGS MQQRRRSSTI RHALSSLLGG
     ANVHSPAVLN NTTKGGNNNG NIRSSNTDAQ LLGKKQNKQP PPNARRHSTT AIQGSISDSA
     TTTPRSSTSD TNRRTSGRLS VDQEPRISGG RYSQIEEDST VLDFDDDHNS SAVVSSDLSS
     TSLTRLANSK KFNEQFLIEY LTARGLLGPK TVLSNEYLKI SISTSGESVF LPTISSNDDE
     YLSRLNGLND GTDDAEADFF MDGIDQQEGN TPSLATTAAA TESGGSINEN RDTLLRENNS
     GDHPGSGSEL NTRSVEIDSS MVSYSIAVIV SVKKPTRFTD MQLELCSRVK VFWNTGVPPT
     KTFNEEFYNA ASMKWNLNDE NFDLFVPLSI SPDDQMIENN SNDRQMRLFK NIPTEERLYL
     DKTKTKASLL NAIDVNKTHL YQPGDYVFLV PVVFSNHIPE TIYLPSARVS YRLRLATKAI
     NRKGFYRQDS NSPQPIVSPD SSSSLSSTTS SLKLTETESA QAHRRISNTL FSKVKNHLHM
     SSHQLKNEES GEEDIFAEYP IKVIRTPPPV AVSTANKPIY INRVWTDSLS YEISFAQKYV
     SLNSEVPIKI KLAPICKNVC VKRIHVSITE RVTFVSKGYE YEYDQTDPVA KDPYNPYYLD
     FASKRRKERS VSLFEIRTKE KGTRALREEI VENSFNDNLL SYSPFDDDSD SKGNPKERLG
     ITEPIIIETK LKFPKYEDLD KRTAKIIPPY GIDAYTSIPN PEHAVANGPS HRRPSVIGFL
     SGHKGSKSHE ENEKPVYDPK FHQTIIKSNS GLPVKTHTRL NTPKRGLYLD SLHFSNVYCR
     HKLEIMLRIS KPDPECPSKL RHYEVLIDTP IFLVSEQCNS GNMELPTYDM ATMEGKGNQV
     PLSMNSDFFG NTCPPPPTFE EAISVPASPI VSPMGSPNIM ASYDPDLLSI QQLNLSRTTS
     VSGPSGYSDD AGVPNVNRNS ISNANAMNGS ISNSAFVSGN SGQGVARARA TSVNDRSRFN
     NLDKLLSTPS PVNRSHNSSP TNGLSQANGT VRIPNATTEN SKDKQNEFFK KGYTLANVKD
     DEEQEGIVSS SSADSLLSHG NEPPRYDEIV PLMSDEE
//