ECM14_YEAST
ID ECM14_YEAST Reviewed; 430 AA.
AC P38836; D3DL80;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE AltName: Full=Extracellular mutant protein 14 {ECO:0000303|PubMed:9335584};
DE Flags: Precursor;
GN Name=ECM14 {ECO:0000303|PubMed:9335584};
GN OrderedLocusNames=YHR132C {ECO:0000312|SGD:S000001174};
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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, AND DISRUPTION PHENOTYPE.
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 FUNCTION, LACK OF CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP DISRUPTION PHENOTYPE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=33256608; DOI=10.1186/s12860-020-00330-w;
RA McDonald R.C., Schott M.J., Idowu T.A., Lyons P.J.;
RT "Biochemical and genetic analysis of Ecm14, a conserved fungal
RT pseudopeptidase.";
RL BMC Mol. Biol. 21:86-86(2020).
CC -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC organization and biogenesis. {ECO:0000269|PubMed:33256608,
CC ECO:0000269|PubMed:9335584}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14562095}. Secreted
CC {ECO:0000269|PubMed:33256608}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:33256608}.
CC -!- DISRUPTION PHENOTYPE: Growth rate is increased in lithium chloride
CC (PubMed:33256608). Calcofluor White sensitivity is background dependent
CC (PubMed:9335584, PubMed:33256608). {ECO:0000269|PubMed:33256608,
CC ECO:0000269|PubMed:9335584}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue in position 391 essential for
CC carbopeptidase activity. The mature form lacks catalytic activity
CC towards synthetic peptide substrates. {ECO:0000269|PubMed:33256608}.
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DR EMBL; U10398; AAB68415.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06824.1; -; Genomic_DNA.
DR PIR; S48976; S48976.
DR RefSeq; NP_012000.1; NM_001179262.1.
DR AlphaFoldDB; P38836; -.
DR SMR; P38836; -.
DR BioGRID; 36564; 72.
DR DIP; DIP-4615N; -.
DR IntAct; P38836; 2.
DR STRING; 4932.YHR132C; -.
DR MaxQB; P38836; -.
DR PaxDb; P38836; -.
DR PRIDE; P38836; -.
DR EnsemblFungi; YHR132C_mRNA; YHR132C; YHR132C.
DR GeneID; 856533; -.
DR KEGG; sce:YHR132C; -.
DR SGD; S000001174; ECM14.
DR VEuPathDB; FungiDB:YHR132C; -.
DR eggNOG; KOG2650; Eukaryota.
DR GeneTree; ENSGT00940000165901; -.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; P38836; -.
DR OMA; HQHAREH; -.
DR BioCyc; YEAST:G3O-31170-MON; -.
DR PRO; PR:P38836; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38836; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Metal-binding; Reference proteome; Secreted; Signal; Vacuole; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..430
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000004417"
FT PROPEP 25..105
FT /evidence="ECO:0000305|PubMed:33256608"
FT /id="PRO_0000453255"
FT BINDING 182..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 311..312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 251..272
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 430 AA; 49829 MW; 1B9F5C0D18266A88 CRC64;
MLHMNSLWGC FLFVLLAVTG AVQGLQEDYS EYAVYRFTSD NYSTLVRDVI APLTDDYDVW
TRSNNFIDIK LPKEIGEQIN DGQVIIDNMN ELIQNTLPTS QMMAREQAVF ENDYDFFFNE
YRDLDTIYMW LDLLERSFPS LVAVEHLGRT FEGRELKALH ISGNKPESNP EKKTIVITGG
IHAREWISVS TVCWALYQLL NRYGSSKKET KYLDDLDFLV IPVFNPDGYA YTWSHDRLWR
KNRQRTHVPQ CLGIDIDHSF GFQWEKAHTH ACSEEYSGET PFEAWEASAW YKYINETKGD
YKIYGYIDMH SYSQEILYPY AYSCDALPRD LENLLELSYG LSKAIRSKSG RNYDVISACK
DRGSDIFPGL GAGSALDFMY HHRAHWAFQL KLRDTGNHGF LLPPENIKPV GKETYAALKY
FCDFLLDPEI
