ID   MCPA_TRIRU              Reviewed;         422 AA.
AC   A6XGK3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Metallocarboxypeptidase A;
DE            Short=MCPA;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14A;
DE   Flags: Precursor;
GN   Name=MCPA;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   PubMed=18222721; DOI=10.1016/j.ijmm.2007.11.005;
RA   Zaugg C., Jousson O., Lechenne B., Staib P., Monod M.;
RT   "Trichophyton rubrum secreted and membrane-associated carboxypeptidases.";
RL   Int. J. Med. Microbiol. 298:669-682(2008).
RN   [2]
RP   INDUCTION.
RX   PubMed=19098130; DOI=10.1128/ec.00208-08;
RA   Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA   Bueno M., Giddey K., Staib P.;
RT   "Gene expression profiling in the human pathogenic dermatophyte
RT   Trichophyton rubrum during growth on proteins.";
RL   Eukaryot. Cell 8:241-250(2009).
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000269|PubMed:18222721}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18222721}.
CC   -!- INDUCTION: Expression is strongly increased during growth on protein-
CC       rich medium. Expressed at even higher levels when keratin is present in
CC       the protein-rich medium. {ECO:0000269|PubMed:19098130}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; EU024297; ABW79919.1; -; Genomic_DNA.
DR   EMBL; DQ778058; ABG67896.1; -; mRNA.
DR   AlphaFoldDB; A6XGK3; -.
DR   SMR; A6XGK3; -.
DR   MEROPS; M14.014; -.
DR   PRIDE; A6XGK3; -.
DR   VEuPathDB; FungiDB:TERG_04176; -.
DR   OrthoDB; 524270at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.340; -; 1.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   Pfam; PF02244; Propep_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..112
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384105"
FT   CHAIN           113..422
FT                   /note="Metallocarboxypeptidase A"
FT                   /id="PRO_0000384106"
FT   ACT_SITE        385
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         310..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        248..271
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  47106 MW;  11A5047BB434AF40 CRC64;
     MRSVLSLALL AANVVTAAVV SPFDYSGYKV IRVPTQKDNV KEVQRVITDL NLDTWKYPKS
     EGQNADIVVP PSQISSFMER ISGMNIEMMH EDLGLSIRNE TSFEAYSAGY APDINWFKSY
     HSYQDHLSYL QDLQGLFRTR SEYVDAGKSH EGRTIPALHI WGSGGKNSKP AIIFHGTIHA
     REWITTMVTE YMAWSFLSQY NKNADITSIV DNFDIWIFPI VNPDGFAFTQ TSNRLWRKNR
     QPNPNARCPG RDLNRNYPYQ WVGPGSSSNP CSDTYRGAQP GDGTEIKVHI ANMKKIAANK
     GIAMFVDWHS YGQLFMSPYG YSCTARPPTD ARHQELSRIF AQALKAVHGT PYKTGPICNT
     IYQVNGDSVD YALEVLKVKL SLTAELRDTG ARGFVLPADQ IIPSGEETLA GTVAMLKAVI
     QG