MCPA_ARTBC
ID MCPA_ARTBC Reviewed; 422 AA.
AC D4AS12; D4AS11;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable metallocarboxypeptidase A;
DE Short=MCPA;
DE EC=3.4.17.-;
DE AltName: Full=Carboxypeptidase M14A;
DE Flags: Precursor;
GN Name=MCPA; ORFNames=ARB_07026/ARB_07027;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP INDUCTION.
RX PubMed=19942661; DOI=10.1099/mic.0.033464-0;
RA Staib P., Zaugg C., Mignon B., Weber J., Grumbt M., Pradervand S.,
RA Harshman K., Monod M.;
RT "Differential gene expression in the pathogenic dermatophyte Arthroderma
RT benhamiae in vitro versus during infection.";
RL Microbiology 156:884-895(2010).
CC -!- FUNCTION: Extracellular metalloprotease that contributes to
CC pathogenicity. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460}.
CC -!- INDUCTION: Expression is up-regulated during infection.
CC {ECO:0000269|PubMed:19942661}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE34075.1; Type=Erroneous gene model prediction; Note=ARB_07026 and ARB_07027 have been merged into one gene ARB_07026/ARB_07027.; Evidence={ECO:0000305};
CC Sequence=EFE34076.1; Type=Erroneous gene model prediction; Note=ARB_07026 and ARB_07027 have been merged into one gene ARB_07026/ARB_07027.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000007; EFE34075.1; ALT_SEQ; Genomic_DNA.
DR EMBL; ABSU01000007; EFE34076.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003014464.1; XM_003014418.1.
DR RefSeq; XP_003014465.1; XM_003014419.1.
DR AlphaFoldDB; D4AS12; -.
DR SMR; D4AS12; -.
DR STRING; 663331.D4AS12; -.
DR MEROPS; M14.014; -.
DR EnsemblFungi; EFE34075; EFE34075; ARB_07026.
DR EnsemblFungi; EFE34076; EFE34076; ARB_07027.
DR GeneID; 9520516; -.
DR GeneID; 9520517; -.
DR KEGG; abe:ARB_07026; -.
DR KEGG; abe:ARB_07027; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_1937617_0_0_1; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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; Reference proteome; Secreted; Signal; Virulence;
KW 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_0000398175"
FT CHAIN 113..422
FT /note="Probable metallocarboxypeptidase A"
FT /id="PRO_0000398176"
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; 47104 MW; F9BCB27189424307 CRC64;
MRSVLSLALL AANVVTAAVV APFDYSGYKV IRVPTQKDNV KEVQRIITDL 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
