ID   MCPB_TRIRU              Reviewed;         538 AA.
AC   A6XHF7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Carboxypeptidase 2;
DE            EC=3.4.17.-;
DE   AltName: Full=Carboxypeptidase M14B;
DE   AltName: Full=Carboxypeptidase MCPB;
DE   Flags: Precursor;
GN   Name=MCPB; Synonyms=CARB2;
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).
CC   -!- FUNCTION: Extracellular metalloprotease that contributes to
CC       pathogenicity. {ECO:0000269|PubMed:18222721}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18222721}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU024296; ABW79918.1; -; Genomic_DNA.
DR   EMBL; DQ786567; ABH03555.1; -; mRNA.
DR   AlphaFoldDB; A6XHF7; -.
DR   VEuPathDB; FungiDB:TERG_02214; -.
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   InterPro; IPR000834; Peptidase_M14.
DR   Pfam; PF00246; Peptidase_M14; 1.
PE   2: Evidence at transcript level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Protease; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..538
FT                   /note="Carboxypeptidase 2"
FT                   /id="PRO_0000384111"
FT   REGION          53..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   538 AA;  59861 MW;  C5309457D7706DA4 CRC64;
     MVAYRFLTLI SLGLGSHCVS ALQYGYNQLS THKDPAVVAG AFPAINGTHL RSPAFTSPGT
     VSRGFSDGTS GPTRDETMEG FMRRLARSNS WMAYHEAGFK SEEGRKFPYM YLSASSSSVE
     NPSSRKLRVW LQGGVHGNEP AGDQSMLVLL GDLAANQKWA AKLLEKMDIL VLPRYNPDGV
     FYFQRYLATN FDPNRDHLKL ARQQTRDIKE LFAKFSPHIA TDMHEFTAGR AFGPKKDFIY
     AADALFSAAK NLNIDEGIRQ LSEKLFAKRM GKDIEAAGLR WDPYITLGES SSSKLLLREA
     GTDAKIGRNA MGLSQCVVFL CETRGIGIAD QHFERRTLSG LVMAKSVLQT AVDNFDEVYN
     TIERGIRRFT NSRNDIVLTD KSPIIERTFG MLNTTDASLF DYPIDFATTT PAEPVLTRSR
     PRAYLIPPSW PDIVKRLEVF GVKADKLPYS YVGPVEALNV TSVTFDKEFY EGVVTTTVET
     KLVERSIRLP PGSYLVKTNQ KNAALAFVAL EPENIDSFAS FGIIPVNTGD QYPIFRLK