ID   MEP2_COCP7              Reviewed;         362 AA.
AC   C5PE62; Q3KRR1;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Neutral protease 2 homolog MEP2;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MEP2;
DE   AltName: Full=Metalloproteinase 2;
DE   Flags: Precursor;
GN   Name=MEP2; ORFNames=CPC735_001400;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=16177346; DOI=10.1128/iai.73.10.6689-6703.2005;
RA   Hung C.Y., Seshan K.R., Yu J.J., Schaller R., Xue J., Basrur V.,
RA   Gardner M.J., Cole G.T.;
RT   "A metalloproteinase of Coccidioides posadasii contributes to evasion of
RT   host detection.";
RL   Infect. Immun. 73:6689-6703(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Shows high activities on basic nuclear
CC       substrates such as histone and protamine. May be involved in virulence
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; AY987806; AAY45752.1; -; Genomic_DNA.
DR   EMBL; ACFW01000044; EER24795.1; -; Genomic_DNA.
DR   RefSeq; XP_003066940.1; XM_003066894.1.
DR   AlphaFoldDB; C5PE62; -.
DR   SMR; C5PE62; -.
DR   EnsemblFungi; EER24795; EER24795; CPC735_001400.
DR   GeneID; 9692333; -.
DR   KEGG; cpw:CPC735_001400; -.
DR   VEuPathDB; FungiDB:CPC735_001400; -.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   BRENDA; 3.4.24.39; 9184.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Virulence;
KW   Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..177
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407066"
FT   CHAIN           178..362
FT                   /note="Neutral protease 2 homolog MEP2"
FT                   /id="PRO_0000407067"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..255
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..280
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  39191 MW;  27AD751A089E3C0E CRC64;
     MLFPSIVAAL AALANPVLSL TIPQATGSEL DVQLSAIGNT RIKAVITNKA DRQLKLLKYN
     NFFDDGPIQK AGVFKDGQPV KFEGMLRRVL MKNLEPSLFV SLSPGQTVER EFDIASTADL
     ASGGAYSVFS QGAIPFAEGD GTTIAGAVAF KSNKLDLDID GALAATVSKA INPISARTRV
     ESACRGEQRE TLLKALEYSA QLSRAAAQAA QNNTRKVEEY FMKSDAQTVE TIVARLNAVA
     QESSSTDSGA TRYFCNDRGN QCTPNTIAYT LPSLNVVVNC PIYYDLPVIS DECHAQDQAT
     TCLHEFTHNP GVYDPYCRDH AYGYDGIRKL SPEQALLNAD TYSLFANGKP KSQTTSNFNL
     KF