ID   MCPI_NERVS              Reviewed;          53 AA.
AC   P86912;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Metallocarboxypeptidase inhibitor;
DE            Short=MCPI {ECO:0000250|UniProtKB:P01075};
DE   AltName: Full=Carboxypeptidase inhibitor;
DE            Short=NvCI;
DE   Contains:
DE     RecName: Full=Metallocarboxypeptidase inhibitor c;
DE     AltName: Full=Carboxypeptidase inhibitor c;
DE              Short=NvCIc;
OS   Nerita versicolor (Four-tooth nerite) (Sea snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Neritimorpha; Cycloneritida; Neritoidea; Neritidae; Nerita.
OX   NCBI_TaxID=159942;
RN   [1]
RP   PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH
RP   HUMAN CPA4 AND ZINC, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND DISULFIDE
RP   BONDS.
RX   PubMed=22294694; DOI=10.1074/jbc.m111.330100;
RA   Covaleda G., del Rivero M.A., Chavez M.A., Aviles F.X., Reverter D.;
RT   "Crystal structure of novel metallocarboxypeptidase inhibitor from marine
RT   mollusk Nerita versicolor in complex with human carboxypeptidase A4.";
RL   J. Biol. Chem. 287:9250-9258(2012).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-53, FUNCTION, AND MASS SPECTROMETRY.
RA   Covaleda Cortes G.;
RT   "Kinetic and proteomic identification of protease inhibitors in marine
RT   invertebrates. Characterization of a carboxypeptidase inhibitor isolated
RT   from the mollusc Nerita versicolor.";
RL   Submitted (AUG-2013) to UniProtKB.
CC   -!- FUNCTION: Metallocarboxypeptidase inhibitor. Has an inhibitory effect
CC       on bovine CPA1 and CPB2, human CPA1, CPA2, CPA4, CPB1 and CPB2, and
CC       porcine CPB1. Does not inhibit D.melanogaster svr (carboxypeptidase D).
CC       Shows no activity against serine proteases subtilisin or bovine
CC       trypsin, cysteine protease papain, and aspartyl protease porcine
CC       pepsin. {ECO:0000269|PubMed:22294694, ECO:0000269|Ref.2}.
CC   -!- SUBUNIT: Monomer. Interacts (via C-terminus) with human CPA4.
CC       {ECO:0000269|PubMed:22294694}.
CC   -!- MASS SPECTROMETRY: [Metallocarboxypeptidase inhibitor]: Mass=5944.608;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:22294694};
CC   -!- MASS SPECTROMETRY: [Metallocarboxypeptidase inhibitor c]:
CC       Mass=5798.289; Method=MALDI; Evidence={ECO:0000269|Ref.2};
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   PDB; 4A94; X-ray; 1.70 A; C/D=1-53.
DR   PDB; 5MRV; X-ray; 1.85 A; C=1-53.
DR   PDBsum; 4A94; -.
DR   PDBsum; 5MRV; -.
DR   AlphaFoldDB; P86912; -.
DR   SMR; P86912; -.
DR   MEROPS; I92.001; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Zinc.
FT   CHAIN           1..53
FT                   /note="Metallocarboxypeptidase inhibitor"
FT                   /id="PRO_0000415947"
FT   CHAIN           2..53
FT                   /note="Metallocarboxypeptidase inhibitor c"
FT                   /id="PRO_0000424664"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with metallocarboxypeptidase
FT                   partner"
FT                   /evidence="ECO:0000269|PubMed:22294694"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000269|PubMed:22294694"
FT   DISULFID        15..51
FT                   /evidence="ECO:0000269|PubMed:22294694"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000269|PubMed:22294694"
FT   STRAND          22..29
FT                   /evidence="ECO:0007829|PDB:4A94"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:4A94"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:4A94"
SQ   SEQUENCE   53 AA;  5951 MW;  06965727D43AF1EF CRC64;
     FHVPDDRPCI NPGRCPLVPD ATCTFVCKAA DNDFGYECQH VWTFEGQRVG CYA