ID   MCPIB_NERVS             Reviewed;          53 AA.
AC   C0HJE8;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Metallocarboxypeptidase inhibitor b {ECO:0000303|Ref.1};
DE            Short=MCPI {ECO:0000303|Ref.1};
DE   Contains:
DE     RecName: Full=Metallocarboxypeptidase inhibitor d {ECO:0000303|Ref.1};
DE     AltName: Full=Carboxypeptidase inhibitor d {ECO:0000303|Ref.1};
DE              Short=NvCId {ECO:0000303|Ref.1};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, 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 porcine CPB1. Does not inhibit D.melanogaster svr
CC       (carboxypeptidase D). Shows no activity against serine proteases
CC       subtilisin or bovine trypsin, cysteine protease papain, and aspartyl
CC       protease porcine pepsin. {ECO:0000250|UniProtKB:P86912,
CC       ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: [Metallocarboxypeptidase inhibitor b]:
CC       Mass=5959.853; Method=MALDI; Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Metallocarboxypeptidase inhibitor d]:
CC       Mass=5812.535; Method=MALDI; Evidence={ECO:0000269|Ref.1};
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DR   AlphaFoldDB; C0HJE8; -.
DR   SMR; C0HJE8; -.
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   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Zinc.
FT   CHAIN           1..53
FT                   /note="Metallocarboxypeptidase inhibitor b"
FT                   /id="PRO_0000424665"
FT   CHAIN           2..53
FT                   /note="Metallocarboxypeptidase inhibitor d"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000424666"
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:0000250"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000250|UniProtKB:P86912"
FT   DISULFID        15..51
FT                   /evidence="ECO:0000250|UniProtKB:P86912"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000250|UniProtKB:P86912"
SQ   SEQUENCE   53 AA;  5965 MW;  06965333857BF1EF CRC64;
     FHVPDDRPCI KPGRCPLVPD ATCTFVCKAA DNDFGYECQH VWTFEGQRVG CYA