ID   MCPI_HIRME              Reviewed;          81 AA.
AC   P81511;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Metallocarboxypeptidase inhibitor;
DE   AltName: Full=Leech carboxypeptidase inhibitor;
DE            Short=LCI;
DE   Flags: Precursor;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-81, AND MASS
RP   SPECTROMETRY.
RX   PubMed=9830043; DOI=10.1074/jbc.273.49.32927;
RA   Reverter D., Vendrell J., Canals F., Horstmann J., Aviles F.X., Fritz H.,
RA   Sommerhoff C.P.;
RT   "A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis.
RT   Isolation, sequence analysis, cDNA cloning, recombinant expression, and
RT   characterization.";
RL   J. Biol. Chem. 273:32927-32933(1998).
RN   [2]
RP   STRUCTURE BY NMR, AND X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX
RP   WITH HUMAN CPA2.
RX   PubMed=10742178; DOI=10.1038/74092;
RA   Reverter D., Fernandez-Catalan C., Baumgartner R., Pfander R., Huber R.,
RA   Bode W., Vendrell J., Holak T.A., Aviles F.X.;
RT   "Structure of a novel leech carboxypeptidase inhibitor determined free in
RT   solution and in complex with human carboxypeptidase A2.";
RL   Nat. Struct. Biol. 7:322-328(2000).
CC   -!- FUNCTION: Tightly binding, competitive inhibitor of different types of
CC       pancreatic-like carboxypeptidases.
CC   -!- MASS SPECTROMETRY: Mass=7326; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9830043};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I46 family.
CC       {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; AJ010948; CAA09422.1; -; mRNA.
DR   PDB; 1DTD; X-ray; 1.65 A; B=20-80.
DR   PDB; 1DTV; NMR; -; A=16-81.
DR   PDB; 1ZFI; NMR; -; A=16-81.
DR   PDB; 1ZFL; NMR; -; A=16-81.
DR   PDB; 2ABZ; X-ray; 2.16 A; C/D/E/F=16-81.
DR   PDBsum; 1DTD; -.
DR   PDBsum; 1DTV; -.
DR   PDBsum; 1ZFI; -.
DR   PDBsum; 1ZFL; -.
DR   PDBsum; 2ABZ; -.
DR   AlphaFoldDB; P81511; -.
DR   SMR; P81511; -.
DR   MINT; P81511; -.
DR   MEROPS; I46.001; -.
DR   EvolutionaryTrace; P81511; -.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1040.10; -; 1.
DR   InterPro; IPR024063; Prot_inh_LCI.
DR   SUPFAM; SSF57620; SSF57620; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:9830043"
FT   CHAIN           16..81
FT                   /note="Metallocarboxypeptidase inhibitor"
FT                   /id="PRO_0000026725"
FT   SITE            80
FT                   /note="Interaction with carboxypeptidase"
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..48
FT   DISULFID        32..76
FT   DISULFID        33..57
FT   DISULFID        36..72
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   HELIX           55..60
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:1DTD"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:1DTD"
SQ   SEQUENCE   81 AA;  9068 MW;  7D7E175E6933922A CRC64;
     MFLLVFLCCL HLVISSHTPD ESFLCYQPDQ VCCFICRGAA PLPSEGECNP HPTAPWCREG
     AVEWVPYSTG QCRTTCIPYV E