MCPI_MELCP
ID MCPI_MELCP Reviewed; 197 AA.
AC P82968;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Four-domain proteases inhibitor;
DE AltName: Full=McaPI;
OS Melithaea caledonica.
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Alcyonacea;
OC Scleraxonia; Melithaeidae; Melithaea.
OX NCBI_TaxID=156534;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND VARIANT VAL-195.
RA Peduzzi J., Longeon A., Guyot M., Barthelemy M.;
RT "Amino acid sequence and kinetic properties of a four-domain proteases
RT inhibitor from the gorgonian Melithaea caledonica.";
RL Submitted (MAR-2001) to UniProtKB.
CC -!- FUNCTION: Inhibits trypsin, kallikrein, subtilisin Carlsberg, human
CC leukocyte elastase, porcine pancreatic elastase and chymotrypsin. Two
CC domains are for the inhibition of chymotrypsin. {ECO:0000269|Ref.1}.
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 AlphaFoldDB; P82968; -.
DR SMR; P82968; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00050; Kazal_1; 2.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00280; KAZAL; 3.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF100895; SSF100895; 3.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51465; KAZAL_2; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW Serine protease inhibitor.
FT CHAIN 1..197
FT /note="Four-domain proteases inhibitor"
FT /id="PRO_0000073197"
FT DOMAIN 1..47
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 48..95
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 96..143
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 144..194
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 7..8
FT /note="Reactive bond 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 55..56
FT /note="Reactive bond 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 103..104
FT /note="Reactive bond 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 154..155
FT /note="Reactive bond 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 1..31
FT /evidence="ECO:0000250"
FT DISULFID 5..24
FT /evidence="ECO:0000250"
FT DISULFID 13..45
FT /evidence="ECO:0000250"
FT DISULFID 49..79
FT /evidence="ECO:0000250"
FT DISULFID 53..72
FT /evidence="ECO:0000250"
FT DISULFID 61..93
FT /evidence="ECO:0000250"
FT DISULFID 97..127
FT /evidence="ECO:0000250"
FT DISULFID 101..120
FT /evidence="ECO:0000250"
FT DISULFID 109..141
FT /evidence="ECO:0000250"
FT DISULFID 144..194
FT /evidence="ECO:0000250"
FT DISULFID 153..177
FT /evidence="ECO:0000250"
FT DISULFID 169..190
FT /evidence="ECO:0000250"
FT VARIANT 195
FT /note="M -> V"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 197 AA; 21248 MW; 199D08A489879579 CRC64;
CDLACSLIYA PVCGSDGKTY PSECSMEATA CIDEVVITKV HDGPCETKCS AACTKEYNPQ
CGTDGVTYAN PCTLEYAKCK SDGEITFDHA GPCKPKCPTV CTLEYNPQCG TDGRTYGNPC
QLKVAECESD GRITLDHPGE CDACSLKKVV GPCRGAFRRY YFDSVSGKCE EFVYGGCGGN
DNNFKTLDAC QKRCMEE
