ID   IPK2_CENMR              Reviewed;          50 AA.
AC   P84755;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Protease inhibitor 2 {ECO:0000303|PubMed:16546427, ECO:0000303|PubMed:17976011};
DE   AltName: Full=CmPI-II {ECO:0000303|PubMed:16546427, ECO:0000303|PubMed:17976011};
DE   AltName: Full=Protease inhibitor-II {ECO:0000303|PubMed:16546427, ECO:0000303|PubMed:17976011};
OS   Cenchritis muricatus (Beaded periwinkle).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Littorinimorpha; Littorinoidea; Littorinidae; Cenchritis.
OX   NCBI_TaxID=197001;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RX   PubMed=17976011; DOI=10.1515/bc.2007.129;
RA   Gonzalez Y., Pons T., Gil J., Besada V., Alonso-del-Rivero M., Tanaka A.S.,
RA   Araujo M.S., Chavez M.A.;
RT   "Characterization and comparative 3D modeling of CmPI-II, a novel 'non-
RT   classical' Kazal-type inhibitor from the marine snail Cenchritis muricatus
RT   (Mollusca).";
RL   Biol. Chem. 388:1183-1194(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-20, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=16546427; DOI=10.1016/j.cbpa.2006.01.022;
RA   Gonzalez Y., Tanaka A.S., Hirata I.Y., del Rivero M.A., Oliva M.L.V.,
RA   Araujo M.S., Chavez M.A.;
RT   "Purification and partial characterization of human neutrophil elastase
RT   inhibitors from the marine snail Cenchritis muricatus (Mollusca).";
RL   Comp. Biochem. Physiol. 146A:506-513(2007).
CC   -!- FUNCTION: Serine protease inhibitor. Strongly inhibits human neutrophil
CC       elastase and trypsin, also inhibits porcine pancreatic elastase and
CC       subtilisin A. Does not inhibit chymotrypsin, plasma kallikrein,
CC       pancreatic kallikrein, thrombin or papain.
CC       {ECO:0000269|PubMed:16546427, ECO:0000269|PubMed:17976011}.
CC   -!- MASS SPECTROMETRY: Mass=5469; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16546427};
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DR   PDB; 2N71; NMR; -; A=1-50.
DR   PDBsum; 2N71; -.
DR   AlphaFoldDB; P84755; -.
DR   BMRB; P84755; -.
DR   SMR; P84755; -.
DR   MEROPS; I01.046; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..50
FT                   /note="Protease inhibitor 2"
FT                   /id="PRO_0000073200"
FT   DOMAIN          2..50
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            11..12
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        10..29
FT                   /evidence="ECO:0000250|UniProtKB:P01003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        18..50
FT                   /evidence="ECO:0000250|UniProtKB:P01003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00798"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:2N71"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:2N71"
FT   STRAND          23..27
FT                   /evidence="ECO:0007829|PDB:2N71"
FT   HELIX           28..37
FT                   /evidence="ECO:0007829|PDB:2N71"
FT   STRAND          44..48
FT                   /evidence="ECO:0007829|PDB:2N71"
SQ   SEQUENCE   50 AA;  5486 MW;  6925CF7F9BB71E28 CRC64;
     AEDCVGRKAC TREWYPVCGS DGVTYSNPCN FSAQQEQCDP NITIAHMGEC