ID   PNLN_PANAR              Reviewed;          79 AA.
AC   B3EWX6; A0A0K0WTK7; B3EWX7;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 3.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Panulirin {ECO:0000303|PubMed:24047891};
DE   Flags: Precursor;
OS   Panulirus argus (Caribbean spiny lobster) (Palinurus argus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC   Palinuroidea; Palinuridae; Panulirus.
OX   NCBI_TaxID=6737;
RN   [1] {ECO:0000312|EMBL:AKS26291.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pacios-Michelena A., Crabbe K., Montero-Alejo V., Perdomo-Morales R.,
RA   Vanden Broeck J.;
RT   "Cloning and sequencing of protease inhibitor panulirin from the spiny
RT   lobster Panulirus argus, immune challenge and tissue dependent transcript
RT   regulation.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 27-74, FUNCTION, SUBUNIT, TISSUE SPECIFICITY, PRESENCE
RP   OF DISULFIDE BONDS, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND 3D-STRUCTURE MODELING.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:24047891};
RX   PubMed=24047891; DOI=10.1074/jbc.m113.464297;
RA   Perdomo-Morales R., Montero-Alejo V., Corzo G., Besada V., Vega-Hurtado Y.,
RA   Gonzalez-Gonzalez Y., Perera E., Porto-Verdecia M.;
RT   "The Trypsin Inhibitor Panulirin Regulates the Prophenoloxidase-activating
RT   System in the Spiny Lobster Panulirus argus.";
RL   J. Biol. Chem. 288:31867-31879(2013).
CC   -!- FUNCTION: Involved in the melanization cascade in response to
CC       lipopolysaccharide (LPS). In vitro, reversibly and competitively
CC       inhibits trypsin (Ki=8.6 nM) but not serine proteases chymotrypsin,
CC       elastase, subtilisin, thrombin and plasmin, cysteine peptidase papain
CC       or metallopeptidase carboxypeptidase A. {ECO:0000269|PubMed:24047891}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24047891}.
CC   -!- TISSUE SPECIFICITY: Expressed in hemocytes (at protein level).
CC       {ECO:0000269|PubMed:24047891}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:24047891}.
CC   -!- MASS SPECTROMETRY: Mass=5367.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:24047891};
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DR   EMBL; KR350473; AKS26291.1; -; mRNA.
DR   AlphaFoldDB; B3EWX6; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Immunity; Protease inhibitor;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..26
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445629"
FT   PEPTIDE         27..74
FT                   /note="Panulirin"
FT                   /evidence="ECO:0000269|PubMed:24047891"
FT                   /id="PRO_0000421238"
FT   PROPEP          75..79
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445630"
FT   DISULFID        33..63
FT                   /evidence="ECO:0000305|PubMed:24047891"
FT   DISULFID        40..56
FT                   /evidence="ECO:0000305|PubMed:24047891"
FT   DISULFID        46..64
FT                   /evidence="ECO:0000305|PubMed:24047891"
FT   CONFLICT        73
FT                   /note="K -> Q (in Ref. 1; AKS26291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   79 AA;  8705 MW;  1E37C9A5F1FEF1A3 CRC64;
     MKNKAVLMLM ALFLVAVTQV HGDPEPSYKA RSCTAYGYFC MIPPRCRGTV VANHWCRARG
     HICCSSPSNV YGKNQLLAA