ID   COAG_TACGI              Reviewed;         175 AA.
AC   P15566;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Coagulogen;
DE   Contains:
DE     RecName: Full=Coagulin chain A;
DE   Contains:
DE     RecName: Full=Peptide C;
DE   Contains:
DE     RecName: Full=Coagulin chain B;
OS   Tachypleus gigas (Southeast Asian horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Tachypleus.
OX   NCBI_TaxID=6852;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6469947; DOI=10.1093/oxfordjournals.jbchem.a134792;
RA   Miyata T., Usui K., Iwanaga S.;
RT   "The amino acid sequence of coagulogen isolated from southeast Asian
RT   horseshoe crab, Tachypleus gigas.";
RL   J. Biochem. 95:1793-1801(1984).
CC   -!- FUNCTION: Coagulogen is a gel-forming protein of hemolymph; it hinders
CC       the spread of invaders by immobilizing them.
CC   -!- SUBUNIT: Coagulogen is cleaved after Arg-18 and Arg-46 by a clotting
CC       enzyme contained in the hemocyte and activated by a bacterial endotoxin
CC       (lipopolysaccharide). This cleavage releases the peptide C and leaves 2
CC       chains of coagulin, A and B, linked by two disulfide bonds. Coagulin
CC       molecules interlink to form a gel.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- SIMILARITY: Belongs to the coagulin family. {ECO:0000305}.
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DR   PIR; A28851; A28851.
DR   AlphaFoldDB; P15566; -.
DR   SMR; P15566; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042381; P:hemolymph coagulation; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR000275; Coagulin.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   Pfam; PF02035; Coagulin; 1.
DR   PIRSF; PIRSF002379; Coagulogen; 1.
DR   PRINTS; PR00763; COAGULIN.
DR   SUPFAM; SSF57501; SSF57501; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemolymph clotting; Secreted.
FT   CHAIN           1..18
FT                   /note="Coagulin chain A"
FT                   /id="PRO_0000020959"
FT   PEPTIDE         19..46
FT                   /note="Peptide C"
FT                   /id="PRO_0000020960"
FT   CHAIN           47..175
FT                   /note="Coagulin chain B"
FT                   /id="PRO_0000020961"
FT   DISULFID        8..167
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..95
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..161
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..168
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..172
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   175 AA;  19771 MW;  0AD341551491475B CRC64;
     DDTNAPLCLC DEPGILGRKE FVSDATKTII EKAVEEVAKE GGVSGRGFSL FSHHPVFREC
     GKYECRTVRP EHSRCYNFPP FIHFKSECPV STRDCEPVFG YTAAGEFRVI VQAPRAGFRQ
     CVWQHKCRYG SNNCGFNGRC TQQRSVVRLV TFNLEKNGFL CETFRTCCGC PCRSF