COAG_LIMPO
ID COAG_LIMPO Reviewed; 195 AA.
AC P03998;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 25-MAY-2022, entry version 79.
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;
DE Flags: Precursor;
OS Limulus polyphemus (Atlantic horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Limulus.
OX NCBI_TaxID=6850;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3756166; DOI=10.1016/0167-4781(86)90079-5;
RA Cheng S.M., Suzuki A., Zon G., Liu T.Y.;
RT "Characterization of a complementary deoxyribonucleic acid for the
RT coagulogen of Limulus polyphemus.";
RL Biochim. Biophys. Acta 868:1-8(1986).
RN [2]
RP PROTEIN SEQUENCE OF 21-195.
RX PubMed=6378904; DOI=10.1016/s0021-9258(17)47244-9;
RA Miyata T., Hiranaga M., Umezu M., Iwanaga S.;
RT "Amino acid sequence of the coagulogen from Limulus polyphemus hemocytes.";
RL J. Biol. Chem. 259:8924-8933(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-38 and Arg-66 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 EMBL; X04424; CAA28020.1; -; mRNA.
DR PIR; A43790; WCHCA.
DR RefSeq; XP_013783200.1; XM_013927746.1.
DR AlphaFoldDB; P03998; -.
DR SMR; P03998; -.
DR GeneID; 106467396; -.
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;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:6378904"
FT CHAIN 21..38
FT /note="Coagulin chain A"
FT /id="PRO_0000020956"
FT PEPTIDE 39..66
FT /note="Peptide C"
FT /id="PRO_0000020957"
FT CHAIN 67..195
FT /note="Coagulin chain B"
FT /id="PRO_0000020958"
FT DISULFID 28..188
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 30..115
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250"
FT DISULFID 80..182
FT /evidence="ECO:0000250"
FT DISULFID 85..141
FT /evidence="ECO:0000250"
FT DISULFID 95..189
FT /evidence="ECO:0000250"
FT DISULFID 108..161
FT /evidence="ECO:0000250"
FT DISULFID 147..191
FT /evidence="ECO:0000250"
FT DISULFID 155..193
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="H -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..106
FT /note="PS -> HP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21818 MW; 5F7CF52BE3A463BA CRC64;
MEKKLLGIAI LFVTVVSVLA GDPNVPTCLC EEPTLLGRKV IVSQETKDKI EEAVQAITDK
DEISGRGFSI FGGHPAFKEC GKYECRTVTS EDSRCYNFFP FHHFPSECPV SVSACEPTFG
YTTSNELRII VQAPKAGFRQ CVWQHKCRAY GSNFCQRTGR CTQQRSVVRL VTYDLEKGVF
FCENVRTCCG CPCRS
