COAG_TACTR
ID COAG_TACTR Reviewed; 195 AA.
AC P02681;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 93.
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 Tachypleus tridentatus (Japanese horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Tachypleus.
OX NCBI_TaxID=6853;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3759932; DOI=10.1093/oxfordjournals.jbchem.a121696;
RA Miyata T., Matsumoto H., Hattori M., Sakaki Y., Iwanaga S.;
RT "Two types of coagulogen mRNAs found in horseshoe crab (Tachypleus
RT tridentatus) hemocytes: molecular cloning and nucleotide sequences.";
RL J. Biochem. 100:213-220(1986).
RN [2]
RP PROTEIN SEQUENCE OF 21-195.
RX PubMed=504251;
RA Takagi T., Hokama Y., Morita T., Iwanaga S., Nakamura S., Niwa M.;
RT "Amino acid sequence studies on horseshoe crab (Tachypleus tridentatus)
RT coagulogen and the mechanism of gel formation.";
RL Prog. Clin. Biol. Res. 29:169-184(1979).
RN [3]
RP PROTEIN SEQUENCE OF 21-71.
RX PubMed=985525; DOI=10.1016/s0006-291x(76)80217-3;
RA Nakamura S., Takagi T., Iwanaga S., Niwa M., Takahashi K.;
RT "Amino acid sequence studies on the fragments produced from horseshoe crab
RT coagulogen during gel formation: homologies with primate fibrinopeptide
RT B.";
RL Biochem. Biophys. Res. Commun. 72:902-908(1976).
RN [4]
RP PROTEIN SEQUENCE OF 67-195.
RX PubMed=6378899; DOI=10.1093/oxfordjournals.jbchem.a134752;
RA Takagi T., Hokama Y., Miyata T., Morita T., Iwanaga S.;
RT "Amino acid sequence of Japanese horseshoe crab (Tachypleus tridentatus)
RT coagulogen B chain: completion of the coagulogen sequence.";
RL J. Biochem. 95:1445-1457(1984).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9003754; DOI=10.1002/j.1460-2075.1996.tb01070.x;
RA Bergner A., Oganessyan V., Muta T., Iwanaga S., Typke D., Huber R.,
RA Bode W.;
RT "Crystal structure of a coagulogen, the clotting protein from horseshoe
RT crab: a structural homologue of nerve growth factor.";
RL EMBO J. 15:6789-6797(1996).
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 -!- MISCELLANEOUS: The sequence shown is that of coagulogen-1.
CC -!- SIMILARITY: Belongs to the coagulin family. {ECO:0000305}.
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DR EMBL; X04192; CAA27780.1; -; mRNA.
DR PIR; A94306; WCHCJ.
DR PIR; B27257; B27257.
DR PDB; 1AOC; X-ray; 2.00 A; A/B=21-195.
DR PDBsum; 1AOC; -.
DR AlphaFoldDB; P02681; -.
DR SMR; P02681; -.
DR EvolutionaryTrace; P02681; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemolymph clotting; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:504251,
FT ECO:0000269|PubMed:985525"
FT CHAIN 21..38
FT /note="Coagulin chain A"
FT /id="PRO_0000020962"
FT PEPTIDE 39..66
FT /note="Peptide C"
FT /evidence="ECO:0000269|PubMed:6378899"
FT /id="PRO_0000020963"
FT CHAIN 67..195
FT /note="Coagulin chain B"
FT /id="PRO_0000020964"
FT DISULFID 28..187
FT /note="Interchain (between A and B chains)"
FT DISULFID 30..115
FT /note="Interchain (between A and B chains)"
FT DISULFID 80..181
FT DISULFID 85..141
FT DISULFID 95..188
FT DISULFID 108..160
FT DISULFID 147..190
FT DISULFID 154..192
FT VARIANT 102
FT /note="T -> I (in coagulogen-2)"
FT VARIANT 106
FT /note="L -> S (in coagulogen-2)"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1AOC"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:1AOC"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1AOC"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1AOC"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:1AOC"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1AOC"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1AOC"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1AOC"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 163..173
FT /evidence="ECO:0007829|PDB:1AOC"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:1AOC"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1AOC"
SQ SEQUENCE 195 AA; 21840 MW; A437B86AC0F6EB23 CRC64;
MEKKLFGIAL LLTTVASVLA ADTNAPICLC DEPGVLGRTQ IVTTEIKDKI EKAVEAVAQE
SGVSGRGFSI FSHHPVFREC GKYECRTVRP EHSRCYNFPP FTHFKLECPV STRDCEPVFG
YTVAGEFRVI VQAPRAGFRQ CVWQHKCRFG SNSCGYNGRC TQQRSVVRLV TYNLEKDGFL
CESFRTCCGC PCRSF
