ID   LICI3_TACTR             Reviewed;         414 AA.
AC   Q94823;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Intracellular coagulation inhibitor 3 {ECO:0000305};
DE   AltName: Full=Limulus intracellular coagulation inhibitor 3 {ECO:0000303|PubMed:8798603};
DE            Short=LICI-3 {ECO:0000303|PubMed:8798603};
DE   Flags: Precursor;
OS   Tachypleus tridentatus (Japanese horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Tachypleus.
OX   NCBI_TaxID=6853 {ECO:0000312|EMBL:BAA12795.1};
RN   [1] {ECO:0000312|EMBL:BAA12795.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-42; 210-226 AND 302-332,
RP   FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=8798603; DOI=10.1074/jbc.271.39.23768;
RA   Agarwala K.L., Kawabata S., Miura Y., Kuroki Y., Iwanaga S.;
RT   "Limulus intracellular coagulation inhibitor type 3. Purification,
RT   characterization, cDNA cloning, and tissue localization.";
RL   J. Biol. Chem. 271:23768-23774(1996).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits clotting factor G and
CC       to a lesser extent proclotting enzyme and clotting factor C.
CC       {ECO:0000269|PubMed:8798603}.
CC   -!- SUBUNIT: Monomer (PubMed:8798603). Forms a covalent heterodimer with
CC       clotting factor G subunit beta chain B (PubMed:8798603).
CC       {ECO:0000269|PubMed:8798603}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q27086}.
CC       Note=Localizes in the large granules of hemocytes (By similarity).
CC       Secreted in hemolymph in response to external stimuli (By similarity).
CC       {ECO:0000250|UniProtKB:Q27086}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in hemocytes (at protein
CC       level). {ECO:0000269|PubMed:8798603}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8798603}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000255|RuleBase:RU000411}.
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DR   EMBL; D85341; BAA12795.1; -; mRNA.
DR   AlphaFoldDB; Q94823; -.
DR   SMR; Q94823; -.
DR   MEROPS; I04.064; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR015557; Serpin_B1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8798603"
FT   CHAIN           23..414
FT                   /note="Intracellular coagulation inhibitor 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004322072"
FT   SITE            381..382
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   414 AA;  46394 MW;  B9512303D6AAAF39 CRC64;
     MKTLIFTLSS LQLIFLPQLS LGNYLLDEIL HLSDVDQQQL SAVTRITNAS NYFGFDLYNT
     LKGSGNVLIS PYSLSCAMAM VYLGSRGVTE REMHSVLNYG SFGLTRDDVR LGFQQAINTL
     TSNTIGYTLD TANALLIQRS FEVQEDFRQK IETDFGAEVR EVDFQSQTTI VQQAINTWTA
     HKTQNNIQNI LKEPPDSNTL LFFLNAVYFK GFWETTFDPK QSTIMKFYNN GSVSTDTVMM
     MMESRLPFGY VESLNCLALE MPYQGRNVTM LLLLPVSPNG LPELEQALSP ASISLIYSTL
     RKRRVKVFIP KFKLEEEYEE VLKEGLSDMG MKSLFGFNAN LNGITEDTGL YVTTVVHKTS
     IEVDEEGTVA SAASGVGGGW RSATPRFMAN HPFLFFIRHS ETGAVLFMGR VSQL