ID   LICI1_TACTR             Reviewed;         418 AA.
AC   Q27085;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Intracellular coagulation inhibitor 1 {ECO:0000305};
DE   AltName: Full=Limulus intracellular coagulation inhibitor 1 {ECO:0000303|PubMed:8276848};
DE            Short=LICI-1 {ECO:0000303|PubMed:8276848};
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:BAA03374.1};
RN   [1] {ECO:0000312|EMBL:BAA03374.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-56; 92-106; 127-149;
RP   156-183; 188-206; 278-295; 313-382 AND 389-415, FUNCTION, SUBUNIT, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=8276848; DOI=10.1016/s0021-9258(17)42383-0;
RA   Miura Y., Kawabata S., Iwanaga S.;
RT   "A Limulus intracellular coagulation inhibitor with characteristics of the
RT   serpin superfamily. Purification, characterization, and cDNA cloning.";
RL   J. Biol. Chem. 269:542-547(1994).
RN   [2]
RP   INTERACTION WITH BIG DEFENSIN.
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 specifically inhibits clotting
CC       factor C (PubMed:8276848). Does not inhibit clotting factor B or
CC       proclotting enzyme (PubMed:8276848). {ECO:0000269|PubMed:8276848}.
CC   -!- SUBUNIT: Monomer (PubMed:8276848). Forms a covalent heterodimer with
CC       clotting factor C (PubMed:8276848). Interacts with big defensin
CC       (PubMed:8798603). {ECO:0000269|PubMed:8276848,
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: Expressed in hemocytes (at protein level).
CC       {ECO:0000269|PubMed:8276848}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8276848}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000255|RuleBase:RU000411}.
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DR   EMBL; D14483; BAA03374.1; -; mRNA.
DR   PIR; A53120; A53120.
DR   AlphaFoldDB; Q27085; -.
DR   SMR; Q27085; -.
DR   MEROPS; I04.062; -.
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..24
FT                   /evidence="ECO:0000269|PubMed:8276848"
FT   CHAIN           25..418
FT                   /note="Intracellular coagulation inhibitor 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004203906"
FT   SITE            383..384
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   418 AA;  47523 MW;  F9B79109AFC921A5 CRC64;
     MKLGDWKFCL LLFQLMFLTN VCLSDLSFNP YKWPVNQLRR VIGAVKVTNT SNYFGFSLYE
     NLNSNGNVFI SPYSLASVMA MLYLGARGVT KNEMDLTLGY NSVNLNSEDL VLGFQQSLLL
     LNAESKEYQL ETANSLMIQN TFNILDNYKR MLEDKFGANV QDVDFINKAE LVQRYINAWV
     AFKTKNKIPI LLNEPLKPET RLAFFNAVYF KGVWETKFDS ALTRRATFYN NGYVPTQVPM
     MMLRGIFPFA YVSSLRSYVL ELPYKGHEVS MLLLLPKDRN GISDLERDLS SSSLDSVTSN
     LREIGVLVTI PKFKLEETYE DDLKQSLESM GMTSLFSEAN ANLEGITGHR DLFVTKITHR
     TLIEVNEEGT EASGISSVVA GVRSGWKRPT FTADHPFVFF IRHNRSGIIL FMGRVSQL