ID   LICI2_TACTR             Reviewed;         408 AA.
AC   Q27086;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Intracellular coagulation inhibitor 2 {ECO:0000305};
DE   AltName: Full=Limulus intracellular coagulation inhibitor 2 {ECO:0000303|PubMed:7822280};
DE            Short=LICI-2 {ECO:0000303|PubMed:7822280};
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:BAA06909.1};
RN   [1] {ECO:0000312|EMBL:BAA06909.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-39; 142-147; 171-207;
RP   261-270; 276-302 AND 373-392, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-174, AND DISULFIDE BOND.
RX   PubMed=7822280; DOI=10.1074/jbc.270.2.558;
RA   Miura Y., Kawabata S., Wakamiya Y., Nakamura T., Iwanaga S.;
RT   "A limulus intracellular coagulation inhibitor type 2. Purification,
RT   characterization, cDNA cloning, and tissue localization.";
RL   J. Biol. Chem. 270:558-565(1995).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=7822328; DOI=10.1074/jbc.270.2.892;
RA   Muta T., Seki N., Takaki Y., Hashimoto R., Oda T., Iwanaga A., Tokunaga F.,
RA   Iwanaga S.;
RT   "Purified horseshoe crab factor G. Reconstitution and characterization of
RT   the (1-->3)-beta-D-glucan-sensitive serine protease cascade.";
RL   J. Biol. Chem. 270:892-897(1995).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits proclotting enzyme
CC       and to a lesser extent clotting factor C and clotting factor G.
CC       {ECO:0000269|PubMed:7822280, ECO:0000269|PubMed:7822328}.
CC   -!- SUBUNIT: Monomer (PubMed:7822280). Forms a covalent heterodimer with
CC       clotting factor C chain B (PubMed:7822280). Forms a covalent
CC       heterodimer with proclotting enzyme heavy chain (PubMed:7822280).
CC       {ECO:0000269|PubMed:7822280}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7822280}.
CC       Note=Localizes in the large granules of hemocytes (PubMed:7822280).
CC       Secreted in hemolymph in response to external stimuli (PubMed:7822280).
CC       {ECO:0000269|PubMed:7822280}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in hemocytes (at protein
CC       level). {ECO:0000269|PubMed:7822280}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000255|RuleBase:RU000411}.
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DR   EMBL; D32211; BAA06909.1; -; mRNA.
DR   PIR; A55533; A55533.
DR   AlphaFoldDB; Q27086; -.
DR   SMR; Q27086; -.
DR   MEROPS; I04.063; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
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; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:7822280"
FT   CHAIN           23..408
FT                   /note="Intracellular coagulation inhibitor 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004203526"
FT   SITE            372..373
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:7822280"
FT   DISULFID        50..249
FT                   /evidence="ECO:0000305|PubMed:7822280"
SQ   SEQUENCE   408 AA;  46659 MW;  BF1E9C6F44E01B23 CRC64;
     MLSRRTLDCC LVMLIVSTTF CQELHFYKEK ADRSHENLKT AVNQFGIHLC RRLLNEGKNI
     IFSPFSLSTA LSMAFVGARG NTAIEMRSGL GFREAGLAQE DVPDSFYQAF QLLKSDQSGD
     KFYVANTALV QNNYNILNSY KRILHRKFYS DIQPVDFVRN GLWVKEMVNK WVSNITHNKI
     TSLIDKPLSP LTRLFLLNAV YFKGSWKTQF DRKRTTLSLF YNNNKVARRV EMMSLTNKFP
     YTYDSELKCQ VLELPYDGDK TSMIFILPEW DVRLKHVENA LSAQSVKQLI NNLQDTEIVV
     TIPKFKLENS PQIKEYLQVM GMNEAFSFSA DFSGMNGRRN LFVKDVLHKA MIDVNEEGSE
     AAAVSGVVVM LKSASHNLPT FVANHPFMFL IINKESGMIL FLGSVREL