ID   TL5B_TACTR              Reviewed;         316 AA.
AC   Q9U8W7; Q9U8W6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Techylectin-5B;
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] {ECO:0000305, ECO:0000312|EMBL:BAA84189.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-33 AND 242-247,
RP   FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:10468566};
RX   PubMed=10468566; DOI=10.1073/pnas.96.18.10086;
RA   Gokudan S., Muta T., Tsuda R., Koori K., Kawahara T., Seki N., Mizunoe Y.,
RA   Wai S.N., Iwanaga S., Kawabata S.;
RT   "Horseshoe crab acetyl group-recognizing lectins involved in innate
RT   immunity are structurally related to fibrinogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10086-10091(1999).
CC   -!- FUNCTION: Lectin involved in innate immunity. Agglutinates all types of
CC       human erythrocytes, Gram-positive and Gram-negative bacteria. Has a
CC       stronger agglutinating activity towards Gram-negative bacteria than
CC       towards Gram-positive bacteria. Specifically recognizes acetyl group-
CC       containing substances on agglutinated cells. The hemagglutinating
CC       activity was inhibited by EDTA, acetyl group-containing mono- and
CC       disaccharides, N-acetyl derivatives of amino acids, other acetyl group-
CC       containing substances, propionamide and benzamide. Enhances the
CC       antimicrobial activity of big defensin against Gram-positive bacteria
CC       but not against Gram-negative bacteria. {ECO:0000269|PubMed:10468566}.
CC   -!- SUBUNIT: Tetramer. {ECO:0000269|PubMed:10468566}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemocytes. {ECO:0000269|PubMed:10468566}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA84190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB024738; BAA84189.1; -; mRNA.
DR   EMBL; AB024739; BAA84190.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9U8W7; -.
DR   SMR; Q9U8W7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 1.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR020837; Fibrinogen_CS.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW   Metal-binding; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:10468566"
FT   CHAIN           28..316
FT                   /note="Techylectin-5B"
FT                   /evidence="ECO:0000269|PubMed:10468566"
FT                   /id="PRO_0000260046"
FT   DOMAIN          86..307
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT   SITE            254
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT   SITE            264
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT   SITE            281
FT                   /note="Implicated in ligand binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..124
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        250..263
FT                   /evidence="ECO:0000250|UniProtKB:Q9U8W8,
FT                   ECO:0000255|PROSITE-ProRule:PRU00739"
FT   CONFLICT        3
FT                   /note="T -> S (in Ref. 1; BAA84190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="D -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="P -> S (in Ref. 1; BAA84190)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  36112 MW;  6FFBEFD4159EDF1D CRC64;
     MHTVLYSNMK NMFQLLSFLC VSLLVAGDVH HHAACSTVCS LKGILDSVSD LTDLAKERLA
     TLQNPICSKD KAFYMETYTN VTQNKAEKNG LPINCATVYQ QGNRTSGIYM IWPLFLNHPI
     SVFCDMETAG GGWTVIQRRG DFGQPIQNFY QTWESYKNGF GNLTKEFWLG NDIIFVLTNQ
     DSVVLRVDLE DFEGGRRYAE AVEFLVRSEI ELYKMSFKTY KGDAGDSLSQ HNNMPFTTKD
     RDNDKWEKNC AEAYKGGWWY NACHHSNLNG MYLRGPHEES AVGVNWYQWR GHNYSLKVSE
     MKIRPIIFVP GEGLPK