TL5A_TACTR
ID TL5A_TACTR Reviewed; 292 AA.
AC Q9U8W8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Techylectin-5A;
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:BAA84188.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-31; 104-109 AND 275-280,
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND PYROGLUTAMATE FORMATION AT
RP GLN-24.
RC TISSUE=Heart {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).
RN [2] {ECO:0000312|PDB:1JC9}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 24-292, AND SUBUNIT.
RX PubMed=11707569; DOI=10.1073/pnas.201523798;
RA Kairies N., Beisel H.-G., Fuentes-Prior P., Tsuda R., Muta T., Iwanaga S.,
RA Bode W., Huber R., Kawabata S.;
RT "The 2.0-A crystal structure of tachylectin 5A provides evidence for the
RT common origin of the innate immunity and the blood coagulation systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13519-13524(2001).
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: Multimeric. PubMed:10468566 and PubMed:11707569 are in
CC disagreement about the nature of the multimer, PubMed:10468566 finds
CC hexamers and octamers, the results in PubMed:11707569 suggest
CC tetramers. {ECO:0000269|PubMed:10468566, ECO:0000269|PubMed:11707569}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart and intestine, weakly
CC expressed in hepatopancreas. Not found in hemocytes, stomach, nervous
CC tissue or skeletal muscle. {ECO:0000269|PubMed:10468566}.
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DR EMBL; AB024737; BAA84188.1; -; mRNA.
DR PDB; 1JC9; X-ray; 2.01 A; A=24-292.
DR PDBsum; 1JC9; -.
DR AlphaFoldDB; Q9U8W8; -.
DR SMR; Q9U8W8; -.
DR UniLectin; Q9U8W8; -.
DR PRIDE; Q9U8W8; -.
DR EvolutionaryTrace; Q9U8W8; -.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lectin; Metal-binding; Pyrrolidone carboxylic acid; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10468566"
FT CHAIN 24..292
FT /note="Techylectin-5A"
FT /evidence="ECO:0000269|PubMed:10468566"
FT /id="PRO_0000260045"
FT DOMAIN 63..286
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11707569"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11707569"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 209
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 233
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 243
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 259
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 260
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT SITE 271
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000269|PubMed:11707569"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10468566"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11707569"
FT DISULFID 229..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11707569"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1JC9"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1JC9"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1JC9"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:1JC9"
SQ SEQUENCE 292 AA; 33787 MW; D028DE1E2716F71A CRC64;
MHNLRNILFV ITLIGQKYGL TSSQNKELCD VTSSTGLLDS IKVMASHVKE QLKDKGTSEV
AQPIVSPDPT DCADILLNGY RSSGGYRIWP KSWMTVGTLN VYCDMETDGG GWTVIQRRGN
YGNPSDYFYK PWKNYKLGFG NIEKDFWLGN DRIFALTNQR NYMIRFDLKD KENDTRYAIY
QDFWIENEDY LYCLHIGNYS GDAGNSFGRH NGHNFSTIDK DHDTHETHCA QTYKGGWWYD
RCHESNLNGL YLNGEHNSYA DGIEWRAWKG YHYSLPQVEM KIRPVEFNII GN
