TAL2_TACTR
ID TAL2_TACTR Reviewed; 255 AA.
AC Q27084;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Tachylectin-2;
DE AltName: Full=Lectin L10c;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8537358; DOI=10.1074/jbc.270.52.31008;
RA Okino N., Kawabata S., Saito T., Hirata M., Takagi T., Iwanaga S.;
RT "Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10)
RT from horseshoe crab hemocytes.";
RL J. Biol. Chem. 270:31008-31015(1995).
RN [2]
RP DOMAINS WD REPEATS.
RX PubMed=12223283; DOI=10.1016/s0304-4165(02)00322-7;
RA Kawabata S., Tsuda R.;
RT "Molecular basis of non-self recognition by the horseshoe crab
RT tachylectins.";
RL Biochim. Biophys. Acta 1572:414-421(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-255.
RX PubMed=10228146; DOI=10.1093/emboj/18.9.2313;
RA Beisel H.G., Kawabata S., Iwanaga S., Huber R., Bode W.;
RT "Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding
RT lectin involved in the innate immunity host defense of the Japanese
RT horseshoe crab Tachypleus tridentatus.";
RL EMBO J. 18:2313-2322(1999).
CC -!- FUNCTION: Lectin that binds specifically to N-acetylglucosamine and N-
CC acetylgalactosamine. Is part of the innate immunity host defense system
CC of the horseshoe crab.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8537358}.
CC Cytoplasmic granule {ECO:0000269|PubMed:8537358}. Note=Stored in large
CC secretory granules of hemocytes and secreted upon stimulation by
CC lipopolysaccharides (LPS).
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DR EMBL; D45909; BAA08313.1; -; mRNA.
DR PIR; PC1320; PC1320.
DR PDB; 1TL2; X-ray; 2.00 A; A=20-255.
DR PDB; 3KIF; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=83-186.
DR PDB; 3KIH; X-ray; 2.49 A; A/B/C/D/E=57-152.
DR PDBsum; 1TL2; -.
DR PDBsum; 3KIF; -.
DR PDBsum; 3KIH; -.
DR AlphaFoldDB; Q27084; -.
DR SMR; Q27084; -.
DR UniLectin; Q27084; -.
DR EvolutionaryTrace; Q27084; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR023294; Tachylectin2.
DR InterPro; IPR036813; Tachylectin2_sf.
DR Pfam; PF14517; Tachylectin; 1.
DR SUPFAM; SSF50934; SSF50934; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Immunity; Innate immunity; Lectin;
KW Repeat; Secreted; Signal; WD repeat.
FT SIGNAL 1..19
FT CHAIN 20..255
FT /note="Tachylectin-2"
FT /id="PRO_0000041404"
FT REPEAT 20..67
FT /note="WD 1"
FT REPEAT 68..114
FT /note="WD 2"
FT REPEAT 115..161
FT /note="WD 3"
FT REPEAT 162..208
FT /note="WD 4"
FT REPEAT 209..255
FT /note="WD 5"
FT VARIANT 148
FT /note="I -> V (in L10A/B)"
FT VARIANT 232
FT /note="H -> Y (in L10A/B)"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3KIH"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1TL2"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1TL2"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1TL2"
SQ SEQUENCE 255 AA; 28881 MW; A5FF0F888A72973B CRC64;
MKFLLVVLGF IGFLKDGITV GGESMLRGVY QDKFYQGTYP QNKNDNWLAR ATLIGKGGWS
NFKFLFLSPG GELYGVLNDK IYKGTPPTHD NDNWMGRAKK IGNGGWNQFQ FLFFDPNGYL
YAVSKDKLYK ASPPQSDTDN WIARATEIGS GGWSGFKFLF FHPNGYLYAV HGQQFYKALP
PVSNQDNWLA RATKIGQGGW DTFKFLFFSS VGTLFGVQGG KFYEDYPPSY AHDNWLARAK
LIGNGGWDDF RFLFF
