ID   LECM2_BITAR             Reviewed;         148 AA.
AC   Q6X5T4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=C-type lectin 2;
DE            Short=CTL-2;
DE   Flags: Precursor;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=14557069; DOI=10.1016/s0378-1119(03)00716-9;
RA   Harrison R.A., Oliver J., Hasson S.S., Bharati K., Theakston R.D.G.;
RT   "Novel sequences encoding venom C-type lectins are conserved in
RT   phylogenetically and geographically distinct Echis and Bitis viper
RT   species.";
RL   Gene 315:95-102(2003).
CC   -!- FUNCTION: Mannose-binding lectin which recognizes specific carbohydrate
CC       structures and agglutinates a variety of animal cells by binding to
CC       cell-surface glycoproteins and glycolipids. May be a calcium-dependent
CC       lectin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR   EMBL; AY254326; AAQ01207.1; -; mRNA.
DR   AlphaFoldDB; Q6X5T4; -.
DR   SMR; Q6X5T4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Lectin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..148
FT                   /note="C-type lectin 2"
FT                   /id="PRO_0000355244"
FT   DOMAIN          34..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           118..120
FT                   /note="Mannose-binding"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        100
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   148 AA;  17232 MW;  7BA753DE38FC9D76 CRC64;
     MGRFIFVSFG LLVVFLSLSG IGADQECLPG WSFYEGHCYK VFDEYKNWTD AEQYCTEQEN
     GGHLVSFHNR EEVDFVVKLG YTILKADIVW IGLRDFWREC HWGWSNGAQL DYKGWNDEPN
     CFIAYTVGNK WLRRKCSSTQ QFVCKSPA