LECM_OXYSU
ID LECM_OXYSU Reviewed; 158 AA.
AC D2YVH7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=C-type lectin mannose-binding isoform;
DE Short=CTL;
DE AltName: Full=Venom C-type lectin mannose-binding isoform 1;
DE Flags: Precursor;
OS Oxyuranus scutellatus (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21115100; DOI=10.1016/j.biochi.2010.11.006;
RA Earl S.T., Robson J., Trabi M., de Jersey J., Masci P.P., Lavin M.F.;
RT "Characterisation of a mannose-binding C-type lectin from Oxyuranus
RT scutellatus snake venom.";
RL Biochimie 93:519-527(2011).
CC -!- FUNCTION: Mannose-binding lectin that binds to and agglutinates rabbit
CC (but not human) erythrocytes in a calcium-dependent manner.
CC {ECO:0000269|PubMed:21115100}.
CC -!- SUBUNIT: Dimer. Probably disulfide-linked homodimer.
CC {ECO:0000269|PubMed:21115100}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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; EF194719; ABP94092.1; -; mRNA.
DR AlphaFoldDB; D2YVH7; -.
DR SMR; D2YVH7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Hemagglutinin; Lectin;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..158
FT /note="C-type lectin mannose-binding isoform"
FT /id="PRO_0000422547"
FT DOMAIN 33..155
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 119..121
FT /note="Mannose-binding"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 54..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 61..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 158 AA; 18345 MW; 9C23B50CEEDA7867 CRC64;
MGRFLLVTLS LLVGAFSLNE ANSCCCPQDW LPKNGFCYKV FNDHKNWNDA EMFCRKFKPG
CHLASIHSNA DSADLAEYVS DYLKSDGNVW IGLNDPRKQR TWVWSDRSPT NYYSWNRGEP
NNSKNNEYCV HLWALSGYLK WNDTPCKALY SFICQCRF
