LECG_BOTAT
ID LECG_BOTAT Reviewed; 77 AA.
AC P0DM53;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=C-type lectin galatrox;
DE Short=CTL;
DE Flags: Fragments;
OS Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8725;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, AND SUBUNIT.
RC STRAIN=Northern Brazil; TISSUE=Venom;
RX PubMed=21297119; DOI=10.1093/abbs/gmr003;
RA Mendonca-Franqueiro Ede P., Alves-Paiva Rde M., Sartim M.A., Callejon D.R.,
RA Paiva H.H., Antonucci G.A., Rosa J.C., Cintra A.C., Franco J.J.,
RA Arantes E.C., Dias-Baruffi M., Sampaio S.V.;
RT "Isolation, functional, and partial biochemical characterization of
RT galatrox, an acidic lectin from Bothrops atrox snake venom.";
RL Acta Biochim. Biophys. Sin. 43:181-192(2011).
CC -!- FUNCTION: Lectin that displays hemagglutinating activity on all types
CC of trypsinized human erythrocytes (A+, B+, AB+, and O+), with a higher
CC sensitivity to AB+ type. Is inhibited by different carbohydrates with
CC alpha-lactose displaying the most potent ability to block agglutination
CC (followed by D-fucose, D-galactose, D-rhamnose, D-mannose, and D-
CC sucrose). Is also inhibited by EDTA and pretreatment with heat. In
CC addition, it induces significant cell death in HL-60 cells in a dose-
CC dependent manner, with an IC(50) close to 250 ug/ml. Is a calcium-
CC dependent lectin. {ECO:0000269|PubMed:21297119}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:21297119}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=16264.09; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21297119};
CC -!- MISCELLANEOUS: In contrast to B.atrox venom, does not induce edema in
CC mouse paw nor does it induce mast cell degranulation (tested on RBL-2H3
CC cell line). Has no significant effect on plasma coagulation in vitro
CC nor does it induce platelet aggregation (PubMed:21297119).
CC {ECO:0000305|PubMed:21297119}.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DM53; -.
DR SMR; P0DM53; -.
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; IPR016187; CTDL_fold.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin;
KW Metal-binding; Secreted.
FT CHAIN 1..>77
FT /note="C-type lectin galatrox"
FT /id="PRO_0000423034"
FT DOMAIN 10..>77
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 3..14
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 31..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 38..?
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT UNSURE 67
FT /note="Assigned by comparison with orthologs"
FT NON_CONS 54..55
FT /evidence="ECO:0000305"
FT NON_TER 77
SQ SEQUENCE 77 AA; 9243 MW; BA7EDEEA2E4BB6E1 CRC64;
NNCPQDWLPM NGLCYKIFDE LKAWKDAEMF CRKYKPGCHL ASIILYGESP EWAEGHSEVW
LGLWDKKKDF SWEWTDR
