ID   SLB_ECHCA               Reviewed;         146 AA.
AC   Q7T247;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Snaclec echicetin subunit beta;
DE   Flags: Precursor;
OS   Echis carinatus (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=40353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF
RP   24-146, AND DISULFIDE BONDS.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=14659748; DOI=10.1016/j.jmb.2003.10.048;
RA   Jasti J., Paramasivam M., Srinivasan A., Singh T.P.;
RT   "Crystal structure of echicetin from Echis carinatus (Indian saw-scaled
RT   viper) at 2.4 A resolution.";
RL   J. Mol. Biol. 335:167-176(2004).
CC   -!- FUNCTION: Binding of echicetin to glycoprotein Ibalpha (GP1BA) receptor
CC       on platelets alone results in inhibition of platelet aggregation, while
CC       binding to both GPIba receptor and IgMk promotes platelet aggregation
CC       and signal transduction. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:14659748}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   -!- CAUTION: The name echicetin has been given to 2 different proteins,
CC       this one from E.carinatus and another one for which the subspecies has
CC       been specified (E.carinatus sochureki). Most experiments have been done
CC       on E.carinatus sochureki. {ECO:0000305}.
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DR   EMBL; AY268948; AAP41219.2; -; mRNA.
DR   PDB; 1OZ7; X-ray; 2.40 A; B=24-146.
DR   PDBsum; 1OZ7; -.
DR   AlphaFoldDB; Q7T247; -.
DR   SMR; Q7T247; -.
DR   EvolutionaryTrace; Q7T247; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..146
FT                   /note="Snaclec echicetin subunit beta"
FT                   /id="PRO_0000355266"
FT   DOMAIN          32..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        98
FT                   /note="Interchain (with C-78 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:14659748"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           70..76
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          119..123
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   TURN            124..127
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:1OZ7"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:1OZ7"
SQ   SEQUENCE   146 AA;  17243 MW;  E2F46A51D6DC6831 CRC64;
     MGRFISVSFG LLVLLLSLSG TGANCLPDWS VYEGYCYKVF KERMNWADAE KFCTKQHKDG
     HLVSFRNSKE VDFVISLAFP MLKNDLVWIG LTDYWRDCNW EWSDGAQLDY KAWDNERHCF
     IYKNTDNQWT RRDCTWTFSF VCKCPA