SLB_ECHCA
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