SLA_GLOBR
ID SLA_GLOBR Reviewed; 154 AA.
AC Q9YGN5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Snaclec salmorin subunit A;
DE Flags: Precursor;
OS Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS brevicaudus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=259325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-43, FUNCTION, AND
RP SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10963789; DOI=10.1016/s0049-3848(00)00260-7;
RA Koh Y.-S., Chung K.-H., Kim D.-S.;
RT "Purification and cDNA cloning of salmorin that inhibits fibrinogen
RT clotting.";
RL Thromb. Res. 99:389-398(2000).
CC -!- FUNCTION: Inhibits thrombin-induced fibrinogen clotting and factor Xa-
CC induced prothrombin activation. Binds to thrombin and prothrombin
CC exosites. {ECO:0000269|PubMed:10963789}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000269|PubMed:10963789}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AF125309; AAD18055.1; -; mRNA.
DR AlphaFoldDB; Q9YGN5; -.
DR SMR; Q9YGN5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion 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 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10963789"
FT CHAIN 24..154
FT /note="Snaclec salmorin subunit A"
FT /id="PRO_0000355235"
FT DOMAIN 34..153
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 55..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104
FT /note="Interchain (with C-98 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 154 AA; 17293 MW; 8D06F7DDFA0D140D CRC64;
MGRFIFVSFG LLVVFLSLSG TGADFFCPSG WGSNNGHCYQ AFNQRMTWED AERFCSAQAK
GGHLVSIETR AEADFVAHVV AERIETSFPH VWIGLRDEGK EQQCSSEWSD GSSVSYENWI
EAESKTCLGL ELDSNYHKWV NVYCGQRNPF VCEA
