SLA_TRIST
ID SLA_TRIST Reviewed; 152 AA.
AC Q71RR4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit A;
DE Short=IX/X-bp subunit A;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Lee W.-H., Liu H., Zhang Y.;
RT "Cloning and characterization of C-type lectins from Trimeresurus
RT stejnegeri venom.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Anticoagulant protein which binds to the gamma-
CC carboxyglutamic acid-domain regions of factors IX (F9) and factor X
CC (F10) in the presence of calcium with a 1 to 1 stoichiometry.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Calcium is required for ligand binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AF354911; AAQ15153.1; -; mRNA.
DR AlphaFoldDB; Q71RR4; -.
DR SMR; Q71RR4; -.
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 2: Evidence at transcript level;
KW Blood coagulation cascade inhibiting toxin; Calcium; Disulfide bond;
KW Hemostasis impairing toxin; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..152
FT /note="Snaclec coagulation factor IX/factor X-binding
FT protein subunit A"
FT /id="PRO_0000355311"
FT DOMAIN 32..151
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 25..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 53..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 102
FT /note="Interchain (with C-98 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 152 AA; 17092 MW; 2E355C53C01E243A CRC64;
MGRFIFVSFG LLVVAASLSG TGADCLSGWS SYEGHCYKAF ELYKTWEDAE SFCMEGVKGG
HLVSIESSGE ADFVAQLISE NMKRLDFFVW IGLRVQGDEK QCNSEWSDGS SVSYENWIES
ESKTCLGLEQ QTKFRKWVNL YCGQRIPFVC EA
