SL9B_ECHCA
ID SL9B_ECHCA Reviewed; 125 AA.
AC Q9PSM8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Snaclec coagulation factor IX/factor X-binding protein subunit B;
DE Short=IX/X-BP subunit B;
DE AltName: Full=ECLV IX/X-BP subunit B;
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 PROTEIN SEQUENCE, FUNCTION, DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=8611513; DOI=10.1021/bi952520q;
RA Chen Y.L., Tsai I.H.;
RT "Functional and sequence characterization of coagulation factor IX/factor
RT X-binding protein from the venom of Echis carinatus leucogaster.";
RL Biochemistry 35:5264-5271(1996).
CC -!- FUNCTION: Anticoagulant protein which binds to coagulation factor IX
CC (F9) and coagulation factor X (F10) in the presence of calcium. It may
CC bind the gamma-carboxyglutamic acid-domain regions of factors with a 1
CC to 1 stoichiometry. The dissociation constant (K(d)) are 6.6 nM for
CC factor IX (F9) and 125 nM for factor X (F10). Does not bind
CC carbohydrates. {ECO:0000269|PubMed:8611513}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000269|PubMed:8611513}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8611513}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:8611513}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR AlphaFoldDB; Q9PSM8; -.
DR SMR; Q9PSM8; -.
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; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Metal-binding; Secreted; Toxin.
FT CHAIN 1..125
FT /note="Snaclec coagulation factor IX/factor X-binding
FT protein subunit B"
FT /id="PRO_0000415606"
FT DOMAIN 1..122
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 2..13
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8611513"
FT DISULFID 30..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8611513"
FT DISULFID 75
FT /note="Interchain (with C-81 in subunit A)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8611513"
FT DISULFID 97..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8611513"
SQ SEQUENCE 125 AA; 14372 MW; EDFEC2E49686CDD6 CRC64;
DCSSGWTAYG KHCYKVFDEP KTWEDAEKFC SEQANGGHLV SFRSSKEADF VVTLTAQTKE
SEIVWMGLSK IWNQCDWGWT NGAKLNYEAW AEAESYCVWF SSTNKEWKSR PCSLFGHFVC
KSPAW