SLUB_DEIAC
ID SLUB_DEIAC Reviewed; 146 AA.
AC Q8JIW1; Q9IAM0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Snaclec agkisacutacin subunit B;
DE Short=Agk-B;
DE Flags: Precursor;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-50; 59-83; 102-107 AND
RP 112-114, AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10558903; DOI=10.1006/bbrc.1999.1685;
RA Cheng X., Qian Y., Liu Q.D., Li B.X., Zhang M., Liu J.;
RT "Purification, characterization, and cDNA cloning of a new fibrinogenlytic
RT venom protein, Agkisacutacin, from Agkistrodon acutus venom.";
RL Biochem. Biophys. Res. Commun. 265:530-535(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Yu H., Xiang K., Wang Y., Liu J.;
RT "B chain of agkisacutacin from Deinagkistrodon acutus.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=12058182;
RA Cheng X., Xu Z.Y., Liu Q.D., Li X.-M., Li X.Y., Liu J.;
RT "Purification and characterization of a platelet agglutinating inhibiting
RT protein (Agkisacutacin) from Agkistrodon acutus venom.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 32:653-656(2000).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=15925567; DOI=10.1016/j.bbrc.2005.05.033;
RA Li W.-F., Chen L., Li X.-M., Liu J.;
RT "A C-type lectin-like protein from Agkistrodon acutus venom binds to both
RT platelet glycoprotein Ib and coagulation factor IX/factor X.";
RL Biochem. Biophys. Res. Commun. 332:904-912(2005).
CC -!- FUNCTION: Anticoagulant protein which binds to the gamma-
CC carboxyglutamic acid-domain regions of factor IX (F9) and factor X
CC (F10) in the presence of calcium with a 1 to 1 stoichiometry. Also
CC inhibits platelet aggregation by binding to platelet glycoprotein
CC Ibalpha (GP1BA) and functioning as a blocker of von Willebrand factor
CC (VWF). Is devoid of hemorrhagic and lethal activities. Possesses
CC antithrombotic and thrombolytic activities. Also hydrolyzes the Aalpha-
CC chain of fibrinogen (FGA). Does not affect the Bbeta-chain (FGB) and
CC the gamma chain (FGG). {ECO:0000269|PubMed:10558903,
CC ECO:0000269|PubMed:12058182, ECO:0000269|PubMed:15925567}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
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; AF176421; AAF26287.1; -; mRNA.
DR EMBL; AY091756; AAM22785.1; -; mRNA.
DR PIR; JC7135; JC7135.
DR AlphaFoldDB; Q8JIW1; -.
DR SMR; Q8JIW1; -.
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; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10558903"
FT CHAIN 24..146
FT /note="Snaclec agkisacutacin subunit B"
FT /id="PRO_0000346756"
FT DOMAIN 24..146
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 70
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..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 98
FT /note="Interchain (with C-102 in subunit A)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 119..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 28
FT /note="D -> E (in Ref. 2; AAM22785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16726 MW; 7360B6D6864131BB CRC64;
MGRFIFVSFG LLVVFLSLSG TAADCPSDWS SYEGHCYKPF DEPKTWADAE KFCTQQHKGS
HLASFHSSEE ADFVVTLTTP SLKTDLVWIG LKNIWNGCYW KWSDGTKLDY KDWREQFECL
VSRTVNNEWL SMDCGTTCSF VCKFQA
