SLUA_DEIAC
ID SLUA_DEIAC Reviewed; 152 AA.
AC Q9IAM1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Snaclec agkisacutacin subunit A;
DE Short=Agk-A;
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 24-53; 84-94 AND 125-152,
RP HETERODIMER WITH AGKISACUTACIN-B, 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 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 [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-152 IN DIMER WITH AAACP,
RP METAL-BINDING SITES, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=11404471; DOI=10.1073/pnas.131179698;
RA Mizuno H., Fujimoto Z., Atoda H., Morita T.;
RT "Crystal structure of an anticoagulant protein in complex with the Gla
RT domain of factor X.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7230-7234(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 24-152 IN DIMER WITH AAACP,
RP METAL-BINDING SITES, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RA Zhu Z., Liu S., Mo X., Yu X., Liang Z., Zang J., Zhao W., Teng M., Niu L.;
RT "Characterizations and crystal structures of two snake venom proteins with
RT the activity of binding coagulation factor X from Agkistrodon acutus.";
RL Submitted (NOV-2004) to the PDB data bank.
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. 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 with subunit B of AaACP or agkisacutacin;
CC disulfide-linked. {ECO:0000269|PubMed:11404471, ECO:0000269|Ref.5}.
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; AF176420; AAF26286.2; -; mRNA.
DR PIR; JC7134; JC7134.
DR PDB; 1IOD; X-ray; 2.30 A; A=24-152.
DR PDB; 1WT9; X-ray; 2.01 A; A=24-152.
DR PDBsum; 1IOD; -.
DR PDBsum; 1WT9; -.
DR AlphaFoldDB; Q9IAM1; -.
DR SMR; Q9IAM1; -.
DR EvolutionaryTrace; Q9IAM1; -.
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 3D-structure; 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..152
FT /note="Snaclec agkisacutacin subunit A"
FT /id="PRO_0000346755"
FT DOMAIN 24..152
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 BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 25..36
FT DISULFID 53..150
FT DISULFID 102
FT /note="Interchain (with C-98 in subunit B)"
FT DISULFID 125..142
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1WT9"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1WT9"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1WT9"
SQ SEQUENCE 152 AA; 17109 MW; 76A0F636DBF0D7AB CRC64;
MGRFIFVSFG LLVVFLSLSG TAADCSSGWS SYEGHCYKVF KQSKTWTDAE SFCTKQVNGG
HLVSIESSGE ADFVGQLIAQ KIKSAKIHVW IGLRAQNKEK QCSIEWSDGS SISYENWIEE
ESKKCLGVHI ETGFHKWENF YCEQQDPFVC EA
