SLAA_DEIAC
ID SLAA_DEIAC Reviewed; 152 AA.
AC Q9DEF9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Snaclec anticoagulant protein subunit A;
DE Short=AaACP-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], AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12175618; DOI=10.1016/s0041-0101(01)00289-6;
RA Tani A., Ogawa T., Nose T., Nikandrov N.N., Deshimaru M., Chijiwa T.,
RA Chang C.C., Fukumaki Y., Ohno M.;
RT "Characterization, primary structure and molecular evolution of
RT anticoagulant protein from Agkistrodon actus venom.";
RL Toxicon 40:803-813(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-152, METAL-BINDING SITES, AND
RP 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 and factor X in the
CC presence of calcium with a 1 to 1 stoichiometry. Also inhibits platelet
CC aggregation by binding to platelet glycoprotein Ibalpha (GP1BA) and
CC functioning as a blocker of vWF. Is devoid of hemorrhagic and lethal
CC activities. Possesses antithrombotic and thrombolytic activities. Also
CC hydrolyzes the Aalpha-chain of fibrinogen. Does not affect the Bbeta-
CC chain and the gamma chain (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12175618}.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000269|Ref.2}.
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; AB036880; BAA99281.1; -; mRNA.
DR PIR; JC7134; JC7134.
DR PDB; 1Y17; X-ray; 2.40 A; A=24-152.
DR PDBsum; 1Y17; -.
DR AlphaFoldDB; Q9DEF9; -.
DR SMR; Q9DEF9; -.
DR EvolutionaryTrace; Q9DEF9; -.
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 Disulfide bond; Hemostasis impairing toxin; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..152
FT /note="Snaclec anticoagulant protein subunit A"
FT /id="PRO_5000049504"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|Ref.2"
FT DISULFID 53..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|Ref.2"
FT DISULFID 102
FT /note="Interchain (with C-98 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|Ref.2"
FT DISULFID 125..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|Ref.2"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:1Y17"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1Y17"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1Y17"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1Y17"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1Y17"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1Y17"
SQ SEQUENCE 152 AA; 17124 MW; 5C59C0F503A4D223 CRC64;
MGRFIFVSFG LLVVYLSLSG TAADCSSSWS SYEGHCYKAF KQSKTWADAE SFCTKQVNGG
HLVSIESSGE ADFVAHLIAQ KIKSAKIHVW IGLRAQNKEK QCSIEWSDGS SISYENWIEE
ESKKCLGVHK ATGFRKWENF YCEQRDPFVC EA
