VM1AA_DEIAC
ID VM1AA_DEIAC Reviewed; 413 AA.
AC Q9PW35;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Snake venom metalloproteinase acutolysin-A;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Hemorrhagin I;
DE Short=HI;
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].
RC TISSUE=Venom gland;
RX PubMed=10482389; DOI=10.1016/s0041-0101(99)00102-6;
RA Liu Q., Xu W., Cheng X., Jin G., Shen X., Luo H., Liu J.;
RT "Molecular cloning and sequence analysis of cDNA encoding haemorrhagic
RT toxin acutolysin A from Agkistrodon acutus.";
RL Toxicon 37:1539-1548(1999).
RN [2]
RP PROTEIN SEQUENCE OF 188-200.
RC TISSUE=Venom;
RA Gong W., Zhu X., Niu L., Teng M., Wang C., Shen W.;
RT "Preliminary amino acid sequence of Agkistrodon acutus hemorrhagin I.";
RL J. China Univ. Sci. Tech. 26:366-368(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 197-388 IN COMPLEX WITH ZINC ION
RP AND CALCIUM ION.
RC TISSUE=Venom;
RX PubMed=9784374; DOI=10.1006/jmbi.1998.2110;
RA Gong W., Zhu X., Liu S., Teng M., Niu L.;
RT "Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc
RT metalloproteinase from the snake venom of Agkistrodon acutus.";
RL J. Mol. Biol. 283:657-668(1998).
CC -!- FUNCTION: This protein is a zinc metalloprotease from snake venom that
CC possesses hemorrhagic activity.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9784374}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; AF174392; AAD51824.1; -; mRNA.
DR PDB; 1BSW; X-ray; 1.95 A; A=191-388.
DR PDB; 1BUD; X-ray; 1.90 A; A=191-388.
DR PDBsum; 1BSW; -.
DR PDBsum; 1BUD; -.
DR AlphaFoldDB; Q9PW35; -.
DR SMR; Q9PW35; -.
DR MEROPS; M12.131; -.
DR EvolutionaryTrace; Q9PW35; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; TAS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; TAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /note="Activation peptide"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000028950"
FT CHAIN 188..390
FT /note="Snake venom metalloproteinase acutolysin-A"
FT /id="PRO_0000028951"
FT PROPEP 391..413
FT /id="PRO_0000028952"
FT DOMAIN 193..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT DISULFID 304..385
FT DISULFID 344..369
FT DISULFID 346..352
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1BUD"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 213..232
FT /evidence="ECO:0007829|PDB:1BUD"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1BUD"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1BUD"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:1BUD"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1BUD"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1BUD"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1BUD"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:1BUD"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1BUD"
SQ SEQUENCE 413 AA; 46565 MW; AF43854C3A25AFA3 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQQK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSKD YSEIHYSPDG RRITTHPLVE DHCYYRGHIR NDADSTASIS
ACNGLKGHFK LQGEMYLIEP MKMSYSEAHA VYKYGNVEKE DEAPKMCGVT QNWESYEPIK
KASQLIVSTE FQRYMEIVIV VDHSMVKKYN GDSDKIKAWV YEMINTITES YSYLYIDIIL
SGLEIWSEKD LINVETSAEN TLKSFGEWRA KDLIHRISHD NAQLLTATDF DGPTIGLAYV
ASMCDPKRSV GVVQDHSSVN RLVAITLAHE MAHNLGVRHD EGSCSCGSGY TCIMSPVINS
EVIKYFSDCS YIQCREYISK ENPPCILNKP LRTDTVSTPV SGNELLEAGK DYD
