VM1AH_AGKCL
ID VM1AH_AGKCL Reviewed; 407 AA.
AC Q92032;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Snake venom metalloproteinase ACLH;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=ACL hemorrhagic toxin I;
DE Short=ACLH-I;
DE Short=ACLHT-I;
DE AltName: Full=Hemorrhagic metalloproteinase ACLH;
DE Flags: Precursor;
OS Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon
OS mokasen laticinctus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX NCBI_TaxID=37195;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7793974; DOI=10.1006/abbi.1995.1352;
RA Selistre de Araujo H.S., Ownby C.L.;
RT "Molecular cloning and sequence analysis of cDNAs for metalloproteinases
RT from broad-banded copperhead Agkistrodon contortrix laticinctus.";
RL Arch. Biochem. Biophys. 320:141-148(1995).
RN [2]
RP PROTEIN SEQUENCE OF 188-208, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8444323; DOI=10.1016/0020-711x(93)90016-8;
RA Johnson E.K., Ownby C.L.;
RT "Isolation of a hemorrhagic toxin from the venom of Agkistrodon contortrix
RT laticinctus (broad-banded copperhead) and pathogenesis of the hemorrhage
RT induced by the toxin in mice.";
RL Int. J. Biochem. 25:267-278(1993).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=11072042; DOI=10.1016/s0041-0101(00)00188-4;
RA Salvini T.F., Belluzzo S.S., Selistre de Araujo H.S., Souza D.H.S.;
RT "Regeneration and change of muscle fiber types after injury induced by a
RT hemorrhagic fraction isolated from Agkistrodon contortrix laticinctus
RT venom.";
RL Toxicon 39:641-649(2001).
RN [4]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=15313443; DOI=10.1016/j.cca.2004.04.004;
RA Garcia L.T., Parreiras e Silva L.T., Ramos O.H.P., Carmona A.K.,
RA Bersanetti P.A., Selistre de Araujo H.S.;
RT "The effect of post-translational modifications on the hemorrhagic activity
RT of snake venom metalloproteinases.";
RL Comp. Biochem. Physiol. 138C:23-32(2004).
CC -!- FUNCTION: This zinc hemorrhagic metalloproteinase has
CC fibrino(geno)lytic activities. It causes hemorrhage and has myonecrotic
CC activity on both fiber types I and II. The recombinant enzyme, without
CC post-translational modifications, also has proteolytic activity, but
CC does not show any hemorrhagic activity. {ECO:0000269|PubMed:11072042,
CC ECO:0000269|PubMed:15313443, ECO:0000269|PubMed:8444323}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Contains sialic acid terminally alpha(2-6)-linked to galactose in
CC a complex N-glycan chain. {ECO:0000269|PubMed:15313443}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR EMBL; U18234; AAC59704.1; -; mRNA.
DR PIR; S66260; S66260.
DR AlphaFoldDB; Q92032; -.
DR SMR; Q92032; -.
DR MEROPS; M12.160; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Fibrinogenolytic toxin; Fibrinolytic toxin; Glycoprotein;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Myotoxin; Protease; Secreted; Sialic acid; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /evidence="ECO:0000269|PubMed:8444323"
FT /id="PRO_5000144381"
FT CHAIN 188..407
FT /note="Snake venom metalloproteinase ACLH"
FT /id="PRO_5000144382"
FT DOMAIN 193..389
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 /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 304..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 344..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 346..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 407 AA; 46109 MW; 954D8D1AC38F3205 CRC64;
MIQVLLVTLC LAAFPYQGSS IILESGNVND YEVVYPRKVT PVPKGAVQPK YEDAMQYELK
VNGEPVVLHL ERNKGLFSKD YSETHYSPDG RKITTYPPVE DHCYYHGRIQ NDADSIASIS
ACNGLKGHFK LQGEMYLIEP LELSDSEAHA VFKYENVEKE DEAPKICGVT QNWESYEPIK
KASQLNLNYQ YQRYVELVTV VDHGMYTKYN GDSDKIRQWV HQMVNTMKES YRYMYIDISL
AGVEIWSNKD LIDVQPAARH TLDSFGEWRE RDLLHRISHD NAQLLTSTDF DGPTIGLAYV
GTMCDPKLST GVVEDHSKIN FLVAVTMAHE MGHNLGMRHD TGSCSCGGYS CIMSPVISDD
SPKYFSNCSY IQCWDFIMKE NPQCILNKPL RTDTVSTPVS GDELLEA
