VM1A_AGKCL
ID VM1A_AGKCL Reviewed; 411 AA.
AC Q92031; C9E1R5;
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 ACLF;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=ACLF-I;
DE AltName: Full=Metalloproteinase VMP-I;
DE Short=AclVMP-I;
DE Flags: Precursor;
GN Name=ACLPREF;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=19799929; DOI=10.1016/j.toxicon.2009.09.016;
RA Jia Y., Perez J.C.;
RT "Molecular cloning and characterization of cDNAs encoding
RT metalloproteinases from snake venom glands.";
RL Toxicon 55:462-469(2010).
RN [3]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10833388; DOI=10.1006/prep.2000.1225;
RA Selistre de Araujo H.S., de Souza E.L., Beltramini L.M., Ownby C.L.,
RA Souza D.H.F.;
RT "Expression, refolding, and activity of a recombinant nonhemorrhagic snake
RT venom metalloprotease.";
RL Protein Expr. Purif. 19:41-47(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12651104; DOI=10.1016/s1046-5928(02)00644-7;
RA Ramos O.H.P., Carmona A.K., Selistre de Araujo H.S.;
RT "Expression, refolding, and in vitro activation of a recombinant snake
RT venom pro-metalloprotease.";
RL Protein Expr. Purif. 28:34-41(2003).
CC -!- FUNCTION: Snake venom zinc metalloprotease that has fibrinolytic
CC activity. The recombinant enzyme cleaves both alpha- and beta-chains of
CC fibrinogen, but not the gamma-chain. The recombinant protein does not
CC produce hemorrhage in mice. Cleaves the peptide substrate Abz-LVEALYQ-
CC EDDnp at the Ala-Leu bond in vitro (PubMed:12651104).
CC {ECO:0000269|PubMed:10833388, ECO:0000269|PubMed:12651104}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline, but not
CC by PMSF. {ECO:0000269|PubMed:10833388, ECO:0000269|PubMed:12651104}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; U18233; AAC59703.1; -; mRNA.
DR EMBL; GQ451436; ACV83930.1; -; mRNA.
DR PIR; S66259; HYSNFA.
DR AlphaFoldDB; Q92031; -.
DR SMR; Q92031; -.
DR MEROPS; M12.133; -.
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; Disulfide bond; Fibrinolytic toxin; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_5000144379"
FT CHAIN 190..411
FT /note="Snake venom metalloproteinase ACLF"
FT /id="PRO_5000144380"
FT DOMAIN 197..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT DISULFID 308..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 348..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 350..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CONFLICT 200
FT /note="E -> G (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="I -> T (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="Y -> H (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
FT CONFLICT 358..359
FT /note="PS -> AA (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="P -> T (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="A -> V (in Ref. 2; ACV83930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46231 MW; 64B45F72BB0298BF CRC64;
MIQVLLVTLC LAAFPYQGSS IILESGNVND YEVVYPRKVT PVPRGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPLVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LELSDSEAHA VYKYENVEKE DEAPKMCGVT QNWESYEPIK
KAFQLNLTPE QQGFPQRYVE LVIVADHRMN TKYNGDSDKI RQWVHQIVNT INEIYRPLNI
RFALVGLEIW SNQDLITVTS VSHDTLASFG NWRETDLLRR QRHDNAQLLT AIDFDGDTVG
LAYVGGMCQL KHSTGVIQDH SAINLLVALT MAHELGHNLG MNHDGNQCHC GANSCVMPSV
LSDQPSKLFS DCSKKDYQTF LPVNNPQCIL NKPLRTDTAS TPVSGNELLE A
