VM12_CROAD
ID VM12_CROAD Reviewed; 203 AA.
AC P34179;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Snake venom metalloproteinase adamalysin-2;
DE Short=SVMP;
DE EC=3.4.24.46;
DE AltName: Full=Adamalysin II;
DE AltName: Full=Proteinase II;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP PARTIAL PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC TISSUE=Venom;
RX PubMed=8223430; DOI=10.1002/j.1460-2075.1993.tb06099.x;
RA Gomis-Rueth F.-X., Kress L.F., Bode W.;
RT "First structure of a snake venom metalloproteinase: a prototype for matrix
RT metalloproteinases/collagenases.";
RL EMBO J. 12:4151-4157(1993).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC TISSUE=Venom;
RX PubMed=8006965; DOI=10.1006/jmbi.1994.1392;
RA Gomis-Rueth F.-X., Kress L.F., Kellerman J., Mayr I., Lee X., Huber R.,
RA Bode W.;
RT "Refined 2.0 A X-ray crystal structure of the snake venom zinc-
RT endopeptidase adamalysin II. Primary and tertiary structure determination,
RT refinement, molecular structure and comparison with astacin, collagenase
RT and thermolysin.";
RL J. Mol. Biol. 239:513-544(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH AN INHIBITOR.
RX PubMed=9428736; DOI=10.1016/s0014-5793(97)01401-4;
RA Cirilli M., Gallina C., Gavuzzo E., Giordano C., Gomis-Rueth F.-X.,
RA Gorini B., Kress L.F., Mazza F., Paradisi M.P., Pochetti G., Politi V.;
RT "2-A X-ray structure of adamalysin II complexed with a peptide phosphonate
RT inhibitor adopting a retro-binding mode.";
RL FEBS Lett. 418:319-322(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ZINC
RP IONS, AND METAL-BINDING SITES.
RX PubMed=9521103; DOI=10.1002/pro.5560070207;
RA Gomis-Rueth F.-X., Meyer E.F., Kress L.F., Politi V.;
RT "Structures of adamalysin II with peptidic inhibitors. Implications for the
RT design of tumor necrosis factor alpha convertase inhibitors.";
RL Protein Sci. 7:283-292(1998).
CC -!- FUNCTION: Has no significant hemorrhagic activity, but inactivates
CC serpins by limited proteolysis of their reactive-site loops.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 1-Phe-|-Val-2, 5-His-|-Leu-6, 14-Ala-|-Leu-15, 15-
CC Leu-|-Tyr-16, and 16-Tyr-|-Leu-17 of insulin B chain.; EC=3.4.24.46;
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:9521103}.
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 PDB; 1IAG; X-ray; 2.00 A; A=3-203.
DR PDB; 2AIG; X-ray; 2.60 A; P=3-203.
DR PDB; 3AIG; X-ray; 2.80 A; A=3-203.
DR PDB; 4AIG; X-ray; 2.00 A; A=3-203.
DR PDBsum; 1IAG; -.
DR PDBsum; 2AIG; -.
DR PDBsum; 3AIG; -.
DR PDBsum; 4AIG; -.
DR AlphaFoldDB; P34179; -.
DR SMR; P34179; -.
DR MEROPS; M12.141; -.
DR PRIDE; P34179; -.
DR EvolutionaryTrace; P34179; -.
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: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; IPR034027; Reprolysin_adamalysin.
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 Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Zinc.
FT CHAIN 1..203
FT /note="Snake venom metalloproteinase adamalysin-2"
FT /id="PRO_0000078196"
FT DOMAIN 7..203
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9521103"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9521103"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9521103"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9521103"
FT DISULFID 118..198
FT DISULFID 158..165
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1IAG"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1IAG"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1IAG"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1IAG"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:1IAG"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4AIG"
SQ SEQUENCE 203 AA; 23076 MW; DAC61380F3C93E48 CRC64;
QQNLPQRYIE LVVVADRRVF MKYNSDLNII RTRVHEIVNI INGFYRSLNI DVSLVNLEIW
SGQDPLTIQS SSSNTLNSEG LWREKVLLNK KKKDNAQLLT AIEFKCETLG KAYLNSMCNP
RSSVGIVKDH SPINLLVAVT MAHELGHNLG MEHDGKDCLR GASLCIMRPG LTPGRSYEFS
DDSMGYYQKF LNQYKPQCIL NKP
