ID VM1T2_PROFL Reviewed; 201 AA. AC P20165; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 3. DT 02-SEP-2026, entry version 121. DE RecName: Full=Snake venom metalloproteinase trimerelysin-2; DE Short=SVMP; DE EC=3.4.24.53; DE AltName: Full=H2 metalloproteinase; DE Short=H2-proteinase; DE AltName: Full=Trimerelysin II; OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops. OX NCBI_TaxID=88087; RN [1] RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND DISULFIDE BONDS. RC TISSUE=Venom; RX PubMed=2777746; DOI=10.1093/oxfordjournals.jbchem.a122805; RA Takeya H., Arakawa M., Miyata T., Iwanaga S., Omori-Satoh T.; RT "Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, RT isolated from the venom of the habu snake, Trimeresurus flavoviridis."; RL J. Biochem. 106:151-157(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS, RP METAL-BINDING SITES, AND DISULFIDE BONDS. RX PubMed=8907175; DOI=10.1093/oxfordjournals.jbchem.a021215; RA Kumasaka T., Yamamoto M., Moriyama H., Tanaka N., Sato M., Katsube Y., RA Yamakawa Y., Omori-Satoh T., Iwanaga S., Ueki T.; RT "Crystal structure of H2-proteinase from the venom of Trimeresurus RT flavoviridis."; RL J. Biochem. 119:49-57(1996). CC -!- FUNCTION: Major venom non-hemorrhagic metalloproteinase. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 CC in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a CC small molecule substrate of microbial collagenase.; EC=3.4.24.53; 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 -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; JU0037; HYTV2. DR PDB; 1WNI; X-ray; 2.20 A; A=1-201. DR AlphaFoldDB; P20165; -. DR SMR; P20165; -. DR MEROPS; M12.155; -. DR EvolutionaryTrace; P20165; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR FunFam; 3.40.390.10:FF:000002; Disintegrin and metalloproteinase domain-containing protein 22; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR034027; Reprolysin_adamalysin. DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1. DR PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1. DR Pfam; PF01421; Reprolysin; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR PDBsum; 1WNI; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Metal-binding; Metalloprotease; Protease; KW Pyrrolidone carboxylic acid; Secreted; Zinc. FT CHAIN 1..201 FT /note="Snake venom metalloproteinase trimerelysin-2" FT /id="PRO_0000078195" FT DOMAIN 6..201 FT /note="Peptidase M12B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276" FT ACT_SITE 143 FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT BINDING 152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT MOD_RES 1 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:2777746" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 117..196 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, FT ECO:0000269|PubMed:2777746" FT DISULFID 158..180 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, FT ECO:0000269|PubMed:2777746" FT DISULFID 160..163 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, FT ECO:0000269|PubMed:2777746" FT STRAND 6..14 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 16..21 FT /evidence="ECO:0007829|PDB:1WNI" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 26..44 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:1WNI" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 71..81 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 82..86 FT /evidence="ECO:0007829|PDB:1WNI" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1WNI" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1WNI" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:1WNI" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 133..147 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1WNI" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 179..192 FT /evidence="ECO:0007829|PDB:1WNI" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:1WNI" SQ SEQUENCE 201 AA; 23014 MW; 31DFA648717ADC10 CRC64; QRFPQRYIEL AIVVDHGMYK KYNQNSDKIK VRVHQMVNHI NEMYRPLNIA ISLNRLQIWS KKDLITVKSA SNVTLESFGN WRETVLLKQQ NNDCAHLLTA TNLNDNTIGL AYKKGMCNPK LSVGLVQDYS PNVFMVAVTM THELGHNLGM EHDDKDKCKC EACIMSDVIS DKPSKLFSDC SKNDYQTFLT KYNPQCILNA P //