VM1T2_PROFL
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 03-AUG-2022, entry version 115.
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}.
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DR PIR; JU0037; HYTV2.
DR PDB; 1WNI; X-ray; 2.20 A; A=1-201.
DR PDBsum; 1WNI; -.
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: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; 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..84
FT /evidence="ECO:0007829|PDB:1WNI"
FT HELIX 86..89
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
