VM1T1_PROMU
ID VM1T1_PROMU Reviewed; 202 AA.
AC U3KRG1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Snake venom metalloproteinase TM-1 {ECO:0000303|PubMed:23732127, ECO:0000303|PubMed:8193588};
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Zinc-dependent metalloproteinase;
OS Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=103944;
RN [1] {ECO:0000312|PDB:4J4M}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH
RP ZINC, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=23732127; DOI=10.1016/j.toxicon.2013.05.009;
RA Chou T.L., Wu C.H., Huang K.F., Wang A.H.;
RT "Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase
RT providing new insights into the inhibition by endogenous tripeptide
RT inhibitors.";
RL Toxicon 71:140-146(2013).
RN [2]
RP PROTEIN SEQUENCE OF 45-59, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Venom;
RX PubMed=7488093; DOI=10.1006/bbrc.1995.2614;
RA Huang K.F., Hung C.C., Pan F.M., Chow L.P., Tsugita A., Chiou S.H.;
RT "Characterization of multiple metalloproteinases with fibrinogenolytic
RT activity from the venom of Taiwan habu (Trimeresurus mucrosquamatus):
RT protein microsequencing coupled with cDNA sequence analysis.";
RL Biochem. Biophys. Res. Commun. 216:223-233(1995).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, PYROGLUTAMATE FORMATION AT GLN-1,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8193588;
RA Huang K.-F., Hung C.C., Chiou S.-H.;
RT "Characterization of three fibrinogenolytic proteases isolated from the
RT venom of Taiwan habu (Trimeresurus mucrosquamatus).";
RL Biochem. Mol. Biol. Int. 31:1041-1050(1993).
RN [4]
RP ACTIVITY REGULATION.
RX PubMed=9703966; DOI=10.1006/bbrc.1998.9017;
RA Huang K.F., Hung C.C., Wu S.H., Chiou S.H.;
RT "Characterization of three endogenous peptide inhibitors for multiple
RT metalloproteinases with fibrinogenolytic activity from the venom of Taiwan
RT habu (Trimeresurus mucrosquamatus).";
RL Biochem. Biophys. Res. Commun. 248:562-568(1998).
CC -!- FUNCTION: Potent fibrinogenolytic protease which cleaves mainly the
CC Aalpha (FGA) and Bbeta (FGB) chains of fibrinogen and slightly the
CC gamma chain (FGG) (PubMed:8193588, PubMed:7488093). Shows preference
CC for substrates having a moderate-size and hydrophobic residue at the
CC P1' position. Preferentially cleaves Ala-|-Leu and Tyr-|-Leu bonds
CC (PubMed:23732127). Is more susceptible to tripeptide inhibitors than
CC TM-3 (AC O57413) (PubMed:9703966). {ECO:0000269|PubMed:23732127,
CC ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588,
CC ECO:0000269|PubMed:9703966}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:23732127};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23732127};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline
CC (PubMed:8193588). Is also inhibited by endogenous tripeptide inhibitors
CC pyroGlu-Asn-Trp, pyroGlu-Gln-Trp, and pyroGlu-Lys-Trp (PubMed:9703966).
CC {ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7488093,
CC ECO:0000269|PubMed:8193588}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7488093,
CC ECO:0000269|PubMed:8193588}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7488093, ECO:0000305|PubMed:8193588}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7488093}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:23732127}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR PDB; 4J4M; X-ray; 1.80 A; A/B=1-202.
DR PDBsum; 4J4M; -.
DR AlphaFoldDB; U3KRG1; -.
DR SMR; U3KRG1; -.
DR MEROPS; M12.155; -.
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; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Pyrrolidone carboxylic acid;
KW Secreted; Zinc.
FT CHAIN 1..202
FT /note="Snake venom metalloproteinase TM-1"
FT /id="PRO_0000448286"
FT DOMAIN 7..202
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255"
FT ACT_SITE 144
FT /evidence="ECO:0000305|PubMed:23732127"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:4J4M"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:4J4M"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:4J4M"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:7488093,
FT ECO:0000305|PubMed:8193588"
FT DISULFID 118..197
FT /evidence="ECO:0000269|PubMed:23732127,
FT ECO:0007744|PDB:4J4M"
FT DISULFID 159..181
FT /evidence="ECO:0000269|PubMed:23732127,
FT ECO:0007744|PDB:4J4M"
FT DISULFID 161..164
FT /evidence="ECO:0000269|PubMed:23732127,
FT ECO:0007744|PDB:4J4M"
FT CONFLICT 46
FT /note="S -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4J4M"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4J4M"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:4J4M"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4J4M"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4J4M"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4J4M"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:4J4M"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:4J4M"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:4J4M"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4J4M"
SQ SEQUENCE 202 AA; 21791 MW; 17A8A521FC2DC9A6 CRC64;
QQRFPQRYVM LAIVADHGMV TKYSGNSSAI TTRVHQMVSH VTEMYSPLNI ATTLSLLRIW
SSKDLITVQS DSSVTLGSFG DWRKVVLLSQ QAHDCAFLNT ATALDDSTIG LAYSNGMCDP
KFSVGLVQDH SSNVFMVAVT MTHELGHNLG MAHDEAGGCA CSSCIMSPAA SSGPSKLFSD
CSKDDYQTFL TNTNPQCILN AP
