ID   VMPA1_MESMA             Reviewed;         393 AA.
AC   U6BLN5;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Venom metalloproteinase BumaMPs1 {ECO:0000303|PubMed:24125658};
DE            Short=MPs1 {ECO:0000305|PubMed:24125658};
DE            EC=3.4.24.- {ECO:0000305};
DE   AltName: Full=Acid trehalase {ECO:0000312|EMBL:AHA36326.1};
DE   Flags: Precursor;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1] {ECO:0000312|EMBL:AHA36326.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=24125658; DOI=10.1016/j.toxicon.2013.10.006;
RA   Xia X., Ma Y., Xue S., Wang A., Tao J., Zhao Y., Zhang Q., Liu R., Lu S.;
RT   "Cloning and molecular characterization of BumaMPs1, a novel
RT   metalloproteinases from the venom of scorpion Buthus martensi Karsch.";
RL   Toxicon 76:234-238(2013).
CC   -!- FUNCTION: Metalloprotease. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00276};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24125658}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:24125658}.
CC   -!- PTM: Contains several disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   EMBL; KF492696; AHA36326.1; -; mRNA.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..393
FT                   /note="Venom metalloproteinase BumaMPs1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5012407113"
FT   DOMAIN          167..377
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   REGION          378..393
FT                   /note="Disintegrin-like domain"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   393 AA;  44399 MW;  2F640BD0458FEB8E CRC64;
     MFVHLLVLLF AAVEAIPTGR FEVVYPSMVT FRSGIKRIRF RALDEDIELR LEPAGDVIAD
     DFTVINGENG EVDHSVNIQS LKRKLYKDAK VGAALHIDED GSLIINGIVN SKLRIEPDTS
     KKASRNGIIA HRVIEVIEDE QLFHDVIILP PGLTRTFNYS EPLPDDKCVK IEYVFVTESS
     FTKSFQISSM ETYLANMMNM VKIMFDSLDL GIEVAIIGII KLTKENEAKL APYIPLCSRE
     MDSRETLDDM AEFYCNSADK LIQNADIVTL ITTRPLGTFD ENGYFFNIHL GIAFLDNICV
     YCYKYAIVKE DTGIYQLANT VAHESAHLLG CDHDGEKGSL DCSARDGYIM SWNNEKIGKK
     FSPCCKKRVE ELITRRKINH CIVETCDGKR KRN