ID   VMP_TITOB               Reviewed;         370 AA.
AC   A0A1E1WVX2;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Metalloproteinase;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
OS   Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=1221240;
RN   [1] {ECO:0000312|EMBL:JAT91179.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 265-275, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Telson, and Venom;
RX   PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA   de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA   Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA   Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT   "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT   obscurus and T. serrulatus scorpions.";
RL   PLoS ONE 13:e0193739-e0193739(2018).
CC   -!- FUNCTION: Metalloprotease that may disrupt the cell matrix and the
CC       process of clotting blood or hemolymph. {ECO:0000305|PubMed:29561852}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29561852}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29561852}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {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   EMBL; GEMQ01000010; JAT91179.1; -; Transcribed_RNA.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..370
FT                   /note="Metalloproteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5012610735"
FT   DOMAIN          170..370
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   CARBOHYD        226
FT                   /note="N-linked (GalNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   370 AA;  42166 MW;  46E28B0882C4BCBF CRC64;
     MYLAYIFFLF ATVSAIPTGR VEIVFPSVET SRSGMKTVKF RALGEDVELK LEPAGDILAQ
     DFALYNGNQE KQQSVNVESL RRRLYRDSAN GAALLIDDDE QPPSIEGIVF SKLRISPHEW
     KEVTEEGKRA HQVEELTSDR DSYLSDDILI PDFQREMVSF TRIDRNDKCI VIEVLLVTDR
     KFTERCETNE ALTEYVTLLS SVTEALFRQL DSGWQLRLLG IMTFTNETEP PLFEESKHPN
     GAYKPVFVNK INDYFRENPT SLSKNADIIG ILLTRSMRDR MDDWYSFEGL AFGNSVCSGN
     KACAINAYEK AEQAAYNLAH EMAHSLGIFH DGEFYRCVPE EVSEVISCPN SNYIMGYNSG
     DNYGKIFRMF