ID   DM43_DIDMR              Reviewed;         291 AA.
AC   P82957;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Venom metalloproteinase inhibitor DM43;
OS   Didelphis marsupialis (Southern opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX   NCBI_TaxID=9268;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND GLYCOSYLATION AT ASN-23; ASN-156;
RP   ASN-160 AND ASN-175.
RC   TISSUE=Serum;
RX   PubMed=11815628; DOI=10.1074/jbc.m200589200;
RA   Neves-Ferreira A.G.C., Perales J., Fox J.W., Shannon J.D., Makino D.L.,
RA   Garratt R.C., Domont G.B.;
RT   "Structural and functional analyses of DM43, a snake venom
RT   metalloproteinase inhibitor from Didelphis marsupialis serum.";
RL   J. Biol. Chem. 277:13129-13137(2002).
CC   -!- FUNCTION: Metalloproteinase inhibitor.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Blood and milk.
CC   -!- PTM: N-glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=42691; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11815628};
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DR   AlphaFoldDB; P82957; -.
DR   SMR; P82957; -.
DR   MEROPS; I43.001; -.
DR   iPTMnet; P82957; -.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Repeat.
FT   CHAIN           1..291
FT                   /note="Venom metalloproteinase inhibitor DM43"
FT                   /id="PRO_0000072680"
FT   DOMAIN          22..79
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          114..171
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          191..288
FT                   /note="Ig-like V-type 3"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11815628"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11815628"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11815628"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11815628"
FT   DISULFID        28..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        121..163
FT   DISULFID        213..265
SQ   SEQUENCE   291 AA;  32390 MW;  17A496227E69A65B CRC64;
     LKAMDPTPPL WIKTESPSTP WTNVTLLCVA TNTEELSFQV WKDGELLSTL PVVGLVGKFW
     LGPVTADNRG IYRCRILTSE NDWTPLSAPV EVTGKEPLPA PSLHAEPGPW ILPGLETKLH
     CRGMLLGMIF DLYQEGEQEP VKSSQTPSAE ATFIVNSTGN YSCLYRAPAS APSVNSTPSE
     TIHVVIPDFL PKANFYILND RDFRPGDIVT FSCWARFSER EYDLEFKLFK DGQETPVEVV
     PISDPMKVFF DLTAVGPKDG GKYSCRYRFR NGPPIWSEDS NVLELDLSTG Q