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IOVO_LOPNY
ID   IOVO_LOPNY              Reviewed;          56 AA.
AC   P67954; P05586;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Ovomucoid;
DE   Flags: Fragment;
OS   Lophura nycthemera (Silver pheasant) (Gennaeus nycthemerus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Lophura.
OX   NCBI_TaxID=9046;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3828298; DOI=10.1021/bi00375a028;
RA   Laskowski M. Jr., Kato I., Ardelt W., Cook J., Denton A., Empie M.W.,
RA   Kohr W.J., Park S.J., Parks K., Schatzley B.L., Schoenberger O.L.,
RA   Tashiro M., Vichot G., Whatley H.E., Wieczorek A., Wieczorek M.;
RT   "Ovomucoid third domains from 100 avian species: isolation, sequences, and
RT   hypervariability of enzyme-inhibitor contact residues.";
RL   Biochemistry 26:202-221(1987).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=3971987; DOI=10.1111/j.1432-1033.1985.tb08762.x;
RA   Bode W., Epp O., Huber R., Laskowski M. Jr., Ardelt W.;
RT   "The crystal and molecular structure of the third domain of silver pheasant
RT   ovomucoid (OMSVP3).";
RL   Eur. J. Biochem. 147:387-395(1985).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=1870129; DOI=10.1016/0022-2836(91)90114-l;
RA   Musil D., Bode W., Huber R., Laskowski M. Jr., Lin T.-Y., Ardelt W.;
RT   "Refined X-ray crystal structures of the reactive site modified ovomucoid
RT   inhibitor third domains from silver pheasant (OMSVP3*) and from Japanese
RT   quail (OMJPQ3*).";
RL   J. Mol. Biol. 220:739-755(1991).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: Avian ovomucoid consists of three homologous, tandem Kazal
CC       family inhibitory domains.
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DR   PDB; 1IY5; NMR; -; A=3-56.
DR   PDB; 1IY6; NMR; -; A=3-56.
DR   PDB; 2OVO; X-ray; 1.50 A; A=1-56.
DR   PDB; 4OVO; X-ray; 2.50 A; A=1-56.
DR   PDBsum; 1IY5; -.
DR   PDBsum; 1IY6; -.
DR   PDBsum; 2OVO; -.
DR   PDBsum; 4OVO; -.
DR   AlphaFoldDB; P67954; -.
DR   SMR; P67954; -.
DR   EvolutionaryTrace; P67954; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001239; Prot_inh_Kazal-m.
DR   Pfam; PF00050; Kazal_1; 1.
DR   PRINTS; PR00290; KAZALINHBTR.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Repeat; Secreted; Serine protease inhibitor.
FT   CHAIN           <1..>56
FT                   /note="Ovomucoid"
FT                   /id="PRO_0000073138"
FT   DOMAIN          6..56
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            18..19
FT                   /note="Reactive bond 3"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        8..38
FT   DISULFID        16..35
FT   DISULFID        24..56
FT   NON_TER         1
FT   NON_TER         56
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:2OVO"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:1IY5"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:2OVO"
FT   HELIX           34..43
FT                   /evidence="ECO:0007829|PDB:2OVO"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:2OVO"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:2OVO"
SQ   SEQUENCE   56 AA;  6039 MW;  D3D5BE5E3081CE4E CRC64;
     LAAVSVDCSE YPKPACTMEY RPLCGSDNKT YGNKCNFCNA VVESNGTLTL SHFGKC
 
 
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