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