IOVO_MELGA
ID IOVO_MELGA Reviewed; 185 AA.
AC P68390; P01004;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ovomucoid;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP PROTEIN SEQUENCE.
RA Kato I., Kohr W.J., Laskowski M. Jr.;
RT "Evolution of avian ovomucoids.";
RL (In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.);
RL Regulatory proteolytic enzymes and their inhibitors, pp.197-206, Pergamon
RL Press, New York (1978).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THIRD DOMAIN.
RX PubMed=6750612; DOI=10.1073/pnas.79.16.4868;
RA Fujinaga M., Read R.J., Sielecki A., Ardelt W., Laskowski M. Jr.,
RA James M.N.G.;
RT "Refined crystal structure of the molecular complex of Streptomyces griseus
RT protease B, a serine protease, with the third domain of the ovomucoid
RT inhibitor from turkey.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:4868-4872(1982).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THIRD DOMAIN.
RA Ding J., Qasim M.A., Laskowski M. Jr., James M.N.G.;
RL Submitted (JUL-1997) to the PDB data bank.
RN [4]
RP STRUCTURE BY NMR OF THIRD DOMAIN.
RX PubMed=1753953;
RA Andrianov A.M.;
RT "Conformation of the third domain of turkey ovomucoid in solution.
RT Structural analysis by two-dimensional Overhauser nuclear effect
RT spectroscopy.";
RL Mol. Biol. (Mosk.) 25:1215-1225(1991).
RN [5]
RP STRUCTURE BY NMR OF THIRD DOMAIN.
RX PubMed=8089842; DOI=10.1006/jmbi.1994.1573;
RA Krezel A.M., Darba P., Robertson A.D., Fejzo J., Macura S., Markley J.L.;
RT "Solution structure of turkey ovomucoid third domain as determined from
RT nuclear magnetic resonance data.";
RL J. Mol. Biol. 242:203-214(1994).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: Avian ovomucoid consists of three homologous, tandem Kazal
CC family inhibitory domains.
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DR PIR; A01238; TITKM.
DR PDB; 1CHO; X-ray; 1.80 A; I=130-185.
DR PDB; 1CSO; X-ray; 1.90 A; I=135-185.
DR PDB; 1CT0; X-ray; 1.80 A; I=135-185.
DR PDB; 1CT2; X-ray; 1.65 A; I=135-185.
DR PDB; 1CT4; X-ray; 1.60 A; I=135-185.
DR PDB; 1DS2; X-ray; 1.70 A; I=135-185.
DR PDB; 1DS3; X-ray; 1.65 A; I=135-185.
DR PDB; 1HJA; X-ray; 2.30 A; I=135-185.
DR PDB; 1OMT; NMR; -; A=130-185.
DR PDB; 1OMU; NMR; -; A=130-185.
DR PDB; 1PPF; X-ray; 1.80 A; I=130-185.
DR PDB; 1R0R; X-ray; 1.10 A; I=135-185.
DR PDB; 1SGD; X-ray; 1.80 A; I=135-185.
DR PDB; 1SGE; X-ray; 1.80 A; I=135-185.
DR PDB; 1SGN; X-ray; 1.80 A; I=135-185.
DR PDB; 1SGP; X-ray; 1.40 A; I=135-185.
DR PDB; 1SGQ; X-ray; 1.90 A; I=135-185.
DR PDB; 1SGR; X-ray; 1.80 A; I=135-185.
DR PDB; 1SGY; X-ray; 1.80 A; I=135-185.
DR PDB; 1TUR; NMR; -; A=130-185.
DR PDB; 1TUS; NMR; -; A=130-185.
DR PDB; 1YU6; X-ray; 1.55 A; C/D=1-185.
DR PDB; 1Z7K; X-ray; 1.90 A; B=65-126, C=12-15.
DR PDB; 2GKR; X-ray; 1.16 A; I=135-185.
DR PDB; 2GKT; X-ray; 1.23 A; I=135-185.
DR PDB; 2GKV; X-ray; 1.70 A; A/B=135-185.
DR PDB; 2SGD; X-ray; 1.80 A; I=135-185.
DR PDB; 2SGE; X-ray; 1.80 A; I=135-185.
DR PDB; 2SGF; X-ray; 1.75 A; I=135-185.
DR PDB; 2SGP; X-ray; 1.80 A; I=135-185.
DR PDB; 2SGQ; X-ray; 1.80 A; I=135-185.
DR PDB; 3SGB; X-ray; 1.80 A; I=130-185.
DR PDB; 3SGQ; X-ray; 1.80 A; I=135-185.
DR PDBsum; 1CHO; -.
DR PDBsum; 1CSO; -.
DR PDBsum; 1CT0; -.
DR PDBsum; 1CT2; -.
DR PDBsum; 1CT4; -.
DR PDBsum; 1DS2; -.
DR PDBsum; 1DS3; -.
DR PDBsum; 1HJA; -.
DR PDBsum; 1OMT; -.
DR PDBsum; 1OMU; -.
DR PDBsum; 1PPF; -.
DR PDBsum; 1R0R; -.
DR PDBsum; 1SGD; -.
DR PDBsum; 1SGE; -.
DR PDBsum; 1SGN; -.
DR PDBsum; 1SGP; -.
DR PDBsum; 1SGQ; -.
DR PDBsum; 1SGR; -.
DR PDBsum; 1SGY; -.
DR PDBsum; 1TUR; -.
DR PDBsum; 1TUS; -.
DR PDBsum; 1YU6; -.
DR PDBsum; 1Z7K; -.
DR PDBsum; 2GKR; -.
DR PDBsum; 2GKT; -.
DR PDBsum; 2GKV; -.
DR PDBsum; 2SGD; -.
DR PDBsum; 2SGE; -.
DR PDBsum; 2SGF; -.
DR PDBsum; 2SGP; -.
DR PDBsum; 2SGQ; -.
DR PDBsum; 3SGB; -.
DR PDBsum; 3SGQ; -.
DR AlphaFoldDB; P68390; -.
DR BMRB; P68390; -.
DR SMR; P68390; -.
DR MINT; P68390; -.
DR Allergome; 2116; Mel g 1.
DR MEROPS; I01.001; -.
DR MEROPS; I01.002; -.
DR MEROPS; I01.003; -.
DR EvolutionaryTrace; P68390; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
DR DisProt; DP01011; -.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001239; Prot_inh_Kazal-m.
DR Pfam; PF00050; Kazal_1; 3.
DR PRINTS; PR00290; KAZALINHBTR.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR PROSITE; PS00282; KAZAL_1; 2.
DR PROSITE; PS51465; KAZAL_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..185
FT /note="Ovomucoid"
FT /id="PRO_0000073142"
FT DOMAIN 1..63
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 64..128
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 131..185
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 88..89
FT /note="Reactive bond 2 for trypsin"
FT SITE 147..148
FT /note="Reactive bond 3 for chymotrypsin, elastase,
FT proteases A and B, and subtilisin"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 5..43
FT DISULFID 22..40
FT DISULFID 30..61
FT DISULFID 69..108
FT DISULFID 86..105
FT DISULFID 94..126
FT DISULFID 137..167
FT DISULFID 145..164
FT DISULFID 153..185
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1Z7K"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1Z7K"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1OMT"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1OMT"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1R0R"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1R0R"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1R0R"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:1R0R"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1R0R"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1R0R"
SQ SEQUENCE 185 AA; 20156 MW; 24BB83F5A66A1A76 CRC64;
VEVDCSRFPN TTNEEGKDVL VCTEDLRPIC GTDGVTHSEC LLCAYNIEYG TNISKEHDGE
CREAVPMDCS RYPNTTSEEG KVMILCNKAL NPVCGTDGVT YDNECVLCAH NLEQGTSVGK
KHDGECRKEL AAVSVDCSEY PKPACTLEYR PLCGSDNKTY GNKCNFCNAV VESNGTLTLS
HFGKC
