IOVO_COTJA
ID IOVO_COTJA Reviewed; 186 AA.
AC P01003;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ovomucoid;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE.
RA Kato I., Schrode J., Wilson K.A., Laskowski M. Jr.;
RL (In) Peeters H. (eds.);
RL Protides of the biological fluids, Proc. 23th colloquium, pp.235-243,
RL Pergamon Press, New York (1976).
RN [2]
RP SEQUENCE REVISION TO 64-67; 140 AND 158.
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 [3]
RP PROTEIN SEQUENCE OF 131-186.
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 [4]
RP VARIANT GLY-162.
RX PubMed=6771272; DOI=10.1016/s0021-9258(18)43606-x;
RA Bogard W.C. Jr., Kato I., Laskowski M. Jr.;
RT "A Ser162/Gly162 polymorphism in Japanese quail ovomucoid.";
RL J. Biol. Chem. 255:6569-6574(1980).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THIRD DOMAIN.
RX PubMed=6752426; DOI=10.1016/0022-2836(82)90212-1;
RA Papamokos E., Weber E., Bode W., Huber R., Empie M.W., Kato I.,
RA Laskowski M. Jr.;
RT "Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type
RT inhibitor, and model building studies of complexes with serine proteases.";
RL J. Mol. Biol. 158:515-537(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF THIRD DOMAIN.
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).
RN [7]
RP STRUCTURE BY NMR OF 131-186.
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. The first domain does not inhibit any tested
CC protease. Domains 2 and 3 inhibit trypsin.
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 PIR; B94430; TIQJM.
DR PDB; 1OVO; X-ray; 1.90 A; A/B/C/D=131-186.
DR PDB; 3OVO; X-ray; 1.55 A; A=131-186.
DR PDBsum; 1OVO; -.
DR PDBsum; 3OVO; -.
DR AlphaFoldDB; P01003; -.
DR BMRB; P01003; -.
DR SMR; P01003; -.
DR MEROPS; I01.001; -.
DR MEROPS; I01.002; -.
DR MEROPS; I01.003; -.
DR EvolutionaryTrace; P01003; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 3.
DR PRINTS; PR00290; KAZALINHBTR.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR PROSITE; PS00282; KAZAL_1; 3.
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..186
FT /note="Ovomucoid"
FT /id="PRO_0000073087"
FT DOMAIN 1..64
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 65..129
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 132..186
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 89..90
FT /note="Reactive bond 2 for trypsin"
FT SITE 148..149
FT /note="Reactive bond 3 for trypsin"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 5..44
FT DISULFID 22..41
FT DISULFID 30..62
FT DISULFID 70..109
FT DISULFID 87..106
FT DISULFID 95..127
FT DISULFID 138..168
FT DISULFID 146..165
FT DISULFID 154..186
FT VARIANT 162
FT /note="S -> G"
FT /evidence="ECO:0000269|PubMed:6771272"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1OVO"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3OVO"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3OVO"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:3OVO"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3OVO"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:3OVO"
SQ SEQUENCE 186 AA; 20477 MW; F2B25AE1A185A72E CRC64;
VEVDCSRFPN TTNEEGKDEV VCPDELRLIC GTDGVTYNHE CMLCFYNKEY GTNISKEQDG
ECGETVPMDC SRYPNTTSED GKVTILCTKD FSFVCGTDGV TYDNECMLCA HNVVQGTSVG
KKHDGECRKE LAAVSVDCSE YPKPACPKDY RPVCGSDNKT YSNKCNFCNA VVESNGTLTL
NHFGKC
