ID   IOVO_CARRE              Reviewed;          54 AA.
AC   P05616;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Ovomucoid;
DE   Flags: Fragment;
OS   Carpococcyx renauldi (Coral-billed ground-cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Carpococcyx.
OX   NCBI_TaxID=8943;
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).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: Avian ovomucoid consists of three homologous, tandem Kazal
CC       family inhibitory domains.
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DR   PIR; A31438; A31438.
DR   AlphaFoldDB; P05616; -.
DR   SMR; P05616; -.
DR   iPTMnet; P05616; -.
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   Pfam; PF00050; Kazal_1; 1.
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   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Repeat; Secreted; Serine protease inhibitor.
FT   CHAIN           <1..>54
FT                   /note="Ovomucoid"
FT                   /id="PRO_0000073076"
FT   DOMAIN          4..54
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            16..17
FT                   /note="Reactive bond 3"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3828298"
FT   DISULFID        6..36
FT   DISULFID        14..33
FT   DISULFID        22..54
FT   NON_TER         1
FT   NON_TER         54
SQ   SEQUENCE   54 AA;  5934 MW;  41069E8CD2FC906E CRC64;
     IATVDCSDYP KPVCTLEDMP LCGSDNITYH NKCYFCNAVA HSNGTLTFSH FGKC