ID   IOVO_CHICK              Reviewed;         210 AA.
AC   P01005;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Ovomucoid;
DE   AltName: Full=Allergen Gal d I;
DE   AltName: Allergen=Gal d 1;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7430252; DOI=10.1083/jcb.87.2.480;
RA   Catterall J.F., Stein J.P., Kristo P., Means A.R., O'Malley B.W.;
RT   "Primary sequence of ovomucoid messenger RNA as determined from cloned
RT   complementary DNA.";
RL   J. Cell Biol. 87:480-487(1980).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-210.
RX   PubMed=3548816; DOI=10.1021/bi00375a027;
RA   Kato I., Schrode J., Kohr W.J., Laskowski M. Jr.;
RT   "Chicken ovomucoid: determination of its amino acid sequence, determination
RT   of the trypsin reactive site, and preparation of all three of its
RT   domains.";
RL   Biochemistry 26:193-201(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-44 (PRECURSOR PROTEIN).
RX   PubMed=721826; DOI=10.1016/s0021-9258(17)34279-5;
RA   Thibodeau S.N., Palmiter R.D., Walsh K.A.;
RT   "Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal
RT   extension.";
RL   J. Biol. Chem. 253:9018-9023(1978).
RN   [4]
RP   GLYCOSYLATION AT ASN-77 AND ASN-199, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15253437; DOI=10.1021/pr034112b;
RA   Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.;
RT   "A new strategy for identification of N-glycosylated proteins and
RT   unambiguous assignment of their glycosylation sites using HILIC enrichment
RT   and partial deglycosylation.";
RL   J. Proteome Res. 3:556-566(2004).
RN   [5]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23075397; DOI=10.1111/febs.12033;
RA   Derache C., Epinette C., Roussel A., Gabant G., Cadene M., Korkmaz B.,
RA   Gauthier F., Kellenberger C.;
RT   "Crystal structure of greglin, a novel non-classical Kazal inhibitor, in
RT   complex with subtilisin.";
RL   FEBS J. 279:4466-4478(2012).
CC   -!- FUNCTION: Serine protease inhibitor. Inhibits trypsin.
CC       {ECO:0000269|PubMed:23075397}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         No decrease in activity observed after incubating at pH 2.5 and pH
CC         7.4 for 1 hour. Retains 20% activity after incubation at pH 12 for 1
CC         hour. {ECO:0000269|PubMed:23075397};
CC       Temperature dependence:
CC         No decrease in activity observed after heating for 1 hour at up to 80
CC         degrees Celsius. Retains 20% activity after incubation at 95 degrees
CC         Celsius for 1 hour. {ECO:0000269|PubMed:23075397};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: Avian ovomucoid consists of three homologous, tandem Kazal
CC       family inhibitory domains.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
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DR   EMBL; J00902; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A92754; TICHM.
DR   RefSeq; NP_001295423.1; NM_001308494.1.
DR   RefSeq; XP_015149249.1; XM_015293763.1.
DR   AlphaFoldDB; P01005; -.
DR   SMR; P01005; -.
DR   STRING; 9031.ENSGALP00000005544; -.
DR   Allergome; 3291; Gal d 1.0101.
DR   Allergome; 359; Gal d 1.
DR   MEROPS; I01.001; -.
DR   MEROPS; I01.002; -.
DR   MEROPS; I01.003; -.
DR   GlyConnect; 479; 44 N-Linked glycans.
DR   iPTMnet; P01005; -.
DR   GeneID; 416236; -.
DR   KEGG; gga:416236; -.
DR   CTD; 84651; -.
DR   VEuPathDB; HostDB:geneid_416236; -.
DR   HOGENOM; CLU_087965_0_0_1; -.
DR   InParanoid; P01005; -.
DR   OMA; DVSPVCG; -.
DR   OrthoDB; 76386at2759; -.
DR   PhylomeDB; P01005; -.
DR   TreeFam; TF352550; -.
DR   PRO; PR:P01005; -.
DR   Proteomes; UP000000539; Chromosome 13.
DR   Bgee; ENSGALG00000003512; Expressed in lung and 2 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR   GO; GO:0005615; C:extracellular space; TAS:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:AgBase.
DR   GO; GO:0019863; F:IgE binding; IDA:AgBase.
DR   GO; GO:0019864; F:IgG binding; IMP:AgBase.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
DR   GO; GO:0048545; P:response to steroid hormone; TAS:AgBase.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   CDD; cd01327; KAZAL_PSTI; 1.
DR   Gene3D; 3.30.60.30; -; 3.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   PANTHER; PTHR47499; SERINE PROTEASE INHIBITOR KAZAL-TYPE 7 SPINK7; 1.
DR   PANTHER; PTHR47499:SF2; SERINE PROTEASE INHIBITOR KAZAL-TYPE 9; 1.
DR   Pfam; PF00050; Kazal_1; 3.
DR   SMART; SM00280; KAZAL; 3.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 3.
DR   PROSITE; PS00282; KAZAL_1; 3.
DR   PROSITE; PS51465; KAZAL_2; 3.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Reference proteome; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:3548816"
FT   CHAIN           25..210
FT                   /note="Ovomucoid"
FT                   /id="PRO_0000016579"
FT   DOMAIN          25..88
FT                   /note="Kazal-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          89..153
FT                   /note="Kazal-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          156..210
FT                   /note="Kazal-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            48..49
FT                   /note="Reactive bond 1 for endoproteinase Lys-C"
FT   SITE            113..114
FT                   /note="Reactive bond 2 for trypsin"
FT   SITE            172..173
FT                   /note="Reactive bond 3"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15253437"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine; partial"
FT                   /evidence="ECO:0000269|PubMed:15253437"
FT   DISULFID        29..68
FT   DISULFID        46..65
FT   DISULFID        54..86
FT   DISULFID        94..133
FT   DISULFID        111..130
FT   DISULFID        119..151
FT   DISULFID        162..192
FT   DISULFID        170..189
FT   DISULFID        178..210
FT   VARIANT         158..159
FT                   /note="Missing (due to an ambiguous intron excision)"
FT   CONFLICT        62
FT                   /note="T -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="D -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="M -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="G -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  22591 MW;  8BE9516B6D38ACF9 CRC64;
     MAMAGVFVLF SFVLCGFLPD AAFGAEVDCS RFPNATDKEG KDVLVCNKDL RPICGTDGVT
     YTNDCLLCAY SIEFGTNISK EHDGECKETV PMNCSSYANT TSEDGKVMVL CNRAFNPVCG
     TDGVTYDNEC LLCAHKVEQG ASVDKRHDGG CRKELAAVSV DCSEYPKPDC TAEDRPLCGS
     DNKTYGNKCN FCNAVVESNG TLTLSHFGKC
//