ID   OVALY_CHICK             Reviewed;         388 AA.
AC   P01014;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ovalbumin-related protein Y;
DE   AltName: Full=Gene Y protein;
GN   Name=SERPINB14B; Synonyms=Y;
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 [GENOMIC DNA].
RX   PubMed=7122240; DOI=10.1093/nar/10.14.4363;
RA   Heilig R., Muraskowsky R., Kloepfer C., Mandel J.-L.;
RT   "The ovalbumin gene family: complete sequence and structure of the Y
RT   gene.";
RL   Nucleic Acids Res. 10:4363-4382(1982).
RN   [2]
RP   PROTEIN SEQUENCE OF 10-21; 20-48; 56-86; 105-124; 110-124; 123-137;
RP   143-153; 186-196; 229-256; 353-373; 362-373 AND 372-385, TISSUE
RP   SPECIFICITY, INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Egg white {ECO:0000303|PubMed:25436390};
RX   PubMed=25436390; DOI=10.1021/jf504469t;
RA   Kim J., Choi Y.H.;
RT   "Differential abundance of egg white proteins in laying hens treated with
RT   corticosterone.";
RL   J. Agric. Food Chem. 62:12346-12359(2014).
RN   [3]
RP   PROTEIN SEQUENCE OF 56-63 AND 156-164, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, AND BLOCKAGE OF N-TERMINUS.
RC   TISSUE=Egg white;
RX   PubMed=16428832; DOI=10.1271/bbb.70.144;
RA   Hirose J., Doi Y., Kitabatake N., Narita H.;
RT   "Ovalbumin-related gene Y protein bears carbohydrate chains of the
RT   ovomucoid type.";
RL   Biosci. Biotechnol. Biochem. 70:144-151(2006).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16428832}.
CC   -!- TISSUE SPECIFICITY: Major protein of egg white (PubMed:25436390,
CC       PubMed:16428832). Expressed in the magnum of the oviduct (at protein
CC       level) (PubMed:25436390). {ECO:0000269|PubMed:16428832,
CC       ECO:0000269|PubMed:25436390}.
CC   -!- INDUCTION: Down-regulated by dietary stress. Decreased expression at
CC       day 14 in the magnum of the oviduct in the corticosterone-fed laying
CC       hens. {ECO:0000269|PubMed:25436390}.
CC   -!- PTM: N-glycosylated on at least two Asn residues by ovomucoid type
CC       carbohydrate units. {ECO:0000269|PubMed:16428832}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J00922; AAA68882.1; -; Genomic_DNA.
DR   PIR; A01244; DYCH.
DR   RefSeq; NP_001026172.1; NM_001031001.1.
DR   AlphaFoldDB; P01014; -.
DR   SMR; P01014; -.
DR   STRING; 9031.ENSGALP00000020967; -.
DR   MEROPS; I04.958; -.
DR   PaxDb; P01014; -.
DR   GeneID; 420897; -.
DR   KEGG; gga:420897; -.
DR   CTD; 420897; -.
DR   VEuPathDB; HostDB:geneid_420897; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; P01014; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; P01014; -.
DR   PRO; PR:P01014; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; PTHR11461; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; SSF56574; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Proteoglycan;
KW   Reference proteome; Secreted.
FT   CHAIN           1..388
FT                   /note="Ovalbumin-related protein Y"
FT                   /id="PRO_0000094131"
FT   SITE            353..354
FT                   /note="Reactive bond homolog"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..121
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43772 MW;  2AF17BF715D7F461 CRC64;
     MDSISVTNAK FCFDVFNEMK VHHVNENILY CPLSILTALA MVYLGARGNT ESQMKKVLHF
     DSITGAGSTT DSQCGSSEYV HNLFKELLSE ITRPNATYSL EIADKLYVDK TFSVLPEYLS
     CARKFYTGGV EEVNFKTAAE EARQLINSWV EKETNGQIKD LLVSSSIDFG TTMVFINTIY
     FKGIWKIAFN TEDTREMPFS MTKEESKPVQ MMCMNNSFNV ATLPAEKMKI LELPYASGDL
     SMLVLLPDEV SGLERIEKTI NFDKLREWTS TNAMAKKSMK VYLPRMKIEE KYNLTSILMA
     LGMTDLFSRS ANLTGISSVD NLMISDAVHG VFMEVNEEGT EATGSTGAIG NIKHSLELEE
     FRADHPFLFF IRYNPTNAIL FFGRYWSP