ID   OVAL_MELGA              Reviewed;         386 AA.
AC   O73860;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Ovalbumin;
DE   AltName: Full=Egg albumin;
GN   Name=SERPINB14;
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   NUCLEOTIDE SEQUENCE [MRNA].
RA   Roberts M.C., Butt A.T., Schenkel E.F., Wong E.A.;
RT   "Turkey ovalbumin cDNA.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 60-85 AND 339-360, AND PHOSPHORYLATION AT SER-69 AND
RP   SER-345.
RX   PubMed=6783411; DOI=10.1111/j.1432-1033.1981.tb05165.x;
RA   Henderson J.Y., Moir A.J.G., Fothergill L.A., Fothergill J.E.;
RT   "Sequences of sixteen phosphoserine peptides from ovalbumins of eight
RT   species.";
RL   Eur. J. Biochem. 114:439-450(1981).
CC   -!- FUNCTION: Storage protein of egg white. Lack protease inhibitory
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Major protein of egg white.
CC   -!- PTM: The signal sequence is not cleaved. The functional signal for
CC       membrane translocation of ovalbumin becomes accessible when the nascent
CC       chain is 50 to 60 residues long. The hydrophobic sequence which lies
CC       between residues 27 and 43 folds back on the preceding residues to form
CC       an amphipathic hairpin structure which is the signal element recognized
CC       by the membrane (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF064546; AAC16664.1; -; mRNA.
DR   RefSeq; NP_001290119.1; NM_001303190.1.
DR   AlphaFoldDB; O73860; -.
DR   SMR; O73860; -.
DR   Allergome; 2115; Mel g 2.
DR   MEROPS; I04.958; -.
DR   iPTMnet; O73860; -.
DR   GeneID; 100303699; -.
DR   KEGG; mgp:100303699; -.
DR   CTD; 569051; -.
DR   InParanoid; O73860; -.
DR   PRO; PR:O73860; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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   Acetylation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..386
FT                   /note="Ovalbumin"
FT                   /id="PRO_0000094129"
FT   SIGNAL          22..48
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250"
FT   SITE            353..354
FT                   /note="Reactive bond homolog"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:6783411"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:6783411"
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   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..121
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  42988 MW;  0B09E86D036BEDD3 CRC64;
     MGSIGAVSME FCFDVFKELK VHHANENIFY SPFTIISALA MVYLGAKDST RTQINKVVRF
     DKLPGFGDSV EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF SLASRLYAEE TYPILPEYLQ
     CVKELYRGGL ESINFQTAAD QARGLINSWV ESQTNGMIKN VLQPSSVDSQ TAMVLVNAIV
     FKGLWEKAFK DEDTQAIPFR VTEQESKPVQ MMYQIGLFKV ASMASEKMKI LELPFASGTM
     SMWVLLPDEV SGLEQLETTI SFEKMTEWIS SNIMEERRIK VYLPRMKMEE KYNLTSVLMA
     MGITDLFSSS ANLSGISSAG SLKISQAAHA AYAEIYEAGR EVIGSAEAGA DATSVSEEFR
     VDHPFLYCIK HNLTNSILFF GRCISP