ID   OVAL_COTCO              Reviewed;         383 AA.
AC   Q6V115;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Ovalbumin;
DE   AltName: Full=Egg albumin;
GN   Name=SERPINB14;
OS   Coturnix coturnix (Common quail) (Tetrao coturnix).
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=9091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen G., Yu X.C., Jiang H.Z., Li M.G.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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; AY354922; AAQ22769.1; -; mRNA.
DR   AlphaFoldDB; Q6V115; -.
DR   SASBDB; Q6V115; -.
DR   SMR; Q6V115; -.
DR   MEROPS; I04.958; -.
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   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; Glycoprotein; Phosphoprotein; Secreted;
KW   Signal.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..383
FT                   /note="Ovalbumin"
FT                   /id="PRO_0000094127"
FT   SIGNAL          22..48
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250"
FT   SITE            353..354
FT                   /note="Reactive bond homolog"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
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   383 AA;  42209 MW;  05C715EDCC0422ED CRC64;
     MGSIGAASME FCFDVFKELK VHHANDNMLY SPFAILSTLA MVFLGAKDST RTQINKVVHF
     DKLPGFGDSI EAQCGTSANV HSSLRDILNQ ITKQNDAYSF SLASRLYAQE TYTVVPEYLQ
     CVKELYRGGL ESVNFQTAAD QARGLINAWV ESQTNGIIRN ILQPSSVDSQ TAMVLVNAIA
     FKGLWEKAFK AEDTQTIPFR VTEQESKPVQ MMHQIGSFKV ASMASEKMKI LELPFASGTM
     SMLVLLPDDV SGLEQLESTI SFEKLTEWTS SSIMEERKVK VYLPRMKMEE KYNLTSLLMA
     MGITDLFSSS ANLSGISSVG SLKIPQAVHA AYAEINEAGR DVVGSAEAGV DATEEFRADH
     PFLFCVKHIE TNAILLFGRC VSP