OVAL_COTJA
ID OVAL_COTJA Reviewed; 383 AA.
AC P19104;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ovalbumin;
DE AltName: Full=Egg albumin;
GN Name=SERPINB14;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
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=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=2216734; DOI=10.1093/nar/18.18.5553;
RA Mucha J., Klaudiny J., Klaudinyova V., Hanes J., Simuth J.;
RT "The sequence of Japanese quail ovalbumin cDNA.";
RL Nucleic Acids Res. 18:5553-5553(1990).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53964; CAA37916.1; -; mRNA.
DR PIR; S11433; S11433.
DR AlphaFoldDB; P19104; -.
DR SMR; P19104; -.
DR MEROPS; I04.958; -.
DR Proteomes; UP000694412; 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 2: Evidence at transcript level;
KW Acetylation; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..383
FT /note="Ovalbumin"
FT /id="PRO_0000094128"
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; 42239 MW; B07241E0AB60C96E CRC64;
MGSIGAASME FCFDVFKELK VHHANDNMLY SPFAILSTLA MVFLGAKDST RTQINKVVHF
DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKQNDAYSF SLASRLYAQE TYTVVPEYLQ
CVKELYRGGL ESVNFQTAAD QARGLINAWV ESQTNGIIRN ILQPSSVDSQ TAMVLVNAIA
FKGLWEKAFK AEDTQTIPFR VTEQESKPVQ MMYQIGSFKV ASMASEKMKI LELPFASGTM
SMLVLLPDDV SGLEQLESII SFEKLTEWTS SSIMEERKVK VYLPRMKMEE KYNLTSLLMA
MGITDLFSSS ANLSGISSVG SLKISQAVHA AHAEINEAGR DVVGSAEAGV DATEEFRADH
PFLFCVKHIE TNAILLFGRC VSP
