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P01012 (OVAL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ovalbumin
Alternative name(s):
Allergen Gal d II
Egg albumin
Plakalbumin
Allergen=Gal d 2
Gene names
Name:SERPINB14
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-inhibitory serpin. Storage protein of egg white. Ref.11 Ref.12

Subunit structure

Homodimer. Ref.18

Subcellular location

Secreted Ref.11.

Tissue specificity

Major protein of egg white.

Domain

The uncleaved signal peptide becomes available for membrane translocation of ovalbumin when the nascent chain is 50 to 60 residues long. The hydrophobic sequence, which lies between residues 27 and 43, folds back on the preceding residues to form an amphipathic hairpin structure which is the signal element recognized by the membrane.

Unlike other serpins, after protease cleavage at the P-P' site, ovalbumin does not have the ability to undergo the conformational transition into the loop-inserted reactive-center-containing thermostabilized form. The bulky arginine residue (Arg-340) at the hinge region appears to be responsible for this lack of loop-inserted conformational change, but not for the absence of serpin inhibitory activity.

During storage of fertilized and non-fertilized eggs or under alkaline conditions, the native ovalbumin conformer (N-ovalbumin) is transformed into a thermostabilized conformer, S-ovalbumin. Ser-165, Ser-237 and Ser-321 take on a D-configuration in this conformer and may be responsible for the thermostability.

Post-translational modification

Undergoes proteolytic cleavage first at the canonical P1-P1' site, and then at the P8-P7 site by subtilisin.

Allergenic properties

Can cause an allergic reaction in humans.

Sequence similarities

Belongs to the serpin family. Ov-serpin subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 386385Ovalbumin
PRO_0000094126
Signal peptide22 – 4827Not cleaved

Sites

Metal binding1921Calcium
Site353 – 3542Cleavage; by elastase or subtilisin
Site359 – 3602Cleavage; by subtilisin

Amino acid modifications

Modified residue21N-acetylglycine Ref.6 Ref.7
Modified residue691Phosphoserine Ref.9
Modified residue3451Phosphoserine Ref.9
Glycosylation2931N-linked (GlcNAc...) Ref.13 Ref.18
Disulfide bond74 ↔ 121 Ref.15 Ref.18

Natural variations

Natural variant2831L → F in strain: Mangyondak. Ref.4
Natural variant3121N → D in a minor component.

Experimental info

Mutagenesis741C → A: Lower thermal denaturation temperature, more susceptible to elastase or subtilisin cleavage and assumes a native-like conformation on alkaline treatment; when associated with or without A-121. Ref.15
Mutagenesis1211C → A: Lower thermal denaturation temperature, more susceptible to elastase or subtilisin cleavage and assumes a native-like conformation on alkaline treatment; when associated with or without A-74. Ref.15
Mutagenesis3401R → T: Significantly more thermostabilized following cleavage at P-P' site. Inserts reactive loop at very slow rate. No inhibitory action against serine proteinases. Ref.10
Sequence conflict51G → A in CAA23681. Ref.5
Sequence conflict1191L → F in CAA23681. Ref.5
Sequence conflict1881A → T in CAA23682. Ref.1

Secondary structure

....................................................................... 386
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01012 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 87179F028B20CEF2

FASTA38642,881
        10         20         30         40         50         60 
MGSIGAASME FCFDVFKELK VHHANENIFY CPIAIMSALA MVYLGAKDST RTQINKVVRF 

        70         80         90        100        110        120 
DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF SLASRLYAEE RYPILPEYLQ 

       130        140        150        160        170        180 
CVKELYRGGL EPINFQTAAD QARELINSWV ESQTNGIIRN VLQPSSVDSQ TAMVLVNAIV 

       190        200        210        220        230        240 
FKGLWEKAFK DEDTQAMPFR VTEQESKPVQ MMYQIGLFRV ASMASEKMKI LELPFASGTM 

       250        260        270        280        290        300 
SMLVLLPDEV SGLEQLESII NFEKLTEWTS SNVMEERKIK VYLPRMKMEE KYNLTSVLMA 

       310        320        330        340        350        360 
MGITDVFSSS ANLSGISSAE SLKISQAVHA AHAEINEAGR EVVGSAEAGV DAASVSEEFR 

       370        380 
ADHPFLFCIK HIATNAVLFF GRCVSP 

« Hide

References

[1]"Sequence of chicken ovalbumin mRNA."
McReynolds L., O'Malley B.W., Nisbet A.D., Fothergill J.E., Givol D., Fields S., Robertson M., Brownlee G.G.
Nature 273:723-728(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence homology at 12 intron-exon junctions in the chick ovalbumin gene."
Catterall J.F., O'Malley B.W., Robertson M.A., Staden R., Tanaka Y., Brownlee G.G.
Nature 275:510-513(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete nucleotide sequence of the chicken chromosomal ovalbumin gene and its biological significance."
Woo S.L.C., Beattie W.G., Catterall J.F., Dugaiczyk A., Staden R., Brownlee G.G., O'Malley B.W.
Biochemistry 20:6437-6446(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Ovalbumin from the chicken called Mangyondak in North Korea."
Kim R., Rim D., Li Y.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-283.
Strain: Mangyondak.
[5]"Sequence of three introns in the chick ovalbumin gene."
Robertson M.A., Staden R., Tanaka Y., Catterall J.F., O'Malley B.W., Brownlee G.G.
Nature 278:370-372(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
[6]"A correction and extension of the acetylated amino terminal sequence of ovalbumin."
Thompson E.O.P., Fisher W.K.
Aust. J. Biol. Sci. 31:443-446(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-17, ACETYLATION AT GLY-2.
[7]"Ovalbumin: a secreted protein without a transient hydrophobic leader sequence."
Palmiter R.D., Gagnon J., Walsh K.A.
Proc. Natl. Acad. Sci. U.S.A. 75:94-98(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-36, ACETYLATION AT GLY-2.
[8]"Amino acid sequences containing half-cystine residues in ovalbumin."
Thompson E.O.P., Fisher W.K.
Aust. J. Biol. Sci. 31:433-442(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-17; 30-36; 61-79; 116-124; 367-374 AND 380-386.
[9]"Sequences of sixteen phosphoserine peptides from ovalbumins of eight species."
Henderson J.Y., Moir A.J.G., Fothergill L.A., Fothergill J.E.
Eur. J. Biochem. 114:439-450(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 60-85 AND 338-360, PHOSPHORYLATION AT SER-69 AND SER-345.
[10]"Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop."
Arii Y., Hirose M.
Biochem. J. 363:403-409(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 354-359, PROTEOLYTIC CLEAVAGE AT ALA-353 AND PHE-359, MUTAGENESIS OF ARG-340.
[11]"The signal sequence of ovalbumin is located near the NH2 terminus."
Meek R.L., Walsh K.A., Palmiter R.D.
J. Biol. Chem. 257:12245-12251(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF UNCLEAVED SIGNAL PEPTIDE, SUBCELLULAR LOCATION.
[12]"Isolation and properties of the signal region from ovalbumin."
Robinson A., Meredith C., Austen B.M.
FEBS Lett. 203:243-246(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF UNCLEAVED SIGNAL PEPTIDE.
[13]"Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities."
Thaysen-Andersen M., Mysling S., Hojrup P.
Anal. Chem. 81:3933-3943(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-293.
[14]"Thermostabilization of ovalbumin by alkaline treatment: Examination of the possible roles of D-serine residues."
Ishimaru T., Ito K., Tanaka M., Matsudomi N.
Protein Sci. 19:1205-1212(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: THERMOSTABILITY OF N- AND S-CONFORMERS.
[15]"The role of the disulfide bridge in the stability and structural integrity of ovalbumin evaluated by site-directed mutagenesis."
Ishimaru T., Ito K., Tanaka M., Tanaka S., Matsudomi N.
Biosci. Biotechnol. Biochem. 75:544-549(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-74 AND CYS-121.
[16]"Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. Its relationship to the structure of cleaved alpha-1-proteinase inhibitor."
Wright H.T., Qian H.X., Huber R.
J. Mol. Biol. 213:513-528(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[17]"Crystal structure of ovalbumin as a model for the reactive centre of serpins."
Stein P.E., Leslie A.G.W., Finch J.T., Turnell W.G., McLaughlin P.J., Carrell R.W.
Nature 347:99-102(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[18]"Crystal structure of uncleaved ovalbumin at 1.95-A resolution."
Stein P.E., Leslie A.G.W., Finch J.T., Carrell R.W.
J. Mol. Biol. 221:941-959(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), METAL-BINDING, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-293.
[19]"Loop-inserted and thermostabilized structure of P1-P1' cleaved ovalbumin mutant R339T."
Yamasaki M., Arii Y., Mikami B., Hirose M.
J. Mol. Biol. 315:113-120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-385 OF MUTANT THR-340, PROTEOLYTIC CLEAVAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00383 mRNA. Translation: CAA23682.1.
M34352 expand/collapse EMBL AC list , M34346, M34347, M34348, M34349, M34350, M34351 Genomic DNA. Translation: AAA48998.1.
V00438 Genomic DNA. Translation: CAA23716.1.
J00895 Genomic DNA. Translation: AAB59956.1.
AY223553 mRNA. Translation: AAO43266.1.
V00382 Genomic DNA. Translation: CAA23681.1.
PIROACH. A90455.
RefSeqNP_990483.1. NM_205152.2.
UniGeneGga.623.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JTIX-ray2.30A/B2-385[»]
1OVAX-ray1.95A/B/C/D2-386[»]
1P1ZX-ray3.26P258-265[»]
1P4LX-ray2.90P258-265[»]
1UHGX-ray1.90A/B/C/D2-385[»]
1VACX-ray2.50P258-265[»]
3CVHX-ray2.90C/O258-265[»]
3P9LX-ray2.00C/F258-265[»]
3P9MX-ray2.00C/F258-265[»]
3PABX-ray2.20C/F259-265[»]
4HKJX-ray3.00C/G/K/O258-265[»]
ProteinModelPortalP01012.
SMRP01012. Positions 2-386.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075085.

Protein family/group databases

Allergome3292. Gal d 2.0101.
360. Gal d 2.
MEROPSI04.958.

PTM databases

UniCarbKBP01012.

Proteomic databases

PaxDbP01012.
PRIDEP01012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000037195; ENSGALP00000036403; ENSGALG00000012869.
GeneID396058.
KEGGgga:396058.

Organism-specific databases

CTD396058.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00740000114938.
HOGENOMHOG000238519.
HOVERGENHBG005957.
InParanoidP01012.
OMAHHANENI.
OrthoDBEOG7327PB.
PhylomeDBP01012.
TreeFamTF352619.

Enzyme and pathway databases

ReactomeREACT_102124. Immune System.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01012.
NextBio20816118.
PROP01012.

Entry information

Entry nameOVAL_CHICK
AccessionPrimary (citable) accession number: P01012
Secondary accession number(s): Q804A4, Q90741
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries