Reviewed, UniProtKB/Swiss-Prot P01012 (OVAL_CHICK)

Names and origin

Protein names

Recommended name:
    Ovalbumin
Alternative name(s):
    Egg albumin
    Plakalbumin
    Allergen Gal d II
    Allergen=Gal d 2

Gene names

Name:

SERPINB14

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Storage protein of egg white. Lack protease inhibitory activity.
Subcellular location	Secreted.
Tissue specificity	Major protein of egg white.
Post-translational modification	The signal sequence is not cleaved. The functional signal for membrane translocation of ovalbumin becomes accessible 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.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Belongs to the serpin family. Ov-serpin subfamily.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Allergen
Domain	Signal
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 386

385

Ovalbumin

PRO_0000094126

Signal peptide

22 – 48

27

Not cleaved

Sites

Site

353 – 354

2

Reactive bond homolog

Amino acid modifications

Modified residue

2

1

N-acetylglycine

Modified residue

69

1

Phosphoserine

Modified residue

345

1

Phosphoserine

Glycosylation

293

1

N-linked (GlcNAc...)

Disulfide bond

74 ↔ 121

Natural variations

Natural variant

283

1

L → F in strain: Mangyondak.

Natural variant

312

1

N → D in a minor component.

Experimental info

Sequence conflict

5

1

G → A in CAA23681. Ref.5

Sequence conflict

119

1

L → F in CAA23681. Ref.5

Sequence conflict

188

1

A → T in CAA23682. Ref.1

Secondary structure

1

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386

Helix Strand Turn

Details...

Helix

4 – 19

16

Turn

20 – 22

3

Beta strand

28 – 30

3

Helix

32 – 43

12

Helix

48 – 58

11

Helix

70 – 74

5

Beta strand

77 – 79

3

Helix

80 – 91

12

Beta strand

97 – 109

13

Helix

116 – 125

10

Beta strand

129 – 133

5

Turn

136 – 138

3

Helix

139 – 153

15

Turn

154 – 156

3

Beta strand

171 – 187

17

Beta strand

195 – 198

4

Beta strand

208 – 222

15

Beta strand

226 – 235

10

Beta strand

238 – 249

12

Turn

250 – 252

3

Helix

253 – 259

7

Helix

262 – 268

7

Turn

271 – 273

3

Beta strand

275 – 284

10

Beta strand

286 – 293

8

Helix

294 – 301

8

Helix

305 – 307

3

Turn

314 – 316

3

Beta strand

318 – 320

3

Beta strand

322 – 335

14

Beta strand

337 – 352

16

Beta strand

358 – 360

3

Beta strand

365 – 371

7

Turn

372 – 375

4

Beta strand

376 – 384

9

Sequences

	Sequence		Length	Mass (Da)
	P01012-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 87179F028B20CEF2	FASTA	386	42,881
	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

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: 661981] [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: 692731] [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: 6272839] [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: 423993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
[6]	"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: 272676] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-36, ACETYLATION AT GLY-2.
[7]	"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: 751625] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17, 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: 751624] [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: 6783411] [Abstract] Cited for: PROTEIN SEQUENCE OF 60-85 AND 338-360, PHOSPHORYLATION AT SER-69 AND SER-345.
[10]	"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: 6749856] [Abstract] Cited for: FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
[11]	"Isolation and properties of the signal region from ovalbumin." Robinson A., Meredith C., Austen B.M. FEBS Lett. 203:243-246(1986) [PubMed: 3732511] [Abstract] Cited for: FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
[12]	"Structure and properties of ovalbumin." Huntington J.A., Stein P.E. J. Chromatogr. B 756:189-198(2001) [PubMed: 11419711] [Abstract] Cited for: REVIEW.
[13]	"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: 2395463] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[14]	"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: 1942038] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[15]	"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: 2352279] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

V00383 mRNA. Translation: CAA23682.1.
M34352 , 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.

PIR

OACH. A90455.

RefSeq

NP_990483.1.

UniGene

Gga.623

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JTI	X-ray	2.30	A/B	1-386	[»]
1OVA	X-ray	1.95	A/B/C/D	1-386	[»]
1P1Z	X-ray	3.26	P	258-265	[»]
1P4L	X-ray	2.90	P	258-264	[»]
1UHG	X-ray	1.90	A/B/C/D	1-386	[»]
1VAC	X-ray	2.50	P	258-265	[»]

ModBase

Search...

Protein family/group databases

MEROPS

I04.958.

PTM databases

GlycoSuiteDB

P01012.

Genome annotation databases

Ensembl

ENSGALG00000012869. Gallus gallus. [Contig view]

GeneID

396058.

KEGG

gga:396058.

Phylogenomic databases

HOGENOM

P01012.

HOVERGEN

P01012.

Family and domain databases

InterPro

IPR000215. Protease_inhib_I4_serpin.
[Graphical view]

PANTHER

PTHR11461. Prot_inh_serpin. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P01012.

Entry information

Entry name

OVAL_CHICK

Accession

Primary (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:	November 25, 2008
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)