P01012 (OVAL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ovalbumin

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

Gene names

Name:

SERPINB14

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › 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	Non-inhibitory serpin. Storage protein of egg white. Ref.11 Ref.12
Subunit structure	Homodimer. Ref.17
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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Allergen
Domain	Signal
Ligand	Calcium Metal-binding
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytosol Traceable author statement. Source: Reactome early endosome lumen Traceable author statement. Source: Reactome extracellular region Inferred from Biological aspect of Ancestor. Source: RefGenome phagolysosome Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from direct assay Ref.17. Source: UniProtKB serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7

Chain

2 – 386

385

Ovalbumin

PRO_0000094126

Signal peptide

22 – 48

27

Not cleaved

Sites

Metal binding

192

1

Calcium

Site

353 – 354

2

Cleavage; by elastase or subtilisin

Site

359 – 360

2

Cleavage; by subtilisin

Amino acid modifications

Modified residue

2

1

N-acetylglycine Ref.6 Ref.7

Modified residue

69

1

Phosphoserine Ref.9

Modified residue

345

1

Phosphoserine Ref.9

Glycosylation

293

1

N-linked (GlcNAc...) Ref.17

Disulfide bond

74 ↔ 121

Ref.14 Ref.17

Natural variations

Natural variant

283

1

L → F in strain: Mangyondak. Ref.4

Natural variant

312

1

N → D in a minor component.

Experimental info

Mutagenesis

74

1

C → 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.14

Mutagenesis

121

1

C → 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.14

Mutagenesis

340

1

R → 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 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 – 22

19

Beta strand

28 – 30

3

Helix

32 – 43

12

Helix

48 – 58

11

Helix

68 – 71

4

Turn

72 – 75

4

Turn

78 – 81

4

Helix

82 – 91

10

Beta strand

96 – 109

14

Helix

116 – 125

10

Beta strand

127 – 129

3

Beta strand

130 – 133

4

Turn

136 – 138

3

Helix

139 – 153

15

Turn

154 – 156

3

Beta strand

173 – 183

11

Beta strand

185 – 187

3

Helix

191 – 193

3

Beta strand

195 – 199

5

Beta strand

207 – 223

17

Helix

224 – 226

3

Beta strand

228 – 235

8

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

324 – 335

12

Beta strand

339 – 341

3

Helix

345 – 352

8

Beta strand

358 – 360

3

Beta strand

365 – 371

7

Turn

372 – 374

3

Beta strand

377 – 384

8

Sequences

	Sequence		Length	Mass (Da)
	P01012 [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] [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]	"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.
[14]	"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, MASS SPECTROMETRY, MUTAGENESIS OF CYS-74 AND CYS-121.
[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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[16]	"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).
[17]	"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.
[18]	"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.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00583974.

PIR

OACH. A90455.

RefSeq

NP_990483.1. NM_205152.2.

UniGene

Gga.623.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JTI	X-ray	2.30	A/B	2-385	[»]
1OVA	X-ray	1.95	A/B/C/D	2-386	[»]
1P1Z	X-ray	3.26	P	258-265	[»]
1P4L	X-ray	2.90	P	258-265	[»]
1UHG	X-ray	1.90	A/B/C/D	2-385	[»]
1VAC	X-ray	2.50	P	258-265	[»]
3CVH	X-ray	2.90	C/O	258-265	[»]
3P9L	X-ray	2.00	C/F	258-265	[»]
3P9M	X-ray	2.00	C/F	258-265	[»]
3PAB	X-ray	2.20	C/F	259-265	[»]
4HKJ	X-ray	3.00	C/G/K/O	258-265	[»]

ProteinModelPortal

P01012.

SMR

P01012. Positions 2-386.

ModBase

Search...

Protein family/group databases

Allergome

3292. Gal d 2.0101.
360. Gal d 2.

MEROPS

I04.958.

PTM databases

GlycoSuiteDB

P01012.

Proteomic databases

PaxDb

P01012.

PRIDE

P01012.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000020995; ENSGALP00000020965; ENSGALG00000012869.
ENSGALT00000037195; ENSGALP00000036403; ENSGALG00000012869.

GeneID

396058.

KEGG

gga:396058.

Organism-specific databases

CTD

396058.

Phylogenomic databases

eggNOG

COG4826.

GeneTree

ENSGT00690000101812.

HOGENOM

HOG000238519.

HOVERGEN

HBG005957.

InParanoid

P01012.

OMA

HHANENI.

OrthoDB

EOG4FBHTJ.

Enzyme and pathway databases

Reactome

REACT_102124. Immune System.

Family and domain databases

InterPro

IPR023795. Protease_inhib_I4_serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075085.

EvolutionaryTrace

P01012.

NextBio

20816118.

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:	April 3, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program