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P01012

- OVAL_CHICK

UniProt

P01012 - OVAL_CHICK

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Protein

Ovalbumin

Gene

SERPINB14

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-inhibitory serpin. Storage protein of egg white.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi192 – 1921Calcium
Sitei353 – 3542Cleavage; by elastase or subtilisin
Sitei359 – 3602Cleavage; by subtilisin

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. serine-type endopeptidase inhibitor activity Source: RefGenome

GO - Biological processi

  1. negative regulation of endopeptidase activity Source: RefGenome
  2. regulation of proteolysis Source: RefGenome
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_197100. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_197101. Endosomal/Vacuolar pathway.
REACT_197102. ER-Phagosome pathway.

Protein family/group databases

MEROPSiI04.958.

Names & Taxonomyi

Protein namesi
Recommended name:
Ovalbumin
Alternative name(s):
Allergen Gal d II
Egg albumin
Plakalbumin
Allergen: Gal d 2
Gene namesi
Name:SERPINB14
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. early endosome lumen Source: Reactome
  3. extracellular region Source: RefGenome
  4. extracellular space Source: InterPro
  5. phagocytic vesicle Source: Reactome
  6. phagolysosome Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Can cause an allergic reaction in humans.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741C → 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. 1 Publication
Mutagenesisi121 – 1211C → 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. 1 Publication
Mutagenesisi340 – 3401R → T: Significantly more thermostabilized following cleavage at P-P' site. Inserts reactive loop at very slow rate. No inhibitory action against serine proteinases. 1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3292. Gal d 2.0101.
360. Gal d 2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 386385OvalbuminPRO_0000094126Add
BLAST
Signal peptidei22 – 4827Not cleavedAdd
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine2 Publications
Modified residuei69 – 691Phosphoserine1 Publication
Disulfide bondi74 ↔ 1212 Publications
Glycosylationi293 – 2931N-linked (GlcNAc...)2 Publications
Modified residuei345 – 3451Phosphoserine1 Publication

Post-translational modificationi

Undergoes proteolytic cleavage first at the canonical P1-P1' site, and then at the P8-P7 site by subtilisin.2 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01012.
PRIDEiP01012.

PTM databases

UniCarbKBiP01012.

Expressioni

Tissue specificityi

Major protein of egg white.

Gene expression databases

ExpressionAtlasiP01012. differential.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2219Combined sources
Turni23 – 253Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 4312Combined sources
Helixi48 – 5811Combined sources
Helixi68 – 714Combined sources
Turni72 – 754Combined sources
Turni78 – 814Combined sources
Helixi82 – 9110Combined sources
Beta strandi96 – 10914Combined sources
Helixi116 – 12510Combined sources
Beta strandi130 – 1334Combined sources
Turni136 – 1383Combined sources
Helixi139 – 15315Combined sources
Turni154 – 1563Combined sources
Beta strandi173 – 18311Combined sources
Beta strandi185 – 1873Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 1995Combined sources
Beta strandi207 – 22317Combined sources
Helixi224 – 2263Combined sources
Beta strandi228 – 2358Combined sources
Beta strandi238 – 24912Combined sources
Turni250 – 2523Combined sources
Helixi253 – 2597Combined sources
Helixi262 – 2687Combined sources
Turni271 – 2733Combined sources
Beta strandi275 – 28410Combined sources
Beta strandi286 – 2938Combined sources
Helixi294 – 3018Combined sources
Helixi305 – 3073Combined sources
Turni314 – 3163Combined sources
Beta strandi318 – 3203Combined sources
Beta strandi324 – 33512Combined sources
Beta strandi339 – 3413Combined sources
Helixi345 – 3528Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi365 – 3717Combined sources
Turni372 – 3743Combined sources
Beta strandi377 – 3848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JTIX-ray2.30A/B2-386[»]
1OVAX-ray1.95A/B/C/D2-386[»]
1P1ZX-ray3.26P258-265[»]
1P4LX-ray2.90P258-265[»]
1UHGX-ray1.90A/B/C/D2-386[»]
1VACX-ray2.50P258-265[»]
3C8KX-ray2.90P258-265[»]
3CVHX-ray2.90C/O258-265[»]
3P9LX-ray2.00C/F258-265[»]
3P9MX-ray2.00C/F258-265[»]
3PABX-ray2.20C/F258-265[»]
4HKJX-ray3.00C/G/K/O258-265[»]
ProteinModelPortaliP01012.
SMRiP01012. Positions 2-386.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01012.

Family & Domainsi

Domaini

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.

Sequence similaritiesi

Belongs to the serpin family. Ov-serpin subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP01012.
OMAiQCVKELY.
OrthoDBiEOG7327PB.
PhylomeDBiP01012.
TreeFamiTF352619.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSIGAASME FCFDVFKELK VHHANENIFY CPIAIMSALA MVYLGAKDST
60 70 80 90 100
RTQINKVVRF DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF
110 120 130 140 150
SLASRLYAEE RYPILPEYLQ CVKELYRGGL EPINFQTAAD QARELINSWV
160 170 180 190 200
ESQTNGIIRN VLQPSSVDSQ TAMVLVNAIV FKGLWEKAFK DEDTQAMPFR
210 220 230 240 250
VTEQESKPVQ MMYQIGLFRV ASMASEKMKI LELPFASGTM SMLVLLPDEV
260 270 280 290 300
SGLEQLESII NFEKLTEWTS SNVMEERKIK VYLPRMKMEE KYNLTSVLMA
310 320 330 340 350
MGITDVFSSS ANLSGISSAE SLKISQAVHA AHAEINEAGR EVVGSAEAGV
360 370 380
DAASVSEEFR ADHPFLFCIK HIATNAVLFF GRCVSP
Length:386
Mass (Da):42,881
Last modified:January 23, 2007 - v2
Checksum:i87179F028B20CEF2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51G → A in CAA23681. (PubMed:423993)Curated
Sequence conflicti119 – 1191L → F in CAA23681. (PubMed:423993)Curated
Sequence conflicti188 – 1881A → T in CAA23682. (PubMed:661981)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti283 – 2831L → F in strain: Mangyondak. 1 Publication
Natural varianti312 – 3121N → D in a minor component.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA90455. OACH.
RefSeqiNP_990483.1. NM_205152.2.
UniGeneiGga.623.

Genome annotation databases

EnsembliENSGALT00000037195; ENSGALP00000036403; ENSGALG00000012869.
GeneIDi396058.
KEGGigga:396058.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi A90455. OACH.
RefSeqi NP_990483.1. NM_205152.2.
UniGenei Gga.623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JTI X-ray 2.30 A/B 2-386 [» ]
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 2-386 [» ]
1VAC X-ray 2.50 P 258-265 [» ]
3C8K X-ray 2.90 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 258-265 [» ]
4HKJ X-ray 3.00 C/G/K/O 258-265 [» ]
ProteinModelPortali P01012.
SMRi P01012. Positions 2-386.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL1075085.

Protein family/group databases

Allergomei 3292. Gal d 2.0101.
360. Gal d 2.
MEROPSi I04.958.

PTM databases

UniCarbKBi P01012.

Proteomic databases

PaxDbi P01012.
PRIDEi P01012.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000037195 ; ENSGALP00000036403 ; ENSGALG00000012869 .
GeneIDi 396058.
KEGGi gga:396058.

Organism-specific databases

CTDi 396058.

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118789.
HOGENOMi HOG000238519.
HOVERGENi HBG005957.
InParanoidi P01012.
OMAi QCVKELY.
OrthoDBi EOG7327PB.
PhylomeDBi P01012.
TreeFami TF352619.

Enzyme and pathway databases

Reactomei REACT_197100. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_197101. Endosomal/Vacuolar pathway.
REACT_197102. ER-Phagosome pathway.

Miscellaneous databases

EvolutionaryTracei P01012.
NextBioi 20816118.
PROi P01012.

Gene expression databases

ExpressionAtlasi P01012. differential.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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. 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.

Entry informationi

Entry nameiOVAL_CHICK
AccessioniPrimary (citable) accession number: P01012
Secondary accession number(s): Q804A4, Q90741
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3