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Protein

Ovalbumin

Gene

SERPINB14

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi192Calcium1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • protease binding Source: AgBase
  • serine-type endopeptidase inhibitor activity Source: AgBase

GO - Biological processi

  • amino acid homeostasis Source: AgBase
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
  • embryo development ending in birth or egg hatching Source: AgBase
  • ion homeostasis Source: AgBase
  • ion transport Source: AgBase
  • response to corticosterone Source: AgBase
  • response to estrogen Source: AgBase
  • response to progesterone Source: AgBase
  • response to steroid hormone Source: AgBase
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-GGA-6798695. Neutrophil degranulation.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 2

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • cytosol Source: Reactome
  • early endosome lumen Source: Reactome
  • endoplasmic reticulum Source: AgBase
  • extracellular region Source: Reactome
  • extracellular space Source: AgBase
  • membrane-bounded vesicle Source: AgBase
  • phagocytic vesicle Source: Reactome
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi74C → 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 Publication1
Mutagenesisi121C → 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 Publication1
Mutagenesisi340R → T: Significantly more thermostabilized following cleavage at P-P' site. Inserts reactive loop at very slow rate. No inhibitory action against serine proteinases. 1 Publication1

Keywords - Diseasei

Allergen

Protein family/group databases

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

Chemistry databases

ChEMBLiCHEMBL1075085.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000941262 – 386OvalbuminAdd BLAST385
Signal peptidei22 – 48Not cleavedAdd BLAST27

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycine2 Publications1
Modified residuei69Phosphoserine1 Publication1
Disulfide bondi74 ↔ 1212 Publications
Glycosylationi293N-linked (GlcNAc...)2 Publications1
Modified residuei345Phosphoserine1 Publication1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei353 – 354Cleavage; by elastase or subtilisin2
Sitei359 – 360Cleavage; by subtilisin2

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01012.
PRIDEiP01012.

PTM databases

iPTMnetiP01012.
UniCarbKBiP01012.

Expressioni

Tissue specificityi

Major protein of egg white.

Gene expression databases

BgeeiENSGALG00000012869.
ExpressionAtlasiP01012. baseline and differential.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protease binding Source: AgBase

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036403.

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 22Combined sources19
Turni23 – 25Combined sources3
Beta strandi28 – 30Combined sources3
Helixi32 – 43Combined sources12
Helixi48 – 58Combined sources11
Helixi68 – 71Combined sources4
Turni72 – 75Combined sources4
Turni78 – 81Combined sources4
Helixi82 – 91Combined sources10
Beta strandi96 – 109Combined sources14
Helixi116 – 125Combined sources10
Beta strandi130 – 133Combined sources4
Turni136 – 138Combined sources3
Helixi139 – 153Combined sources15
Turni154 – 156Combined sources3
Beta strandi173 – 183Combined sources11
Beta strandi185 – 187Combined sources3
Helixi191 – 193Combined sources3
Beta strandi195 – 199Combined sources5
Beta strandi207 – 223Combined sources17
Helixi224 – 226Combined sources3
Beta strandi228 – 235Combined sources8
Beta strandi238 – 249Combined sources12
Turni250 – 252Combined sources3
Helixi253 – 259Combined sources7
Helixi262 – 268Combined sources7
Turni271 – 273Combined sources3
Beta strandi275 – 284Combined sources10
Beta strandi286 – 293Combined sources8
Helixi294 – 301Combined sources8
Helixi305 – 307Combined sources3
Turni314 – 316Combined sources3
Beta strandi318 – 320Combined sources3
Beta strandi324 – 335Combined sources12
Beta strandi339 – 341Combined sources3
Helixi345 – 352Combined sources8
Beta strandi358 – 360Combined sources3
Beta strandi365 – 371Combined sources7
Turni372 – 374Combined sources3
Beta strandi377 – 384Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP01012.
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)DescriptionActionsGraphical viewLength
Sequence conflicti5G → A in CAA23681 (PubMed:423993).Curated1
Sequence conflicti119L → F in CAA23681 (PubMed:423993).Curated1
Sequence conflicti188A → T in CAA23682 (PubMed:661981).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti283L → F in strain: Mangyondak. 1 Publication1
Natural varianti312N → D in a minor component. 1

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.
PIRiA90455. OACH.
RefSeqiNP_990483.1. NM_205152.2.
UniGeneiGga.623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036403.

Chemistry databases

ChEMBLiCHEMBL1075085.

Protein family/group databases

Allergomei3292. Gal d 2.0101.
360. Gal d 2.
MEROPSiI04.958.

PTM databases

iPTMnetiP01012.
UniCarbKBiP01012.

Proteomic databases

PaxDbiP01012.
PRIDEiP01012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi101801591.

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118789.
HOGENOMiHOG000238519.
HOVERGENiHBG005957.
InParanoidiP01012.
PhylomeDBiP01012.
TreeFamiTF352619.

Enzyme and pathway databases

ReactomeiR-GGA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP01012.
PROiP01012.

Gene expression databases

BgeeiENSGALG00000012869.
ExpressionAtlasiP01012. baseline and differential.

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]
ProtoNetiSearch...

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 30, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.