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Protein

Ovalbumin

Gene

SERPINB14

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -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

Keywordsi

LigandCalcium, Metal-binding

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagine2 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 subtilisin1 Publication2
Sitei359 – 360Cleavage; by subtilisin1 Publication2

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP01012
PRIDEiP01012

PTM databases

GlyConnecti475
iPTMnetiP01012
UniCarbKBiP01012

Expressioni

Tissue specificityi

Major protein of egg white.

Gene expression databases

BgeeiENSGALG00000012869 Expressed in 1 organ(s), highest expression level in female gonad

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036403

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
GeneTreeiENSGT00930000150820
HOGENOMiHOG000238519
HOVERGENiHBG005957
InParanoidiP01012
PhylomeDBiP01012
TreeFamiTF352619

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit

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

Similar proteinsi

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

GlyConnecti475
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
GeneTreeiENSGT00930000150820
HOGENOMiHOG000238519
HOVERGENiHBG005957
InParanoidiP01012
PhylomeDBiP01012
TreeFamiTF352619

Miscellaneous databases

EvolutionaryTraceiP01012
PROiPR:P01012

Gene expression databases

BgeeiENSGALG00000012869 Expressed in 1 organ(s), highest expression level in female gonad

Family and domain databases

InterProiView protein in InterPro
IPR023795 Serpin_CS
IPR023796 Serpin_dom
IPR000215 Serpin_fam
IPR036186 Serpin_sf
PANTHERiPTHR11461 PTHR11461, 1 hit
PfamiView protein in Pfam
PF00079 Serpin, 1 hit
SMARTiView protein in SMART
SM00093 SERPIN, 1 hit
SUPFAMiSSF56574 SSF56574, 1 hit
PROSITEiView protein in PROSITE
PS00284 SERPIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiOVAL_CHICK
AccessioniPrimary (citable) accession number: P01012
Secondary accession number(s): Q804A4, Q90741
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 174 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Allergens
    Nomenclature of allergens and list of entries
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Main funding by: National Institutes of Health

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