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P01012

- OVAL_CHICK

UniProt

P01012 - OVAL_CHICK

Protein

Ovalbumin

Gene

SERPINB14

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    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

    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.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00740000114938.
    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

    MGSIGAASME FCFDVFKELK VHHANENIFY CPIAIMSALA MVYLGAKDST    50
    RTQINKVVRF DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF 100
    SLASRLYAEE RYPILPEYLQ CVKELYRGGL EPINFQTAAD QARELINSWV 150
    ESQTNGIIRN VLQPSSVDSQ TAMVLVNAIV FKGLWEKAFK DEDTQAMPFR 200
    VTEQESKPVQ MMYQIGLFRV ASMASEKMKI LELPFASGTM SMLVLLPDEV 250
    SGLEQLESII NFEKLTEWTS SNVMEERKIK VYLPRMKMEE KYNLTSVLMA 300
    MGITDVFSSS ANLSGISSAE SLKISQAVHA AHAEINEAGR EVVGSAEAGV 350
    DAASVSEEFR ADHPFLFCIK HIATNAVLFF GRCVSP 386
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00740000114938.
    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.

    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: October 1, 2014
    This is version 140 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