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Ovalbumin (Allergen Gal d II) (Egg albumin) (Plakalbumin) (allergen Gal d 2)

 OVAL_CHICK              Reviewed;         386 AA.
P01012; Q804A4; Q90741;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
07-JUN-2017, entry version 166.
RecName: Full=Ovalbumin;
AltName: Full=Allergen Gal d II;
AltName: Full=Egg albumin;
AltName: Full=Plakalbumin;
AltName: Allergen=Gal d 2;
Name=SERPINB14;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=661981; DOI=10.1038/273723a0;
McReynolds L., O'Malley B.W., Nisbet A.D., Fothergill J.E., Givol D.,
Fields S., Robertson M., Brownlee G.G.;
"Sequence of chicken ovalbumin mRNA.";
Nature 273:723-728(1978).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=692731; DOI=10.1038/275510a0;
Catterall J.F., O'Malley B.W., Robertson M.A., Staden R., Tanaka Y.,
Brownlee G.G.;
"Nucleotide sequence homology at 12 intron-exon junctions in the chick
ovalbumin gene.";
Nature 275:510-513(1978).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6272839; DOI=10.1021/bi00525a024;
Woo S.L.C., Beattie W.G., Catterall J.F., Dugaiczyk A., Staden R.,
Brownlee G.G., O'Malley B.W.;
"Complete nucleotide sequence of the chicken chromosomal ovalbumin
gene and its biological significance.";
Biochemistry 20:6437-6446(1981).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-283.
STRAIN=Mangyondak;
Kim R., Rim D., Li Y.;
"Ovalbumin from the chicken called Mangyondak in North Korea.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
PubMed=423993; DOI=10.1038/278370a0;
Robertson M.A., Staden R., Tanaka Y., Catterall J.F., O'Malley B.W.,
Brownlee G.G.;
"Sequence of three introns in the chick ovalbumin gene.";
Nature 278:370-372(1979).
[6]
PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT GLY-2.
PubMed=751625; DOI=10.1071/BI9780443;
Thompson E.O.P., Fisher W.K.;
"A correction and extension of the acetylated amino terminal sequence
of ovalbumin.";
Aust. J. Biol. Sci. 31:443-446(1978).
[7]
PROTEIN SEQUENCE OF 2-36, AND ACETYLATION AT GLY-2.
PubMed=272676; DOI=10.1073/pnas.75.1.94;
Palmiter R.D., Gagnon J., Walsh K.A.;
"Ovalbumin: a secreted protein without a transient hydrophobic leader
sequence.";
Proc. Natl. Acad. Sci. U.S.A. 75:94-98(1978).
[8]
PROTEIN SEQUENCE OF 6-17; 30-36; 61-79; 116-124; 367-374 AND 380-386.
PubMed=751624; DOI=10.1071/BI9780433;
Thompson E.O.P., Fisher W.K.;
"Amino acid sequences containing half-cystine residues in ovalbumin.";
Aust. J. Biol. Sci. 31:433-442(1978).
[9]
PROTEIN SEQUENCE OF 60-85 AND 338-360, AND PHOSPHORYLATION AT SER-69
AND SER-345.
PubMed=6783411; DOI=10.1111/j.1432-1033.1981.tb05165.x;
Henderson J.Y., Moir A.J.G., Fothergill L.A., Fothergill J.E.;
"Sequences of sixteen phosphoserine peptides from ovalbumins of eight
species.";
Eur. J. Biochem. 114:439-450(1981).
[10]
PROTEIN SEQUENCE OF 354-359, PROTEOLYTIC CLEAVAGE AT ALA-353 AND
PHE-359, AND MUTAGENESIS OF ARG-340.
PubMed=11931671; DOI=10.1042/0264-6021:3630403;
Arii Y., Hirose M.;
"Probing the serpin structural-transition mechanism in ovalbumin
mutant R339T by proteolytic-cleavage kinetics of the reactive-centre
loop.";
Biochem. J. 363:403-409(2002).
[11]
FUNCTION OF UNCLEAVED SIGNAL PEPTIDE, AND SUBCELLULAR LOCATION.
PubMed=6749856;
Meek R.L., Walsh K.A., Palmiter R.D.;
"The signal sequence of ovalbumin is located near the NH2 terminus.";
J. Biol. Chem. 257:12245-12251(1982).
[12]
FUNCTION OF UNCLEAVED SIGNAL PEPTIDE.
PubMed=3732511; DOI=10.1016/0014-5793(86)80751-7;
Robinson A., Meredith C., Austen B.M.;
"Isolation and properties of the signal region from ovalbumin.";
FEBS Lett. 203:243-246(1986).
[13]
GLYCOSYLATION AT ASN-293.
PubMed=19358553; DOI=10.1021/ac900231w;
Thaysen-Andersen M., Mysling S., Hojrup P.;
"Site-specific glycoprofiling of N-linked glycopeptides using MALDI-
TOF MS: strong correlation between signal strength and glycoform
quantities.";
Anal. Chem. 81:3933-3943(2009).
[14]
THERMOSTABILITY OF N- AND S-CONFORMERS.
PubMed=20512973; DOI=10.1002/pro.398;
Ishimaru T., Ito K., Tanaka M., Matsudomi N.;
"Thermostabilization of ovalbumin by alkaline treatment: Examination
of the possible roles of D-serine residues.";
Protein Sci. 19:1205-1212(2010).
[15]
DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
OF CYS-74 AND CYS-121.
PubMed=21389617; DOI=10.1271/bbb.100772;
Ishimaru T., Ito K., Tanaka M., Tanaka S., Matsudomi N.;
"The role of the disulfide bridge in the stability and structural
integrity of ovalbumin evaluated by site-directed mutagenesis.";
Biosci. Biotechnol. Biochem. 75:544-549(2011).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=2352279; DOI=10.1016/S0022-2836(05)80212-8;
Wright H.T., Qian H.X., Huber R.;
"Crystal structure of plakalbumin, a proteolytically nicked form of
ovalbumin. Its relationship to the structure of cleaved alpha-1-
proteinase inhibitor.";
J. Mol. Biol. 213:513-528(1990).
[17]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
PubMed=2395463; DOI=10.1038/347099a0;
Stein P.E., Leslie A.G.W., Finch J.T., Turnell W.G., McLaughlin P.J.,
Carrell R.W.;
"Crystal structure of ovalbumin as a model for the reactive centre of
serpins.";
Nature 347:99-102(1990).
[18]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), METAL-BINDING, SUBUNIT,
DISULFIDE BOND, AND GLYCOSYLATION AT ASN-293.
PubMed=1942038; DOI=10.1016/0022-2836(91)80185-W;
Stein P.E., Leslie A.G.W., Finch J.T., Carrell R.W.;
"Crystal structure of uncleaved ovalbumin at 1.95-A resolution.";
J. Mol. Biol. 221:941-959(1991).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-385 OF MUTANT THR-340, AND
PROTEOLYTIC CLEAVAGE.
PubMed=11779232; DOI=10.1006/jmbi.2001.5056;
Yamasaki M., Arii Y., Mikami B., Hirose M.;
"Loop-inserted and thermostabilized structure of P1-P1' cleaved
ovalbumin mutant R339T.";
J. Mol. Biol. 315:113-120(2002).
-!- FUNCTION: Non-inhibitory serpin. Storage protein of egg white.
{ECO:0000269|PubMed:3732511, ECO:0000269|PubMed:6749856}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1942038}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6749856}.
-!- 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.
-!- DOMAIN: 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.
-!- DOMAIN: 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.
-!- PTM: Undergoes proteolytic cleavage first at the canonical P1-P1'
site, and then at the P8-P7 site by subtilisin.
{ECO:0000269|PubMed:11779232, ECO:0000269|PubMed:11931671}.
-!- ALLERGEN: Can cause an allergic reaction in humans.
-!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/OA/";
-----------------------------------------------------------------------
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EMBL; V00383; CAA23682.1; -; mRNA.
EMBL; M34352; AAA48998.1; -; Genomic_DNA.
EMBL; M34346; AAA48998.1; JOINED; Genomic_DNA.
EMBL; M34347; AAA48998.1; JOINED; Genomic_DNA.
EMBL; M34348; AAA48998.1; JOINED; Genomic_DNA.
EMBL; M34349; AAA48998.1; JOINED; Genomic_DNA.
EMBL; M34350; AAA48998.1; JOINED; Genomic_DNA.
EMBL; M34351; AAA48998.1; JOINED; Genomic_DNA.
EMBL; V00438; CAA23716.1; -; Genomic_DNA.
EMBL; J00895; AAB59956.1; -; Genomic_DNA.
EMBL; AY223553; AAO43266.1; -; mRNA.
EMBL; V00382; CAA23681.1; -; Genomic_DNA.
PIR; A90455; OACH.
RefSeq; NP_990483.1; NM_205152.2.
UniGene; Gga.623; -.
PDB; 1JTI; X-ray; 2.30 A; A/B=2-386.
PDB; 1OVA; X-ray; 1.95 A; A/B/C/D=2-386.
PDB; 1P1Z; X-ray; 3.26 A; P=258-265.
PDB; 1P4L; X-ray; 2.90 A; P=258-265.
PDB; 1UHG; X-ray; 1.90 A; A/B/C/D=2-386.
PDB; 1VAC; X-ray; 2.50 A; P=258-265.
PDB; 3C8K; X-ray; 2.90 A; P=258-265.
PDB; 3CVH; X-ray; 2.90 A; C/O=258-265.
PDB; 3P9L; X-ray; 2.00 A; C/F=258-265.
PDB; 3P9M; X-ray; 2.00 A; C/F=258-265.
PDB; 3PAB; X-ray; 2.20 A; C/F=258-265.
PDB; 4HKJ; X-ray; 3.00 A; C/G/K/O=258-265.
PDBsum; 1JTI; -.
PDBsum; 1OVA; -.
PDBsum; 1P1Z; -.
PDBsum; 1P4L; -.
PDBsum; 1UHG; -.
PDBsum; 1VAC; -.
PDBsum; 3C8K; -.
PDBsum; 3CVH; -.
PDBsum; 3P9L; -.
PDBsum; 3P9M; -.
PDBsum; 3PAB; -.
PDBsum; 4HKJ; -.
ProteinModelPortal; P01012; -.
SMR; P01012; -.
STRING; 9031.ENSGALP00000036403; -.
ChEMBL; CHEMBL1075085; -.
Allergome; 3292; Gal d 2.0101.
Allergome; 360; Gal d 2.
MEROPS; I04.958; -.
iPTMnet; P01012; -.
UniCarbKB; P01012; -.
PaxDb; P01012; -.
PRIDE; P01012; -.
Ensembl; ENSGALT00000037195; ENSGALP00000036403; ENSGALG00000012869.
GeneID; 396058; -.
KEGG; gga:396058; -.
CTD; 101801591; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118789; -.
HOGENOM; HOG000238519; -.
HOVERGEN; HBG005957; -.
InParanoid; P01012; -.
PhylomeDB; P01012; -.
TreeFam; TF352619; -.
Reactome; R-GGA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P01012; -.
PRO; PR:P01012; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000012869; -.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031905; C:early endosome lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome.
GO; GO:0032010; C:phagolysosome; TAS:Reactome.
GO; GO:0031982; C:vesicle; IDA:AgBase.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:AgBase.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:AgBase.
GO; GO:0080144; P:amino acid homeostasis; TAS:AgBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:AgBase.
GO; GO:0050801; P:ion homeostasis; TAS:AgBase.
GO; GO:0006811; P:ion transport; TAS:AgBase.
GO; GO:0051412; P:response to corticosterone; IDA:AgBase.
GO; GO:0043627; P:response to estrogen; IDA:AgBase.
GO; GO:0032570; P:response to progesterone; IDA:AgBase.
GO; GO:0048545; P:response to steroid hormone; IDA:AgBase.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allergen; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Secreted; Signal.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:272676,
ECO:0000269|PubMed:751625}.
CHAIN 2 386 Ovalbumin.
/FTId=PRO_0000094126.
SIGNAL 22 48 Not cleaved.
METAL 192 192 Calcium.
SITE 353 354 Cleavage; by elastase or subtilisin.
SITE 359 360 Cleavage; by subtilisin.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000269|PubMed:272676,
ECO:0000269|PubMed:751625}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000269|PubMed:6783411}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000269|PubMed:6783411}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19358553,
ECO:0000269|PubMed:1942038}.
DISULFID 74 121 {ECO:0000269|PubMed:1942038,
ECO:0000269|PubMed:21389617}.
VARIANT 283 283 L -> F (in strain: Mangyondak).
{ECO:0000269|Ref.4}.
VARIANT 312 312 N -> D (in a minor component).
MUTAGEN 74 74 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.
{ECO:0000269|PubMed:21389617}.
MUTAGEN 121 121 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.
{ECO:0000269|PubMed:21389617}.
MUTAGEN 340 340 R->T: Significantly more thermostabilized
following cleavage at P-P' site. Inserts
reactive loop at very slow rate. No
inhibitory action against serine
proteinases.
{ECO:0000269|PubMed:11931671}.
CONFLICT 5 5 G -> A (in Ref. 5; CAA23681).
{ECO:0000305}.
CONFLICT 119 119 L -> F (in Ref. 5; CAA23681).
{ECO:0000305}.
CONFLICT 188 188 A -> T (in Ref. 1; CAA23682).
{ECO:0000305}.
HELIX 4 22 {ECO:0000244|PDB:1UHG}.
TURN 23 25 {ECO:0000244|PDB:1OVA}.
STRAND 28 30 {ECO:0000244|PDB:1UHG}.
HELIX 32 43 {ECO:0000244|PDB:1UHG}.
HELIX 48 58 {ECO:0000244|PDB:1UHG}.
HELIX 68 71 {ECO:0000244|PDB:1UHG}.
TURN 72 75 {ECO:0000244|PDB:1UHG}.
TURN 78 81 {ECO:0000244|PDB:1UHG}.
HELIX 82 91 {ECO:0000244|PDB:1UHG}.
STRAND 96 109 {ECO:0000244|PDB:1UHG}.
HELIX 116 125 {ECO:0000244|PDB:1UHG}.
STRAND 130 133 {ECO:0000244|PDB:1UHG}.
TURN 136 138 {ECO:0000244|PDB:1UHG}.
HELIX 139 153 {ECO:0000244|PDB:1UHG}.
TURN 154 156 {ECO:0000244|PDB:1UHG}.
STRAND 173 183 {ECO:0000244|PDB:1UHG}.
STRAND 185 187 {ECO:0000244|PDB:1UHG}.
HELIX 191 193 {ECO:0000244|PDB:1UHG}.
STRAND 195 199 {ECO:0000244|PDB:1UHG}.
STRAND 207 223 {ECO:0000244|PDB:1UHG}.
HELIX 224 226 {ECO:0000244|PDB:1UHG}.
STRAND 228 235 {ECO:0000244|PDB:1UHG}.
STRAND 238 249 {ECO:0000244|PDB:1UHG}.
TURN 250 252 {ECO:0000244|PDB:1OVA}.
HELIX 253 259 {ECO:0000244|PDB:1UHG}.
HELIX 262 268 {ECO:0000244|PDB:1UHG}.
TURN 271 273 {ECO:0000244|PDB:1UHG}.
STRAND 275 284 {ECO:0000244|PDB:1UHG}.
STRAND 286 293 {ECO:0000244|PDB:1UHG}.
HELIX 294 301 {ECO:0000244|PDB:1UHG}.
HELIX 305 307 {ECO:0000244|PDB:1UHG}.
TURN 314 316 {ECO:0000244|PDB:1UHG}.
STRAND 318 320 {ECO:0000244|PDB:1JTI}.
STRAND 324 335 {ECO:0000244|PDB:1UHG}.
STRAND 339 341 {ECO:0000244|PDB:1UHG}.
HELIX 345 352 {ECO:0000244|PDB:1UHG}.
STRAND 358 360 {ECO:0000244|PDB:1UHG}.
STRAND 365 371 {ECO:0000244|PDB:1UHG}.
TURN 372 374 {ECO:0000244|PDB:1UHG}.
STRAND 377 384 {ECO:0000244|PDB:1UHG}.
SEQUENCE 386 AA; 42881 MW; 87179F028B20CEF2 CRC64;
MGSIGAASME FCFDVFKELK VHHANENIFY CPIAIMSALA MVYLGAKDST RTQINKVVRF
DKLPGFGDSI EAQCGTSVNV HSSLRDILNQ ITKPNDVYSF SLASRLYAEE RYPILPEYLQ
CVKELYRGGL EPINFQTAAD QARELINSWV ESQTNGIIRN VLQPSSVDSQ TAMVLVNAIV
FKGLWEKAFK DEDTQAMPFR VTEQESKPVQ MMYQIGLFRV ASMASEKMKI LELPFASGTM
SMLVLLPDEV SGLEQLESII NFEKLTEWTS SNVMEERKIK VYLPRMKMEE KYNLTSVLMA
MGITDVFSSS ANLSGISSAE SLKISQAVHA AHAEINEAGR EVVGSAEAGV DAASVSEEFR
ADHPFLFCIK HIATNAVLFF GRCVSP


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