P01005 (IOVO_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Ovomucoid Alternative name(s): Allergen Gal d I Allergen=Gal d 1
Organism	Gallus gallus (Chicken)
Taxonomic identifier	9031 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Secreted.
Domain	Avian ovomucoid consists of three homologous, tandem Kazal family inhibitory domains.
Allergenic properties	Causes an allergic reaction in human.
Sequence similarities	Contains 3 Kazal-like domains.

Ontologies

Keywords
Cellular component	Secreted
Disease	Allergen
Domain	Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from direct assay. Source: AgBase
Molecular function	IgE binding Inferred from mutant phenotype. Source: AgBase IgG binding Inferred from mutant phenotype. Source: AgBase serine-type endopeptidase inhibitor activity Inferred from direct assay. Source: AgBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Ref.2
	Chain	25 – 210	186	Ovomucoid		PRO_0000016579
Regions
	Domain	25 – 88	64	Kazal-like 1
	Domain	89 – 153	65	Kazal-like 2
	Domain	156 – 210	55	Kazal-like 3
Sites
	Site	48 – 49	2	Reactive bond 1 for endoproteinase Lys-C
	Site	113 – 114	2	Reactive bond 2 for trypsin
	Site	172 – 173	2	Reactive bond 3
Amino acid modifications
	Glycosylation	34	1	N-linked (GlcNAc...)
	Glycosylation	77	1	N-linked (GlcNAc...) Ref.4
	Glycosylation	93	1	N-linked (GlcNAc...)
	Glycosylation	99	1	N-linked (GlcNAc...)
	Glycosylation	199	1	N-linked (GlcNAc...); partial Ref.4
	Disulfide bond	29 ↔ 68
	Disulfide bond	46 ↔ 65
	Disulfide bond	54 ↔ 86
	Disulfide bond	94 ↔ 133
	Disulfide bond	111 ↔ 130
	Disulfide bond	119 ↔ 151
	Disulfide bond	162 ↔ 192
	Disulfide bond	170 ↔ 189
	Disulfide bond	178 ↔ 210
Natural variations
	Natural variant	158 – 159	2	Missing Due to an ambiguous intron excision.
Experimental info
	Sequence conflict	62	1	T → N AA sequence Ref.2
	Sequence conflict	64	1	D → E AA sequence Ref.2
	Sequence conflict	108	1	M → T AA sequence Ref.2
	Sequence conflict	150	1	G → E AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P01005 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 8BE9516B6D38ACF9	FASTA	210	22,591
	10 20 30 40 50 60 MAMAGVFVLF SFVLCGFLPD AAFGAEVDCS RFPNATDKEG KDVLVCNKDL RPICGTDGVT 70 80 90 100 110 120 YTNDCLLCAY SIEFGTNISK EHDGECKETV PMNCSSYANT TSEDGKVMVL CNRAFNPVCG 130 140 150 160 170 180 TDGVTYDNEC LLCAHKVEQG ASVDKRHDGG CRKELAAVSV DCSEYPKPDC TAEDRPLCGS 190 200 210 DNKTYGNKCN FCNAVVESNG TLTLSHFGKC

References

[1]	"Primary sequence of ovomucoid messenger RNA as determined from cloned complementary DNA." Catterall J.F., Stein J.P., Kristo P., Means A.R., O'Malley B.W. J. Cell Biol. 87:480-487(1980) [PubMed: 7430252] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains." Kato I., Schrode J., Kohr W.J., Laskowski M. Jr. Biochemistry 26:193-201(1987) [PubMed: 3548816] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-210.
[3]	"Precursor of egg white ovomucoid. Amino acid sequence of an NH2-terminal extension." Thibodeau S.N., Palmiter R.D., Walsh K.A. J. Biol. Chem. 253:9018-9023(1978) [PubMed: 721826] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-44.
[4]	"A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation." Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P. J. Proteome Res. 3:556-566(2004) [PubMed: 15253437] [Abstract] Cited for: GLYCOSYLATION AT ASN-77 AND ASN-199, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J00902 mRNA. No translation available.
IPI	IPI00597129.
PIR	TICHM. A92754.
UniGene	Gga.5085.
3D structure databases
ProteinModelPortal	P01005.
SMR	P01005. Positions 27-86.
ModBase	Search...
Protein family/group databases
Allergome	3291. Gal d 1.0101. 359. Gal d 1.
MEROPS	I01.001.
PTM databases
GlycoSuiteDB	P01005.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000005554; ENSGALP00000005544; ENSGALG00000003512.
Phylogenomic databases
eggNOG	veNOG16333.
HOVERGEN	HBG006172.
InParanoid	P01005.
OMA	ATCESEG.
OrthoDB	EOG4K6G5H.
PhylomeDB	P01005.
Family and domain databases
InterPro	IPR002350. Prot_inh_Kazal. [Graphical view]
Pfam	PF00050. Kazal_1. 3 hits. [Graphical view]
SMART	SM00280. KAZAL. 3 hits. [Graphical view]
PROSITE	PS00282. KAZAL_1. 3 hits. PS51465. KAZAL_2. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IOVO_CHICK

Accession

Primary (citable) accession number: P01005

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 16, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program