UniProt functional annotation for P01012



	UniProt functional annotation for P01012

UniProt code: P01012.

Organism: Gallus gallus (Chicken).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; Phasianinae; Gallus.

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. Expressed in the magnum of the oviduct (at protein level) (PubMed:25436390). {ECO:0000269|PubMed:25436390}.

Induction: Down-regulated by dietary stress. Decreased expression at day 14 in the magnum of the oviduct in the corticosterone-fed laying hens. {ECO:0000269|PubMed:25436390}.

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}.

Annotations taken from UniProtKB at the EBI.


Organism:		Gallus gallus (Chicken).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; Phasianinae; Gallus.



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. Expressed in the magnum of the oviduct (at protein level) (PubMed:25436390). {ECO:0000269\|PubMed:25436390}.
Induction:		Down-regulated by dietary stress. Decreased expression at day 14 in the magnum of the oviduct in the corticosterone-fed laying hens. {ECO:0000269\|PubMed:25436390}.
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}.