P10184 · IOV7_CHICK
- ProteinOvoinhibitor
- GeneSPINK5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine protease inhibitor involved in antimicrobial egg defense preventing contamination of table eggs (non-fertilized eggs) and protecting the chick embryo (fertilized eggs) (Probable). Inhibits trypsin, chymotrypsin, elastase, subtilisin and a proteinase of fungus Aspergillus oryzae (PubMed:13944692, PubMed:14519973, PubMed:14609095, PubMed:22010862, PubMed:6838526, PubMed:6904299).
Inhibits calcium-activated potassium channels KCNMA1 (bovine) and slo (Drosophila) (PubMed:8973172).
Has antibacterial activity against B.thuringiensis LMSA 3.06.004, but not against S.aureus CIP 103 811, P.aeruginosa PAO1, B.cereus ATCC6464 or B.subtilis ATCC 6633 (PubMed:22010862).
Inhibits calcium-activated potassium channels KCNMA1 (bovine) and slo (Drosophila) (PubMed:8973172).
Has antibacterial activity against B.thuringiensis LMSA 3.06.004, but not against S.aureus CIP 103 811, P.aeruginosa PAO1, B.cereus ATCC6464 or B.subtilis ATCC 6633 (PubMed:22010862).
Miscellaneous
Prevents symptomatic gastoroenteritis in vivo in a mouse model of rotavirus infection. Significantly inhibits intestinal replication of EDIM strain of murine rotavirus in infant mice up to 4 days after intragastrical administration of the virus.
Biotechnology
The galactomannan conjugate of this protein prepared through the Maillard reaction shows almost the same inhibitory activity toward trypsin, chymotrypsin and elastase, with stronger heat and emulsion stability, and better emulsifying properties than the untreated protein. The conjugate can therefore be useful for industrial application.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 92-93 | Reactive bond 1 for trypsin | ||||
Sequence: RN | ||||||
Site | 157-158 | Reactive bond 2 for trypsin | ||||
Sequence: RI | ||||||
Site | 223-224 | Reactive bond 3 for trypsin | ||||
Sequence: RI | ||||||
Site | 289-290 | Reactive bond 4 for trypsin | ||||
Sequence: RI | ||||||
Site | 354-355 | Reactive bond 5 for chymotrypsin | ||||
Sequence: FI | ||||||
Site | 420-421 | Reactive bond 6 for chymotrypsin and elastase | ||||
Sequence: MI | ||||||
Site | 479-480 | Reactive bond 7 for chymotrypsin and elastase | ||||
Sequence: ME |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | protein-containing complex | |
Molecular Function | ion channel inhibitor activity | |
Molecular Function | peptidase inhibitor activity | |
Molecular Function | potassium channel inhibitor activity | |
Molecular Function | protease binding | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | negative regulation of viral genome replication | |
Biological Process | response to corticosterone |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameOvoinhibitor
- Short namesOI ; OvoI
- Alternative names
- Allergen nameGal d OIH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionP10184
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in humans. Binds to IgE of egg-allergic patients. Immunoreactivity is lost by simulated gastric and gastroduodenal digestion (PubMed:23122126).
Binds to rabbit anti-ovomucoid IgG antibody indicating the cross-reactivity between this protein and the ovomucoid protein from egg white (PubMed:6838526).
Binds to rabbit anti-ovomucoid IgG antibody indicating the cross-reactivity between this protein and the ovomucoid protein from egg white (PubMed:6838526).
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000016578 | 1-517 | Ovoinhibitor | |||
Sequence: MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQFVQVALALCCFADIAFGIEVNCSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGICLYNREHGANVEKEYDGECRPKHVTIDCSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGICAYNAEHHTNISKLHDGECKLEIGSVDCSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGICAHNAEQRTHVSKKHDGKCRQEIPEIDCDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGICAHNAQHGTEVKKSHDGRCKERSTPLDCTQYLSNTQNGEAITACPFILQEVCGTDGVTYSNDCSLCAHNIELGTSVAKKHDGRCREEVPELDCSKYKTSTLKDGRQVVACTMIYDPVCATNGVTYASECTLCAHNLEQRTNLGKRKNGRCEEDITKEHCREFQKVSPICTMEYVPHCGSDGVTYSNRCFFCNAYVQSNRTLNLVSMAAC | ||||||
Glycosylation | 72 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 73↔112 | |||||
Sequence: CSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGIC | ||||||
Disulfide bond | 90↔109 | |||||
Sequence: CPRNLKPVCGTDGSTYSNEC | ||||||
Disulfide bond | 98↔130 | |||||
Sequence: CGTDGSTYSNECGICLYNREHGANVEKEYDGEC | ||||||
Disulfide bond | 139↔177 | |||||
Sequence: CSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGIC | ||||||
Disulfide bond | 155↔174 | |||||
Sequence: CPRILKPVCGSDSFTYDNEC | ||||||
Disulfide bond | 163↔195 | |||||
Sequence: CGSDSFTYDNECGICAYNAEHHTNISKLHDGEC | ||||||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 204↔243 | |||||
Sequence: CSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGIC | ||||||
Disulfide bond | 221↔240 | |||||
Sequence: CPRILSPVCGTDGFTYDNEC | ||||||
Disulfide bond | 229↔261 | |||||
Sequence: CGTDGFTYDNECGICAHNAEQRTHVSKKHDGKC | ||||||
Disulfide bond | 270↔309 | |||||
Sequence: CDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGIC | ||||||
Disulfide bond | 287↔306 | |||||
Sequence: CPRILLPVCGTDGFTYDNEC | ||||||
Disulfide bond | 295↔327 | |||||
Sequence: CGTDGFTYDNECGICAHNAQHGTEVKKSHDGRC | ||||||
Disulfide bond | 336↔374 | |||||
Sequence: CTQYLSNTQNGEAITACPFILQEVCGTDGVTYSNDCSLC | ||||||
Disulfide bond | 352↔371 | |||||
Sequence: CPFILQEVCGTDGVTYSNDC | ||||||
Disulfide bond | 360↔392 | |||||
Sequence: CGTDGVTYSNDCSLCAHNIELGTSVAKKHDGRC | ||||||
Disulfide bond | 401↔440 | |||||
Sequence: CSKYKTSTLKDGRQVVACTMIYDPVCATNGVTYASECTLC | ||||||
Disulfide bond | 418↔437 | |||||
Sequence: CTMIYDPVCATNGVTYASEC | ||||||
Disulfide bond | 426↔458 | |||||
Sequence: CATNGVTYASECTLCAHNLEQRTNLGKRKNGRC | ||||||
Disulfide bond | 467↔499 | |||||
Sequence: CREFQKVSPICTMEYVPHCGSDGVTYSNRCFFC | ||||||
Disulfide bond | 477↔496 | |||||
Sequence: CTMEYVPHCGSDGVTYSNRC | ||||||
Disulfide bond | 485↔517 | |||||
Sequence: CGSDGVTYSNRCFFCNAYVQSNRTLNLVSMAAC | ||||||
Glycosylation | 506 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in oviduct (at protein level) (PubMed:3571241).
Expressed in egg white (at protein level) (PubMed:14519973, PubMed:23122126, PubMed:25436390, PubMed:6838526).
Expressed in egg yolk plasma of non-fertilized eggs (at protein level) (PubMed:22010862).
Expressed in the magnum of the oviduct (at protein level) (PubMed:25436390).
Expressed in oviduct (PubMed:14609095, PubMed:3571241).
Expressed in liver (PubMed:11572089, PubMed:22010862, PubMed:3571241).
Expressed in the cortico-medullary border region of the bursa of Fabricius by the bursal secretory dendritic-like cells (PubMed:15252730).
Highly expressed in the magnum of the oviduct, and at a lower level in uterus. Weakly expressed in white isthmus and very weakly in infundibulum. Not expressed in duodenum and kidney (PubMed:22010862).
Expressed in egg white (at protein level) (PubMed:14519973, PubMed:23122126, PubMed:25436390, PubMed:6838526).
Expressed in egg yolk plasma of non-fertilized eggs (at protein level) (PubMed:22010862).
Expressed in the magnum of the oviduct (at protein level) (PubMed:25436390).
Expressed in oviduct (PubMed:14609095, PubMed:3571241).
Expressed in liver (PubMed:11572089, PubMed:22010862, PubMed:3571241).
Expressed in the cortico-medullary border region of the bursa of Fabricius by the bursal secretory dendritic-like cells (PubMed:15252730).
Highly expressed in the magnum of the oviduct, and at a lower level in uterus. Weakly expressed in white isthmus and very weakly in infundibulum. Not expressed in duodenum and kidney (PubMed:22010862).
Induction
Expression is regulated by dietary stress. Significantly increased expression between days 0 to 5 in egg whites of eggs laid by corticosterone-fed hens (at protein level). Decreased expression at day 14 in the magnum of the oviduct in the corticosterone-fed laying hens (PubMed:25436390).
Significantly increased expression by estrogen. Rapidly up-regulated within 0.5 hour after extrogen exposure with a peak at 1-4 hours and diminishing thereafter (PubMed:11572089).
Up-regulated during sexual maturation of pullets (PubMed:22010862).
Significantly increased expression by estrogen. Rapidly up-regulated within 0.5 hour after extrogen exposure with a peak at 1-4 hours and diminishing thereafter (PubMed:11572089).
Up-regulated during sexual maturation of pullets (PubMed:22010862).
Developmental stage
Expressed in liver of pre-laying and egg-laying hens throughout sexual maturation. Expression increases gradually from 13 weeks of age reaching its maximum at 15 weeks of age (pre-laying hens). A significant decrease in expression is observed in 41-week-old hens (egg-laying), a level that is significantly lower than that measured initially in 13-week-old pullets.
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P10184 | P00766 | 2 | EBI-6663991, EBI-6664027 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 67-132 | Kazal-like 1 | ||||
Sequence: FGIEVNCSLYASGIGKDGTSWVACPRNLKPVCGTDGSTYSNECGICLYNREHGANVEKEYDGECRP | ||||||
Domain | 133-197 | Kazal-like 2 | ||||
Sequence: KHVTIDCSPYLQVVRDGNTMVACPRILKPVCGSDSFTYDNECGICAYNAEHHTNISKLHDGECKL | ||||||
Domain | 198-263 | Kazal-like 3 | ||||
Sequence: EIGSVDCSKYPSTVSKDGRTLVACPRILSPVCGTDGFTYDNECGICAHNAEQRTHVSKKHDGKCRQ | ||||||
Domain | 264-329 | Kazal-like 4 | ||||
Sequence: EIPEIDCDQYPTRKTTGGKLLVRCPRILLPVCGTDGFTYDNECGICAHNAQHGTEVKKSHDGRCKE | ||||||
Domain | 330-394 | Kazal-like 5 | ||||
Sequence: RSTPLDCTQYLSNTQNGEAITACPFILQEVCGTDGVTYSNDCSLCAHNIELGTSVAKKHDGRCRE | ||||||
Domain | 395-460 | Kazal-like 6 | ||||
Sequence: EVPELDCSKYKTSTLKDGRQVVACTMIYDPVCATNGVTYASECTLCAHNLEQRTNLGKRKNGRCEE | ||||||
Domain | 461-517 | Kazal-like 7 | ||||
Sequence: DITKEHCREFQKVSPICTMEYVPHCGSDGVTYSNRCFFCNAYVQSNRTLNLVSMAAC |
Domain
Seems to have at least five separate non-overlapping active inhibitory domains; two for trypsin, two for chymotrypsin and one for elastase. They can be bound to the domains simultaneously.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P10184-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length517
- Mass (Da)57,005
- Last updated2020-06-17 v3
- ChecksumA3E2DE5570597C1C
P10184-2
- Name2
- Differences from canonical
- 1-70: MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQFVQVALALCCFADIAFGIE → MIPQ
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_060580 | 1-70 | in isoform 2 | |||
Sequence: MTDWVLHHKVGPLDMTTRYIFPLLPLPFLPHSESKRAVCAPRCSAMRTARQFVQVALALCCFADIAFGIE → MIPQ | ||||||
Sequence conflict | 136 | in Ref. 2; AAA48994/AA sequence and 5; AA sequence | ||||
Sequence: T → M | ||||||
Sequence conflict | 378 | in Ref. 2; AA sequence | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AADN05000072 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
M16141 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M15962 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16127 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16128 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16129 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16130 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16131 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16132 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16133 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16134 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16135 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16136 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16137 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16138 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16139 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
M16140 EMBL· GenBank· DDBJ | AAA48994.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AY225161 EMBL· GenBank· DDBJ | AAP50264.1 EMBL· GenBank· DDBJ | Genomic DNA |