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P68390 (IOVO_MELGA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ovomucoid
OrganismMeleagris gallopavo (Common turkey) [Complete proteome]
Taxonomic identifier9103 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Meleagridinae › Meleagris

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted.

Domain

Avian ovomucoid consists of three homologous, tandem Kazal family inhibitory domains. Ref.2 Ref.3 Ref.4 Ref.5

Sequence similarities

Contains 3 Kazal-like domains.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase inhibitor activity

Inferred from direct assay. Source: AgBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Ovomucoid
PRO_0000073142

Regions

Domain1 – 6363Kazal-like 1
Domain64 – 12865Kazal-like 2
Domain131 – 18555Kazal-like 3

Sites

Site88 – 892Reactive bond 2 for trypsin
Site147 – 1482Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin

Amino acid modifications

Glycosylation1741N-linked (GlcNAc...)
Disulfide bond5 ↔ 43
Disulfide bond22 ↔ 40
Disulfide bond30 ↔ 61
Disulfide bond69 ↔ 108
Disulfide bond86 ↔ 105
Disulfide bond94 ↔ 126
Disulfide bond137 ↔ 167
Disulfide bond145 ↔ 164
Disulfide bond153 ↔ 185

Secondary structure

1 ........... 185
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68390 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 24BB83F5A66A1A76

FASTA18520,156
        10         20         30         40         50         60 
VEVDCSRFPN TTNEEGKDVL VCTEDLRPIC GTDGVTHSEC LLCAYNIEYG TNISKEHDGE 

        70         80         90        100        110        120 
CREAVPMDCS RYPNTTSEEG KVMILCNKAL NPVCGTDGVT YDNECVLCAH NLEQGTSVGK 

       130        140        150        160        170        180 
KHDGECRKEL AAVSVDCSEY PKPACTLEYR PLCGSDNKTY GNKCNFCNAV VESNGTLTLS 


HFGKC

« Hide

References

[1]"Evolution of avian ovomucoids."
Kato I., Kohr W.J., Laskowski M. Jr.
(In) Magnusson S., Ottesen M., Foltmann B., Dano K., Neurath H. (eds.); Regulatory proteolytic enzymes and their inhibitors, pp.197-206, Pergamon Press, New York (1978)
Cited for: PROTEIN SEQUENCE.
[2]"Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey."
Fujinaga M., Read R.J., Sielecki A., Ardelt W., Laskowski M. Jr., James M.N.G.
Proc. Natl. Acad. Sci. U.S.A. 79:4868-4872(1982) [PubMed: 6750612] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THIRD DOMAIN.
[3]Ding J., Qasim M.A., Laskowski M. Jr., James M.N.G.
Submitted (JUL-1997) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THIRD DOMAIN.
[4]"Conformation of the third domain of turkey ovomucoid in solution. Structural analysis by two-dimensional Overhauser nuclear effect spectroscopy."
Andrianov A.M.
Mol. Biol. (Mosk.) 25:1215-1225(1991) [PubMed: 1753953] [Abstract]
Cited for: STRUCTURE BY NMR OF THIRD DOMAIN.
[5]"Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data."
Krezel A.M., Darba P., Robertson A.D., Fejzo J., Macura S., Markley J.L.
J. Mol. Biol. 242:203-214(1994) [PubMed: 8089842] [Abstract]
Cited for: STRUCTURE BY NMR OF THIRD DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRTITKM. A01238.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHOX-ray1.80I130-185[»]
1CSOX-ray1.90I135-185[»]
1CT0X-ray1.80I135-185[»]
1CT2X-ray1.65I135-185[»]
1CT4X-ray1.60I135-185[»]
1DS2X-ray1.70I135-185[»]
1DS3X-ray1.65I135-185[»]
1HJAX-ray2.30I135-185[»]
1OMTNMR-A130-185[»]
1OMUNMR-A130-185[»]
1PPFX-ray1.80I130-185[»]
1R0RX-ray1.10I135-185[»]
1SGDX-ray1.80I135-185[»]
1SGEX-ray1.80I135-185[»]
1SGNX-ray1.80I135-185[»]
1SGPX-ray1.40I135-185[»]
1SGQX-ray1.90I135-185[»]
1SGRX-ray1.80I135-185[»]
1SGYX-ray1.80I135-185[»]
1TURNMR-A130-185[»]
1TUSNMR-A130-185[»]
1YU6X-ray1.55C/D1-185[»]
1Z7KX-ray1.90B65-126[»]
C12-15[»]
2GKRX-ray1.16I135-185[»]
2GKTX-ray1.23I135-185[»]
2GKVX-ray1.70A/B135-185[»]
2SGDX-ray1.80I135-185[»]
2SGEX-ray1.80I135-185[»]
2SGFX-ray1.75I135-185[»]
2SGPX-ray1.80I135-185[»]
2SGQX-ray1.80I135-185[»]
3SGBX-ray1.80I130-185[»]
3SGQX-ray1.80I135-185[»]
ProteinModelPortalP68390.
SMRP68390. Positions 1-61, 65-126, 130-185.
ModBaseSearch...

Protein family/group databases

Allergome2116. Mel g 1.
MEROPSI01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006172.

Family and domain databases

InterProIPR002350. Prot_inh_Kazal.
IPR001239. Prot_inh_Kazal-m.
IPR011497. Prot_Inh_Kazal_2.
[Graphical view]
PfamPF00050. Kazal_1. 2 hits.
PF07648. Kazal_2. 1 hit.
[Graphical view]
PRINTSPR00290. KAZALINHBTR.
SMARTSM00280. KAZAL. 3 hits.
[Graphical view]
PROSITEPS00282. KAZAL_1. 2 hits.
PS51465. KAZAL_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOVO_MELGA
AccessionPrimary (citable) accession number: P68390
Secondary accession number(s): P01004
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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