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P02789 (TRFE_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ovotransferrin
Alternative name(s):
Allergen Gal d III
Conalbumin
Serum transferrin
Allergen=Gal d 3
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transferrins are iron binding transport proteins which can bind two Fe3+ ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.

Subunit structure

Monomer.

Subcellular location

Secreted.

Post-translational modification

Different forms of hen transferrin are distinguished by their carbohydrate composition. Ovotransferrin and embryo serum transferrin but not adult serum transferrin, have bisecting N-acetylglucosamine. Transferrin secreted by embryo hepatocytes in primary culture is marked by the presence of (alpha1-6) fucosylation of the core N-acetylglucosamine. Serum transferrins also differ in the number of attached neuraminic acid residues. In both embryo forms, sialylation occurs on the Man (alpha 1-3)-linked antennae.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the transferrin family.

Contains 2 transferrin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.3
Chain20 – 705686Ovotransferrin
PRO_0000035719

Regions

Domain26 – 352327Transferrin-like 1
Domain364 – 689326Transferrin-like 2
Region352 – 3609Connecting region

Sites

Metal binding791Iron 1
Metal binding1111Iron 1
Metal binding2101Iron 1
Metal binding2691Iron 1
Metal binding4141Iron 2
Metal binding4501Iron 2
Metal binding5431Iron 2
Metal binding6111Iron 2
Binding site1361Carbonate 1
Binding site1401Carbonate 1
Binding site1421Carbonate 1; via amide nitrogen
Binding site1431Carbonate 1; via amide nitrogen
Binding site4751Carbonate 2
Binding site4791Carbonate 2
Binding site4811Carbonate 2; via amide nitrogen
Binding site4821Carbonate 2; via amide nitrogen

Amino acid modifications

Glycosylation4921N-linked (GlcNAc...) Ref.4
Disulfide bond29 ↔ 64 Ref.4 Ref.6
Disulfide bond39 ↔ 55 Ref.6
Disulfide bond134 ↔ 216 Ref.4 Ref.6
Disulfide bond179 ↔ 193 Ref.4 Ref.6
Disulfide bond190 ↔ 201 Ref.4 Ref.6
Disulfide bond247 ↔ 261 Ref.4 Ref.6
Disulfide bond367 ↔ 399 Ref.4 Ref.6
Disulfide bond377 ↔ 390 Ref.6
Disulfide bond424 ↔ 699 Ref.6
Disulfide bond440 ↔ 662 Ref.4 Ref.6
Disulfide bond473 ↔ 549 Ref.4 Ref.6
Disulfide bond497 ↔ 690 Ref.4 Ref.6
Disulfide bond507 ↔ 521 Ref.6
Disulfide bond518 ↔ 532 Ref.6
Disulfide bond589 ↔ 603 Ref.6

Natural variations

Natural variant831A → V.
Natural variant1001V → I.
Natural variant1541R → W.
Natural variant239 – 2402QK → LN.
Natural variant6861S → N.

Experimental info

Sequence conflict1321T → N in CAA26040. Ref.1
Sequence conflict3171L → F in CAA26040. Ref.1

Secondary structure

1 ............................................................................................................................... 705
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02789 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 864201A93146FA84

FASTA70577,777
        10         20         30         40         50         60 
MKLILCTVLS LGIAAVCFAA PPKSVIRWCT ISSPEEKKCN NLRDLTQQER ISLTCVQKAT 

        70         80         90        100        110        120 
YLDCIKAIAN NEADAISLDG GQAFEAGLAP YKLKPIAAEV YEHTEGSTTS YYAVAVVKKG 

       130        140        150        160        170        180 
TEFTVNDLQG KTSCHTGLGR SAGWNIPIGT LLHRGAIEWE GIESGSVEQA VAKFFSASCV 

       190        200        210        220        230        240 
PGATIEQKLC RQCKGDPKTK CARNAPYSGY SGAFHCLKDG KGDVAFVKHT TVNENAPDQK 

       250        260        270        280        290        300 
DEYELLCLDG SRQPVDNYKT CNWARVAAHA VVARDDNKVE DIWSFLSKAQ SDFGVDTKSD 

       310        320        330        340        350        360 
FHLFGPPGKK DPVLKDLLFK DSAIMLKRVP SLMDSQLYLG FEYYSAIQSM RKDQLTPSPR 

       370        380        390        400        410        420 
ENRIQWCAVG KDEKSKCDRW SVVSNGDVEC TVVDETKDCI IKIMKGEADA VALDGGLVYT 

       430        440        450        460        470        480 
AGVCGLVPVM AERYDDESQC SKTDERPASY FAVAVARKDS NVNWNNLKGK KSCHTAVGRT 

       490        500        510        520        530        540 
AGWVIPMGLI HNRTGTCNFD EYFSEGCAPG SPPNSRLCQL CQGSGGIPPE KCVASSHEKY 

       550        560        570        580        590        600 
FGYTGALRCL VEKGDVAFIQ HSTVEENTGG KNKADWAKNL QMDDFELLCT DGRRANVMDY 

       610        620        630        640        650        660 
RECNLAEVPT HAVVVRPEKA NKIRDLLERQ EKRFGVNGSE KSKFMMFESQ NKDLLFKDLT 

       670        680        690        700 
KCLFKVREGT TYKEFLGDKF YTVISSLKTC NPSDILQMCS FLEGK

« Hide

References

[1]"The complete nucleotide sequence of the chicken ovotransferrin mRNA."
Jeltsch J.-M., Chambon P.
Eur. J. Biochem. 122:291-295(1982) [PubMed: 7060577] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence of the chicken ovotransferrin gene."
Jeltsch J.-M., Hen R., Maroteaux L., Garnier J.-M., Chambon P.
Nucleic Acids Res. 15:7643-7645(1987) [PubMed: 3658709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Identical precursors for serum transferrin and egg white conalbumin."
Thibodeau S.N., Lee D.C., Palmiter R.D.
J. Biol. Chem. 253:3771-3774(1978) [PubMed: 649604] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-19.
Tissue: Egg white and Serum.
[4]"The primary structure of hen ovotransferrin."
Williams J., Elleman T.C., Kingston I.B., Wilkins A.G., Kuhn K.A.
Eur. J. Biochem. 122:297-303(1982) [PubMed: 6895872] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[5]"The amino acid sequence of a carbohydrate-containing fragment of hen ovotransferrin."
Kingston I.B., Williams J.
Biochem. J. 147:463-472(1975) [PubMed: 1172663] [Abstract]
Cited for: PROTEIN SEQUENCE OF 480-582.
[6]"The amino acid sequences of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin."
Elleman T.C., Williams J.
Biochem. J. 116:515-532(1970) [PubMed: 4907959] [Abstract]
Cited for: DISULFIDE BONDS.
[7]"Investigation by 360-MHz 1H-nuclear-magnetic-resonance spectroscopy and methylation analysis of the single glycan chain of chicken ovotransferrin."
Dorland L., Haverkamp J., Vliegenthart J.F.G., Spik G., Fournet B., Montreuil J.
Eur. J. Biochem. 100:569-574(1979) [PubMed: 574451] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[8]"Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes."
Jacquinot P.-M., Leger D., Wieruszeski J.-M., Coddeville B., Montreuil J., Spik G.
Glycobiology 4:617-624(1994) [PubMed: 7881176] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[9]"Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin iron release."
Dewan J.C., Mikami B., Hirose M., Sacchettini J.C.
Biochemistry 32:11963-11968(1993) [PubMed: 8218271] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-351.
[10]"Crystal structure of diferric hen ovotransferrin at 2.4-A resolution."
Kurokawa H., Mikami B., Hirose M.
J. Mol. Biol. 254:196-207(1995) [PubMed: 7490743] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), METAL- AND CARBONATE-BINDING SITES.
[11]"Crystal structure of hen apo-ovotransferrin. Both lobes adopt an open conformation upon loss of iron."
Kurokawa H., Dewan J.C., Mikami B., Sacchettini J.C., Hirose M.
J. Biol. Chem. 274:28445-28452(1999) [PubMed: 10497206] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X02009 mRNA. Translation: CAA26040.1.
Y00407 Genomic DNA. Translation: CAA68468.1.
IPIIPI00683271.
PIRTFCHE. A26845.
RefSeqNP_990635.1. NM_205304.1.
UniGeneGga.47699.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIVX-ray3.00A20-705[»]
1IEJX-ray1.65A20-351[»]
1IQ7X-ray2.30A361-705[»]
1JL4X-ray4.30C153-165[»]
1N04X-ray2.80A20-705[»]
1NFTX-ray2.10A23-351[»]
1NNTX-ray2.30A24-351[»]
1OVTX-ray2.40A20-705[»]
1RYXX-ray3.50A20-705[»]
1TFAX-ray1.90A23-351[»]
2D3IX-ray2.15A20-705[»]
ProteinModelPortalP02789.
SMRP02789. Positions 20-705.
ModBaseSearch...

Protein-protein interaction databases

IntActP02789. 2 interactions.

Protein family/group databases

Allergome3293. Gal d 3.0101.
361. Gal d 3.
MEROPSS60.972.

PTM databases

GlycoSuiteDBP02789.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396241.
KEGGgga:396241.

Organism-specific databases

CTD4057.

Phylogenomic databases

eggNOGveNOG05880.
HOVERGENHBG000055.

Family and domain databases

InterProIPR001156. Peptidase_S60.
IPR016357. Transferrin.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
KOK14736.
PANTHERPTHR11485. Peptidase_S60. 1 hit.
PfamPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFPIRSF002549. Transferrin. 1 hit.
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEPS00205. TRANSFERRIN_LIKE_1. 2 hits.
PS00206. TRANSFERRIN_LIKE_2. 2 hits.
PS00207. TRANSFERRIN_LIKE_3. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRFE_CHICK
AccessionPrimary (citable) accession number: P02789
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents