Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ovotransferrin

Gene
N/A
Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Iron 1
Metal bindingi111 – 1111Iron 1
Binding sitei136 – 1361Carbonate 1
Binding sitei140 – 1401Carbonate 1
Binding sitei142 – 1421Carbonate 1; via amide nitrogen
Binding sitei143 – 1431Carbonate 1; via amide nitrogen
Metal bindingi210 – 2101Iron 1
Metal bindingi269 – 2691Iron 1
Metal bindingi414 – 4141Iron 2
Metal bindingi450 – 4501Iron 2
Binding sitei475 – 4751Carbonate 2
Binding sitei479 – 4791Carbonate 2
Binding sitei481 – 4811Carbonate 2; via amide nitrogen
Binding sitei482 – 4821Carbonate 2; via amide nitrogen
Metal bindingi543 – 5431Iron 2
Metal bindingi611 – 6111Iron 2

GO - Molecular functioni

GO - Biological processi

  • acute-phase response Source: AgBase
  • ion transport Source: UniProtKB-KW
  • iron ion homeostasis Source: UniProtKB-KW
  • response to lipopolysaccharide Source: AgBase
Complete GO annotation...

Keywords - Biological processi

Ion transport, Iron transport, Transport

Keywords - Ligandi

Iron, Metal-binding

Protein family/group databases

MEROPSiS60.970.

Names & Taxonomyi

Protein namesi
Recommended name:
Ovotransferrin
Alternative name(s):
Allergen Gal d III
Conalbumin
Serum transferrin
Allergen: Gal d 3
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: AgBase
  • extracellular space Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3293. Gal d 3.0101.
361. Gal d 3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 705686OvotransferrinPRO_0000035719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 64PROSITE-ProRule annotation2 Publications
Disulfide bondi39 ↔ 55PROSITE-ProRule annotation1 Publication
Disulfide bondi134 ↔ 216PROSITE-ProRule annotation2 Publications
Disulfide bondi179 ↔ 193PROSITE-ProRule annotation2 Publications
Disulfide bondi190 ↔ 201PROSITE-ProRule annotation2 Publications
Disulfide bondi247 ↔ 261PROSITE-ProRule annotation2 Publications
Disulfide bondi367 ↔ 399PROSITE-ProRule annotation2 Publications
Disulfide bondi377 ↔ 390PROSITE-ProRule annotation1 Publication
Disulfide bondi424 ↔ 699PROSITE-ProRule annotation1 Publication
Disulfide bondi440 ↔ 662PROSITE-ProRule annotation2 Publications
Disulfide bondi473 ↔ 549PROSITE-ProRule annotation2 Publications
Glycosylationi492 – 4921N-linked (GlcNAc...)1 Publication
Disulfide bondi497 ↔ 690PROSITE-ProRule annotation2 Publications
Disulfide bondi507 ↔ 521PROSITE-ProRule annotation1 Publication
Disulfide bondi518 ↔ 532PROSITE-ProRule annotation1 Publication
Disulfide bondi589 ↔ 603PROSITE-ProRule annotation1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP02789.

PTM databases

UniCarbKBiP02789.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi676501. 1 interaction.
IntActiP02789. 2 interactions.

Structurei

Secondary structure

1
705
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 329Combined sources
Helixi33 – 4513Combined sources
Turni46 – 483Combined sources
Beta strandi49 – 579Combined sources
Helixi61 – 699Combined sources
Turni70 – 723Combined sources
Beta strandi75 – 784Combined sources
Helixi80 – 878Combined sources
Turni89 – 913Combined sources
Beta strandi94 – 1029Combined sources
Beta strandi104 – 11815Combined sources
Helixi125 – 1273Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi132 – 1365Combined sources
Turni141 – 1444Combined sources
Helixi145 – 1539Combined sources
Beta strandi155 – 1573Combined sources
Helixi162 – 1643Combined sources
Helixi167 – 1748Combined sources
Beta strandi175 – 1795Combined sources
Helixi187 – 1904Combined sources
Turni197 – 2015Combined sources
Beta strandi205 – 2073Combined sources
Helixi209 – 21810Combined sources
Beta strandi223 – 2286Combined sources
Helixi231 – 2355Combined sources
Beta strandi237 – 2393Combined sources
Helixi240 – 2423Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi252 – 2543Combined sources
Helixi255 – 2573Combined sources
Turni258 – 2603Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi275 – 2773Combined sources
Helixi279 – 29315Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi308 – 3103Combined sources
Helixi312 – 3143Combined sources
Beta strandi315 – 3195Combined sources
Beta strandi323 – 3286Combined sources
Helixi335 – 3395Combined sources
Helixi341 – 35010Combined sources
Beta strandi354 – 3574Combined sources
Turni359 – 3624Combined sources
Beta strandi363 – 3697Combined sources
Helixi370 – 38314Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3959Combined sources
Helixi396 – 40510Combined sources
Beta strandi410 – 4134Combined sources
Helixi415 – 4239Combined sources
Beta strandi427 – 4337Combined sources
Helixi437 – 4393Combined sources
Beta strandi441 – 4455Combined sources
Beta strandi450 – 46011Combined sources
Helixi465 – 4673Combined sources
Beta strandi470 – 4756Combined sources
Turni480 – 4834Combined sources
Helixi484 – 49411Combined sources
Helixi499 – 5013Combined sources
Beta strandi503 – 5075Combined sources
Beta strandi513 – 5153Combined sources
Helixi516 – 5183Combined sources
Beta strandi525 – 5284Combined sources
Beta strandi534 – 5407Combined sources
Helixi542 – 55211Combined sources
Beta strandi555 – 5606Combined sources
Helixi563 – 5664Combined sources
Beta strandi568 – 5714Combined sources
Turni575 – 5795Combined sources
Helixi582 – 5843Combined sources
Beta strandi585 – 5884Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi594 – 5963Combined sources
Helixi597 – 6026Combined sources
Beta strandi605 – 6084Combined sources
Beta strandi612 – 6154Combined sources
Helixi617 – 6193Combined sources
Helixi620 – 63415Combined sources
Turni639 – 6435Combined sources
Beta strandi650 – 6523Combined sources
Beta strandi654 – 6563Combined sources
Beta strandi662 – 6654Combined sources
Helixi672 – 6765Combined sources
Helixi678 – 68710Combined sources
Turni688 – 6903Combined sources
Helixi694 – 70310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIVX-ray3.00A20-705[»]
1D9KX-ray3.20P/Q153-165[»]
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[»]
ProteinModelPortaliP02789.
SMRiP02789. Positions 20-705.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 352327Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 689326Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni352 – 3609Connecting region

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG000055.
KOiK14736.
PhylomeDBiP02789.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLILCTVLS LGIAAVCFAA PPKSVIRWCT ISSPEEKKCN NLRDLTQQER
60 70 80 90 100
ISLTCVQKAT YLDCIKAIAN NEADAISLDG GQAFEAGLAP YKLKPIAAEV
110 120 130 140 150
YEHTEGSTTS YYAVAVVKKG TEFTVNDLQG KTSCHTGLGR SAGWNIPIGT
160 170 180 190 200
LLHRGAIEWE GIESGSVEQA VAKFFSASCV PGATIEQKLC RQCKGDPKTK
210 220 230 240 250
CARNAPYSGY SGAFHCLKDG KGDVAFVKHT TVNENAPDQK DEYELLCLDG
260 270 280 290 300
SRQPVDNYKT CNWARVAAHA VVARDDNKVE DIWSFLSKAQ SDFGVDTKSD
310 320 330 340 350
FHLFGPPGKK DPVLKDLLFK DSAIMLKRVP SLMDSQLYLG FEYYSAIQSM
360 370 380 390 400
RKDQLTPSPR ENRIQWCAVG KDEKSKCDRW SVVSNGDVEC TVVDETKDCI
410 420 430 440 450
IKIMKGEADA VALDGGLVYT AGVCGLVPVM AERYDDESQC SKTDERPASY
460 470 480 490 500
FAVAVARKDS NVNWNNLKGK KSCHTAVGRT AGWVIPMGLI HNRTGTCNFD
510 520 530 540 550
EYFSEGCAPG SPPNSRLCQL CQGSGGIPPE KCVASSHEKY FGYTGALRCL
560 570 580 590 600
VEKGDVAFIQ HSTVEENTGG KNKADWAKNL QMDDFELLCT DGRRANVMDY
610 620 630 640 650
RECNLAEVPT HAVVVRPEKA NKIRDLLERQ EKRFGVNGSE KSKFMMFESQ
660 670 680 690 700
NKDLLFKDLT KCLFKVREGT TYKEFLGDKF YTVISSLKTC NPSDILQMCS

FLEGK
Length:705
Mass (Da):77,777
Last modified:February 1, 1996 - v2
Checksum:i864201A93146FA84
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321T → N in CAA26040 (PubMed:7060577).Curated
Sequence conflicti317 – 3171L → F in CAA26040 (PubMed:7060577).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831A → V.
Natural varianti100 – 1001V → I.
Natural varianti154 – 1541R → W.
Natural varianti239 – 2402QK → LN.
Natural varianti686 – 6861S → N.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02009 mRNA. Translation: CAA26040.1.
Y00407 Genomic DNA. Translation: CAA68468.1.
PIRiA26845. TFCHE.
RefSeqiNP_990635.1. NM_205304.1.
UniGeneiGga.2551.

Genome annotation databases

GeneIDi396241.
KEGGigga:396241.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02009 mRNA. Translation: CAA26040.1.
Y00407 Genomic DNA. Translation: CAA68468.1.
PIRiA26845. TFCHE.
RefSeqiNP_990635.1. NM_205304.1.
UniGeneiGga.2551.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIVX-ray3.00A20-705[»]
1D9KX-ray3.20P/Q153-165[»]
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[»]
ProteinModelPortaliP02789.
SMRiP02789. Positions 20-705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676501. 1 interaction.
IntActiP02789. 2 interactions.

Protein family/group databases

Allergomei3293. Gal d 3.0101.
361. Gal d 3.
MEROPSiS60.970.

PTM databases

UniCarbKBiP02789.

Proteomic databases

PRIDEiP02789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396241.
KEGGigga:396241.

Organism-specific databases

CTDi7018.

Phylogenomic databases

HOVERGENiHBG000055.
KOiK14736.
PhylomeDBiP02789.

Miscellaneous databases

EvolutionaryTraceiP02789.
PROiP02789.

Family and domain databases

InterProiIPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. 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]
ProtoNetiSearch...

Publicationsi

  1. "The complete nucleotide sequence of the chicken ovotransferrin mRNA."
    Jeltsch J.-M., Chambon P.
    Eur. J. Biochem. 122:291-295(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. 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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19.
    Tissue: Egg white and Serum.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiTRFE_CHICK
AccessioniPrimary (citable) accession number: P02789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.