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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)DescriptionActionsGraphical viewLength
Metal bindingi79Iron 11
Metal bindingi111Iron 11
Binding sitei136Carbonate 11
Binding sitei140Carbonate 11
Binding sitei142Carbonate 1; via amide nitrogen1
Binding sitei143Carbonate 1; via amide nitrogen1
Metal bindingi210Iron 11
Metal bindingi269Iron 11
Metal bindingi414Iron 21
Metal bindingi450Iron 21
Binding sitei475Carbonate 21
Binding sitei479Carbonate 21
Binding sitei481Carbonate 2; via amide nitrogen1
Binding sitei482Carbonate 2; via amide nitrogen1
Metal bindingi543Iron 21
Metal bindingi611Iron 21

GO - Molecular functioni

  • ferric iron binding Source: AgBase
  • iron ion binding Source: AgBase

GO - Biological processi

  • acute-phase response Source: AgBase
  • antimicrobial humoral response Source: AgBase
  • extracellular sequestering of iron ion Source: AgBase
  • intracellular sequestering of iron ion Source: AgBase
  • iron ion transport Source: AgBase
  • response to drug Source: AgBase
  • 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

  • cell Source: GOC
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003571920 – 705OvotransferrinAdd BLAST686

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Glycosylationi492N-linked (GlcNAc...)1 Publication1
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 interactor.
IntActiP02789. 2 interactors.

Structurei

Secondary structure

1705
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 32Combined sources9
Helixi33 – 45Combined sources13
Turni46 – 48Combined sources3
Beta strandi49 – 57Combined sources9
Helixi61 – 69Combined sources9
Turni70 – 72Combined sources3
Beta strandi75 – 78Combined sources4
Helixi80 – 87Combined sources8
Turni89 – 91Combined sources3
Beta strandi94 – 102Combined sources9
Beta strandi104 – 118Combined sources15
Helixi125 – 127Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi132 – 136Combined sources5
Turni141 – 144Combined sources4
Helixi145 – 153Combined sources9
Beta strandi155 – 157Combined sources3
Helixi162 – 164Combined sources3
Helixi167 – 174Combined sources8
Beta strandi175 – 179Combined sources5
Helixi187 – 190Combined sources4
Turni197 – 201Combined sources5
Beta strandi205 – 207Combined sources3
Helixi209 – 218Combined sources10
Beta strandi223 – 228Combined sources6
Helixi231 – 235Combined sources5
Beta strandi237 – 239Combined sources3
Helixi240 – 242Combined sources3
Beta strandi243 – 246Combined sources4
Beta strandi248 – 250Combined sources3
Beta strandi252 – 254Combined sources3
Helixi255 – 257Combined sources3
Turni258 – 260Combined sources3
Beta strandi263 – 267Combined sources5
Beta strandi270 – 273Combined sources4
Beta strandi275 – 277Combined sources3
Helixi279 – 293Combined sources15
Beta strandi294 – 296Combined sources3
Beta strandi298 – 300Combined sources3
Beta strandi308 – 310Combined sources3
Helixi312 – 314Combined sources3
Beta strandi315 – 319Combined sources5
Beta strandi323 – 328Combined sources6
Helixi335 – 339Combined sources5
Helixi341 – 350Combined sources10
Beta strandi354 – 357Combined sources4
Turni359 – 362Combined sources4
Beta strandi363 – 369Combined sources7
Helixi370 – 383Combined sources14
Turni384 – 386Combined sources3
Beta strandi387 – 395Combined sources9
Helixi396 – 405Combined sources10
Beta strandi410 – 413Combined sources4
Helixi415 – 423Combined sources9
Beta strandi427 – 433Combined sources7
Helixi437 – 439Combined sources3
Beta strandi441 – 445Combined sources5
Beta strandi450 – 460Combined sources11
Helixi465 – 467Combined sources3
Beta strandi470 – 475Combined sources6
Turni480 – 483Combined sources4
Helixi484 – 494Combined sources11
Helixi499 – 501Combined sources3
Beta strandi503 – 507Combined sources5
Beta strandi513 – 515Combined sources3
Helixi516 – 518Combined sources3
Beta strandi525 – 528Combined sources4
Beta strandi534 – 540Combined sources7
Helixi542 – 552Combined sources11
Beta strandi555 – 560Combined sources6
Helixi563 – 566Combined sources4
Beta strandi568 – 571Combined sources4
Turni575 – 579Combined sources5
Helixi582 – 584Combined sources3
Beta strandi585 – 588Combined sources4
Beta strandi590 – 592Combined sources3
Beta strandi594 – 596Combined sources3
Helixi597 – 602Combined sources6
Beta strandi605 – 608Combined sources4
Beta strandi612 – 615Combined sources4
Helixi617 – 619Combined sources3
Helixi620 – 634Combined sources15
Turni639 – 643Combined sources5
Beta strandi650 – 652Combined sources3
Beta strandi654 – 656Combined sources3
Beta strandi662 – 665Combined sources4
Helixi672 – 676Combined sources5
Helixi678 – 687Combined sources10
Turni688 – 690Combined sources3
Helixi694 – 703Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02789.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 352Transferrin-like 1PROSITE-ProRule annotationAdd BLAST327
Domaini364 – 689Transferrin-like 2PROSITE-ProRule annotationAdd BLAST326

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni352 – 360Connecting region9

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)DescriptionActionsGraphical viewLength
Sequence conflicti132T → N in CAA26040 (PubMed:7060577).Curated1
Sequence conflicti317L → F in CAA26040 (PubMed:7060577).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti83A → V.1
Natural varianti100V → I.1
Natural varianti154R → W.1
Natural varianti239 – 240QK → LN.2
Natural varianti686S → N.1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676501. 1 interactor.
IntActiP02789. 2 interactors.

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...

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: November 2, 2016
This is version 141 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.