Reviewed,
UniProtKB/Swiss-Prot P56828 (IFNT1_SHEEP)
Last modified
November 25, 2008.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Interferon tau-1 Short name=IFN-tau1 Alternative name(s): Trophoblast protein 1 Short name=TP-1 Trophoblastin Antiluteolysin Trophoblast antiluteolytic protein | ||||
| Gene names |
| ||||
| Organism | Ovis aries (Sheep) | ||||
| Taxonomic identifier | 9940 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Protein attributes
| Sequence length | 195 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity. This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus. In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties. In contrast with other IFNs, IFN-tau is not virally inducible. |
| Subcellular location | Secreted. Note= Secreted into the uterine lumen. |
| Tissue specificity | Constitutively and exclusively expressed in the mononuclear cells of the extraembryonic trophectoderm. |
| Developmental stage | Major secretory product synthesized by the sheep conceptus between days 13 and 21 of pregnancy. |
| Miscellaneous | IFN-tau genes are intronless. They evolved from IFN-omega genes in the ruminantia suborder and have continued to duplicate independently in different lineages of the ruminantia. They encode for proteins very similar in sequence but with different biological potency and pattern of expression. |
| Sequence similarities | Belongs to the alpha/beta interferon family. IFN-alphaII subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Antiviral defense Pregnancy |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Cytokine Hormone |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | defense response Inferred from electronic annotation. Source: InterPro female pregnancyInferred from electronic annotation. Source: UniProtKB-KW response to virusInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | hematopoietin/interferon-class (D200-domain) cytokine receptor binding Inferred from electronic annotation. Source: InterPro hormone activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | By similarity | |||||||||||||||||||
| Chain | 24 – 195 | 172 | Interferon tau-1 | PRO_0000016413 | ||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||
| Disulfide bond | 24 ↔ 122 | |||||||||||||||||||||
| Disulfide bond | 52 ↔ 162 | |||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Helix | 27 – 46 | 20 | ||||||||||||||||||||
| Helix | 64 – 68 | 5 | ||||||||||||||||||||
| Helix | 73 – 95 | 23 | ||||||||||||||||||||
| Helix | 103 – 122 | 20 | ||||||||||||||||||||
| Helix | 138 – 156 | 19 | ||||||||||||||||||||
| Turn | 157 – 159 | 3 | ||||||||||||||||||||
| Helix | 161 – 186 | 26 | ||||||||||||||||||||
Sequences
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References
| [1] | "Interferon-like sequence of ovine trophoblast protein secreted by embryonic trophectoderm." Imakawa K., Antony R.V., Kazemi M., Marotti K.R., Polites H.G., Roberts R.M. Nature 330:377-379(1987) [PubMed: 2446135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Trophoblast. |
| [2] | "Ovine interferon tau suppresses transcription of the estrogen receptor and oxytocin receptor genes in the ovine endometrium." Spencer T.E., Bazer F.W. Endocrinology 137:1144-1147(1996) [PubMed: 8603586] [Abstract] Cited for: FUNCTION. |
| [3] | "Predicted structural motif of IFN tau." Jarpe M.A., Johnson H.M., Bazer F.W., Ott T.L., Curto E.V., Krishna N.R., Pontzer C.H. Protein Eng. 7:863-867(1994) [PubMed: 7971949] [Abstract] Cited for: CIRCULAR DICHROISM ANALYSIS, 3D-STRUCTURE MODELING. |
| [4] | "A three-dimensional model of interferon-tau." Senda T., Saitoh S., Mitsui Y., Li J., Roberts R.M. J. Interferon Cytokine Res. 15:1053-1060(1995) [PubMed: 8746786] [Abstract] Cited for: 3D-STRUCTURE MODELING. |
| [5] | "IFN-tau: a novel subtype I IFN1. Structural characteristics, non-ubiquitous expression, structure-function relationships, a pregnancy hormonal embryonic signal and cross-species therapeutic potentialities." Martal J.L., Chene N.M., Huynh L.P., L'Haridon R.M., Reinaud P.B., Guillomot M.W., Charlier M.A., Charpigny S.Y. Biochimie 80:755-777(1998) [PubMed: 9865498] [Abstract] Cited for: REVIEW. |
| [6] | "Crystal structure of ovine interferon-tau at 2.1 A resolution." Radhakrishnan R., Walter L.J., Subramaniam P.S., Johnson H.M., Walter M.R. J. Mol. Biol. 286:151-162(1999) [PubMed: 9931256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-195, DISULFIDE BONDS. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Y00287 mRNA. Translation: CAA68396.1. | |||||||||||||
| RefSeq | NP_001116871.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 100144750. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P56828. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR012351. 4_helix_cytokine_core. IPR000471. Interferon_abd. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit. | ||||||||||||
| PANTHER | PTHR11691. Interferon_abd. 1 hit. | ||||||||||||
| Pfam | PF00143. Interferon. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00266. INTERFERONAB. | ||||||||||||
| ProDom | PD000550. Interferon_abd. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| SMART | SM00076. IFabd. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00252. INTERFERON_A_B_D. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | IFNT1_SHEEP | ||||||||
| Accession | Primary (citable) accession number: P56828 Secondary accession number(s): P08316 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


