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UniProtKB/Swiss-Prot entry P56828


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IFNT1_SHEEP
Primary accession number P56828
Secondary accession number P08316
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on May 30, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 60)
Name and origin of the protein
Protein name Interferon tau-1 [Precursor]
Synonyms IFN-tau1
Trophoblast protein 1
TP-1
Trophoblastin
Antiluteolysin
Trophoblast antiluteolytic protein
Gene name
Name: IFNT1
Synonyms: OTP
From
Ovis aries (Sheep) [TaxID: 9940] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Caprinae; Ovis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Trophoblast;
DOI=10.1038/330377a0; PubMed=2446135 [NCBI, ExPASy, EBI, Israel, Japan]
Imakawa K., Antony R.V., Kazemi M., Marotti K.R., Polites H.G., Roberts R.M.;
"Interferon-like sequence of ovine trophoblast protein secreted by embryonic trophectoderm.";
Nature 330:377-379(1987).
[2]
FUNCTION.
DOI=10.1210/en.137.3.1144; PubMed=8603586 [NCBI, ExPASy, EBI, Israel, Japan]
Spencer T.E., Bazer F.W.;
"Ovine interferon tau suppresses transcription of the estrogen receptor and oxytocin receptor genes in the ovine endometrium.";
Endocrinology 137:1144-1147(1996).
[3]
CIRCULAR DICHROISM ANALYSIS, AND 3D-STRUCTURE MODELING.
DOI=10.1093/protein/7.7.863; PubMed=7971949 [NCBI, ExPASy, EBI, Israel, Japan]
Jarpe M.A., Johnson H.M., Bazer F.W., Ott T.L., Curto E.V., Krishna N.R., Pontzer C.H.;
"Predicted structural motif of IFN tau.";
Protein Eng. 7:863-867(1994).
[4]
3D-STRUCTURE MODELING.
PubMed=8746786 [NCBI, ExPASy, EBI, Israel, Japan]
Senda T., Saitoh S., Mitsui Y., Li J., Roberts R.M.;
"A three-dimensional model of interferon-tau.";
J. Interferon Cytokine Res. 15:1053-1060(1995).
[5]
REVIEW.
DOI=10.1016/S0300-9084(99)80029-7; PubMed=9865498 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Biochimie 80:755-777(1998).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-195, AND DISULFIDE BONDS.
DOI=10.1006/jmbi.1998.2480; PubMed=9931256 [NCBI, ExPASy, EBI, Israel, Japan]
Radhakrishnan R., Walter L.J., Subramaniam P.S., Johnson H.M., Walter M.R.;
"Crystal structure of ovine interferon-tau at 2.1 A resolution.";
J. Mol. Biol. 286:151-162(1999).
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.
  • SIMILARITY: Belongs to the alpha/beta interferon family. IFN-alphaII subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00287; CAA68396.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001116871.1; -.
3D structure databases
PDB
1B5L; X-ray; 2.10 A; A=24-195.[ExPASy / RCSB / EBI]
PDBsum 1B5L; -.
ModBase P56828.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR000471; Interferon_abd.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR11691; Interferon_abd; 1.
Pfam PF00143; Interferon; 1.
Pfam graphical view of domain structure.
PRINTS PR00266; INTERFERONAB.
ProDom PD000550; Interferon_abd; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00076; IFabd; 1.
SMART graphical view of domain structure.
PROSITE PS00252; INTERFERON_A_B_D; 1.
BLOCKS P56828.
Genome annotation databases
GeneID 100144750; -.
Phylogenomic databases
HOVERGEN P56828; -.
Other
ProtoNet P56828.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antiviral defense; Cytokine; Hormone; Pregnancy; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    23  23     By similarity. 
CHAIN   24   195  172     Interferon tau-1. PRO_0000016413
DISULFID   24   122         
DISULFID   52   162         
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      
Sequence information
Length: 195 AA [This is the length of the unprocessed precursor] Molecular weight: 22193 Da [This is the MW of the unprocessed precursor] CRC64: A4965AE25DEA5BC9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAFVLSLLMA LVLVSYGPGG SLGCYLSRKL MLDARENLKL LDRMNRLSPH SCLQDRKDFG 

        70         80         90        100        110        120 
LPQEMVEGDQ LQKDQAFPVL YEMLQQSFNL FYTEHSSAAW DTTLLEQLCT GLQQQLDHLD 

       130        140        150        160        170        180 
TCRGQVMGEE DSELGNMDPI VTVKKYFQGI YDYLQEKGYS DCAWEIVRVE MMRALTVSTT 

       190 
LQKRLTKMGG DLNSP 

P56828 in FASTA format

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