IFNT1_SHEEP
ID IFNT1_SHEEP Reviewed; 195 AA.
AC P56828; P08316;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Interferon tau-1;
DE Short=IFN-tau-1;
DE AltName: Full=Antiluteolysin;
DE AltName: Full=Trophoblast antiluteolytic protein;
DE AltName: Full=Trophoblast protein 1;
DE Short=TP-1;
DE AltName: Full=Trophoblastin;
DE Flags: Precursor;
GN Name=IFNT1; Synonyms=OTP;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trophoblast;
RX PubMed=2446135; DOI=10.1038/330377a0;
RA Imakawa K., Antony R.V., Kazemi M., Marotti K.R., Polites H.G.,
RA Roberts R.M.;
RT "Interferon-like sequence of ovine trophoblast protein secreted by
RT embryonic trophectoderm.";
RL Nature 330:377-379(1987).
RN [2]
RP FUNCTION.
RX PubMed=8603586; DOI=10.1210/endo.137.3.8603586;
RA Spencer T.E., Bazer F.W.;
RT "Ovine interferon tau suppresses transcription of the estrogen receptor and
RT oxytocin receptor genes in the ovine endometrium.";
RL Endocrinology 137:1144-1147(1996).
RN [3]
RP CIRCULAR DICHROISM ANALYSIS, AND 3D-STRUCTURE MODELING.
RX PubMed=7971949; DOI=10.1093/protein/7.7.863;
RA Jarpe M.A., Johnson H.M., Bazer F.W., Ott T.L., Curto E.V., Krishna N.R.,
RA Pontzer C.H.;
RT "Predicted structural motif of IFN tau.";
RL Protein Eng. 7:863-867(1994).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=8746786; DOI=10.1089/jir.1995.15.1053;
RA Senda T., Saitoh S., Mitsui Y., Li J., Roberts R.M.;
RT "A three-dimensional model of interferon-tau.";
RL J. Interferon Cytokine Res. 15:1053-1060(1995).
RN [5]
RP REVIEW.
RX PubMed=9865498; DOI=10.1016/s0300-9084(99)80029-7;
RA Martal J.L., Chene N.M., Huynh L.P., L'Haridon R.M., Reinaud P.B.,
RA Guillomot M.W., Charlier M.A., Charpigny S.Y.;
RT "IFN-tau: a novel subtype I IFN1. Structural characteristics, non-
RT ubiquitous expression, structure-function relationships, a pregnancy
RT hormonal embryonic signal and cross-species therapeutic potentialities.";
RL Biochimie 80:755-777(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-195, AND DISULFIDE BONDS.
RX PubMed=9931256; DOI=10.1006/jmbi.1998.2480;
RA Radhakrishnan R., Walter L.J., Subramaniam P.S., Johnson H.M., Walter M.R.;
RT "Crystal structure of ovine interferon-tau at 2.1 A resolution.";
RL J. Mol. Biol. 286:151-162(1999).
CC -!- FUNCTION: Paracrine hormone primarily responsible for maternal
CC recognition of pregnancy. Interacts with endometrial receptors,
CC probably type I interferon receptors, and blocks estrogen receptor
CC expression, preventing the estrogen-induced increase in oxytocin
CC receptor expression in the endometrium. This results in the suppression
CC of the pulsatile endometrial release of the luteolytic hormone
CC prostaglandin F2-alpha, hindering the regression of the corpus luteum
CC (luteolysis) and therefore a return to ovarian cyclicity. This, and a
CC possible direct effect of IFN-tau on prostaglandin synthesis, leads in
CC turn to continued ovarian progesterone secretion, which stimulates the
CC secretion by the endometrium of the nutrients required for the growth
CC of the conceptus. In summary, displays particularly high antiviral and
CC antiproliferative potency concurrently with particular weak
CC cytotoxicity, high antiluteolytic activity and immunomodulatory
CC properties. In contrast with other IFNs, IFN-tau is not virally
CC inducible. {ECO:0000269|PubMed:8603586}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted into the uterine lumen.
CC -!- TISSUE SPECIFICITY: Constitutively and exclusively expressed in the
CC mononuclear cells of the extraembryonic trophectoderm.
CC -!- DEVELOPMENTAL STAGE: Major secretory product synthesized by the sheep
CC conceptus between days 13 and 21 of pregnancy.
CC -!- MISCELLANEOUS: IFN-tau genes are intronless. They evolved from IFN-
CC omega genes in the ruminantia suborder and have continued to duplicate
CC independently in different lineages of the ruminantia. They code for
CC proteins very similar in sequence but with different biological potency
CC and pattern of expression.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. IFN-alphaII
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00287; CAA68396.1; -; mRNA.
DR RefSeq; NP_001116871.1; NM_001123399.1.
DR PDB; 1B5L; X-ray; 2.10 A; A=24-195.
DR PDBsum; 1B5L; -.
DR AlphaFoldDB; P56828; -.
DR SMR; P56828; -.
DR GeneID; 100144750; -.
DR KEGG; oas:100144750; -.
DR CTD; 100144750; -.
DR OrthoDB; 1358010at2759; -.
DR EvolutionaryTrace; P56828; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR CDD; cd00095; IFab; 1.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000471; Interferon_alpha/beta/delta.
DR PANTHER; PTHR11691; PTHR11691; 1.
DR Pfam; PF00143; Interferon; 1.
DR PRINTS; PR00266; INTERFERONAB.
DR SMART; SM00076; IFabd; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00252; INTERFERON_A_B_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytokine; Disulfide bond; Hormone;
KW Pregnancy; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..195
FT /note="Interferon tau-1"
FT /id="PRO_0000016413"
FT DISULFID 24..122
FT /evidence="ECO:0000269|PubMed:9931256"
FT DISULFID 52..162
FT /evidence="ECO:0000269|PubMed:9931256"
FT HELIX 27..46
FT /evidence="ECO:0007829|PDB:1B5L"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:1B5L"
FT HELIX 73..95
FT /evidence="ECO:0007829|PDB:1B5L"
FT HELIX 103..122
FT /evidence="ECO:0007829|PDB:1B5L"
FT HELIX 138..156
FT /evidence="ECO:0007829|PDB:1B5L"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1B5L"
FT HELIX 161..186
FT /evidence="ECO:0007829|PDB:1B5L"
SQ SEQUENCE 195 AA; 22193 MW; A4965AE25DEA5BC9 CRC64;
MAFVLSLLMA LVLVSYGPGG SLGCYLSRKL MLDARENLKL LDRMNRLSPH SCLQDRKDFG
LPQEMVEGDQ LQKDQAFPVL YEMLQQSFNL FYTEHSSAAW DTTLLEQLCT GLQQQLDHLD
TCRGQVMGEE DSELGNMDPI VTVKKYFQGI YDYLQEKGYS DCAWEIVRVE MMRALTVSTT
LQKRLTKMGG DLNSP
