IFNT2_SHEEP
ID IFNT2_SHEEP Reviewed; 195 AA.
AC P56829; P08316;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Interferon tau-2;
DE Short=IFN-tau-2;
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=IFNT2;
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] (IFN-TAU2C), AND VARIANT ASP-106.
RX PubMed=2530342;
RA Stewart H.J., Flint A.P., Lamming G.E., McCann S.H., Parkinson T.J.;
RT "Antiluteolytic effects of blastocyst-secreted interferon investigated in
RT vitro and in vivo in the sheep.";
RL J. Reprod. Fertil. Suppl. 37:127-138(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (IFN-TAU2C), AND VARIANT ASP-106.
RX PubMed=2475129; DOI=10.1677/jme.0.0020065;
RA Stewart H.J., McCann S.H., Northrop A.J., Lamming G.E., Flint A.P.;
RT "Sheep antiluteolytic interferon: cDNA sequence and analysis of mRNA
RT levels.";
RL J. Mol. Endocrinol. 2:65-70(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (IFN-TAU2C), AND VARIANT ASP-106.
RC TISSUE=Embryo;
RX PubMed=2753362; DOI=10.1016/0378-1119(89)90082-6;
RA Charlier M., Hue D., Martal J., Gaye P.;
RT "Cloning and expression of cDNA encoding ovine trophoblastin: its identity
RT with a class-II alpha interferon.";
RL Gene 77:341-348(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (IFN-TAU2C), AND VARIANT ASP-106.
RX PubMed=1701245; DOI=10.1093/nar/18.22.6724;
RA Klemann S.W., Imakawa K., Roberts R.M.;
RT "Sequence variability among ovine trophoblast interferon cDNA.";
RL Nucleic Acids Res. 18:6724-6724(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-195 (IFN-TAU2A AND IFN-TAU2B), AND VARIANT
RP LYS-130.
RC TISSUE=Embryo;
RA Winkelman G.L., Roberts R.M., Peterson A.J., Alexenko A.P., Ealy A.D.;
RT "Identification of the expressed forms of ovine interferon-tau in the peri-
RT implantation conceptus: sequence relationships and comparative biological
RT activities.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 24-68.
RX PubMed=3254170; DOI=10.1016/0014-5793(88)80574-x;
RA Charpigny G., Reinaud P., Huet J.-C., Guillomot M., Charlier M.,
RA Pernollet J.-C., Martal J.;
RT "High homology between a trophoblastic protein (trophoblastin) isolated
RT from ovine embryo and alpha-interferons.";
RL FEBS Lett. 228:12-16(1988).
RN [7]
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 [8]
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 [9]
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 [10]
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).
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 -!- POLYMORPHISM: There seems to be three variants of IFN-tau 2: A/P8V2/P7
CC (shown here), B/P8V4 and C/P8. {ECO:0000269|PubMed:1701245,
CC ECO:0000269|PubMed:2475129, ECO:0000269|PubMed:2530342,
CC ECO:0000269|PubMed:2753362, ECO:0000269|Ref.5}.
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}.
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DR EMBL; X07920; CAA30753.1; -; mRNA.
DR EMBL; M26386; AAA31584.1; -; mRNA.
DR EMBL; X56344; CAA39784.1; -; mRNA.
DR EMBL; X56345; CAA39785.1; -; mRNA.
DR EMBL; AF158818; AAD44970.1; -; mRNA.
DR EMBL; AF158820; AAD44972.1; -; mRNA.
DR PIR; S03799; JS0204.
DR RefSeq; NP_001116872.1; NM_001123400.1.
DR AlphaFoldDB; P56829; -.
DR SMR; P56829; -.
DR STRING; 9940.ENSOARP00000022793; -.
DR GeneID; 100144751; -.
DR CTD; 100144751; -.
DR eggNOG; ENOG502T289; Eukaryota.
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 Antiviral defense; Cytokine; Direct protein sequencing; Disulfide bond;
KW Hormone; Pregnancy; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3254170"
FT CHAIN 24..195
FT /note="Interferon tau-2"
FT /id="PRO_0000016414"
FT DISULFID 24..122
FT /evidence="ECO:0000250"
FT DISULFID 52..162
FT /evidence="ECO:0000250"
FT VARIANT 106
FT /note="E -> D (in IFN-tau2C)"
FT /evidence="ECO:0000269|PubMed:1701245,
FT ECO:0000269|PubMed:2475129, ECO:0000269|PubMed:2530342,
FT ECO:0000269|PubMed:2753362"
FT VARIANT 130
FT /note="E -> K (in IFN-tau2B)"
FT /evidence="ECO:0000269|Ref.5"
SQ SEQUENCE 195 AA; 22192 MW; EC4DEE507C269C67 CRC64;
MAFVLSLLMA LVLVSYGPGG SLGCYLSQRL MLDARENLKL LDRMNRLSPH SCLQDRKDFG
LPQEMVEGDQ LQKDQAFPVL YEMLQQSFNL FYTEHSSAAW DTTLLEQLCT GLQQQLDHLD
TCRGQVMGEE DSELGNMDPI VTVKKYFQGI YDYLQEKGYS DCAWEIVRVE MMRALTVSTT
LQKRLTKMGG DLNSP
