IFNTA_SHEEP
ID IFNTA_SHEEP Reviewed; 195 AA.
AC Q08053;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Interferon tau-10;
DE Short=IFN-tau-10;
DE AltName: Full=Antiluteolysin;
DE AltName: Full=TP-02;
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=IFNT10;
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 [GENOMIC DNA].
RC TISSUE=Trophectoderm;
RX PubMed=8485241; DOI=10.1095/biolreprod48.4.768;
RA Nephew K.P., Whaley A.E., Christenson R.K., Imakawa K.;
RT "Differential expression of distinct mRNAs for ovine trophoblast protein-1
RT and related sheep type I interferons.";
RL Biol. Reprod. 48:768-778(1993).
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).
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}.
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DR EMBL; M88770; AAA31504.1; -; Genomic_DNA.
DR PIR; I47067; I47067.
DR AlphaFoldDB; Q08053; -.
DR SMR; Q08053; -.
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 2: Evidence at transcript level;
KW Antiviral defense; Cytokine; Disulfide bond; Glycoprotein; Hormone;
KW Pregnancy; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..195
FT /note="Interferon tau-10"
FT /id="PRO_0000016421"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..122
FT /evidence="ECO:0000250"
FT DISULFID 52..162
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 22069 MW; 16084C3184AC3963 CRC64;
MAFVLSLLMA LVLVSYGPGG SLGCYLSQRL MLDARENLRL LDRMNRLSPH SCLQDRKDFG
LPQEMVEGDQ LQEAQAFCVL YEMLQQSFNL FHTERSSAAW NTTLLEQLCT GLQQQLEDLD
TCRGPVMGEK DSELGKMDPI VTVKKYFQGI HDYLQEKGYS DCAWETVRVE MMRALTSSTT
LQKRLTKTGG DLNSP
