ID   IFNTB_SHEEP             Reviewed;         195 AA.
AC   P28169;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Interferon tau-11;
DE            Short=IFN-tau-11;
DE   AltName: Full=Antiluteolysin;
DE   AltName: Full=P4;
DE   AltName: Full=S4;
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=IFNT11;
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].
RX   PubMed=1374107; DOI=10.1089/jir.1992.12.1;
RA   Leaman D.W., Roberts R.M.;
RT   "Genes for the trophoblast interferons in sheep, goat, and musk ox and
RT   distribution of related genes among mammals.";
RL   J. Interferon Res. 12:1-11(1992).
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   MUTAGENESIS.
RX   PubMed=7929162; DOI=10.1016/s0021-9258(17)31466-7;
RA   Li J., Roberts R.M.;
RT   "Structure-function relationships in the interferon-tau (IFN-tau). Changes
RT   in receptor binding and in antiviral and antiproliferative activities
RT   resulting from site-directed mutagenesis performed near the carboxyl
RT   terminus.";
RL   J. Biol. Chem. 269:24826-24833(1994).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=9002652; DOI=10.1095/biolreprod56.1.214;
RA   Niswender K.D., Li J., Powell M.R., Loos K.R., Roberts R.M., Keisler D.H.,
RA   Smith M.F.;
RT   "Effect of variants of interferon-tau with mutations near the carboxyl
RT   terminus on luteal life span in sheep.";
RL   Biol. Reprod. 56:214-220(1997).
RN   [7]
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; M73241; AAA31573.1; -; Genomic_DNA.
DR   PIR; I47097; I47097.
DR   AlphaFoldDB; P28169; -.
DR   SMR; P28169; -.
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; 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-11"
FT                   /id="PRO_0000016422"
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"
FT   MUTAGEN         166
FT                   /note="I->T: 20-fold reduction in receptor binding
FT                   activity, greatly reduces antiviral and almost abolishes
FT                   antiproliferative activity."
FT   MUTAGEN         183
FT                   /note="Missing: Little effect on receptor binding activity
FT                   but greatly reduces antiviral and almost abolishes
FT                   antiproliferative activity."
FT   MUTAGEN         185..195
FT                   /note="Missing: Little effect on receptor binding activity
FT                   but greatly reduces antiviral and almost abolishes
FT                   antiproliferative activity."
SQ   SEQUENCE   195 AA;  22244 MW;  DC6321E42BDF948A CRC64;
     MAFVLSLLMA LVLVSYGPGG SLGCYLSQRL MLDARENLRL LDRMNRLSPH SCLQDRKDFG
     LPQEMVEGDQ LQEAQAFCVL YEMLQQSFNL FHTERSSAAW NTTLLEQLCT GLQQQLEDLD
     TCRGPVMGEK DSELGKMDPI VTVKKYFQGI HFYLKEKEYS DCAWEIVRVE MMRALSSSTS
     LQERLRKMGG DLNSP