IFNT3_SHEEP
ID IFNT3_SHEEP Reviewed; 172 AA.
AC P56832;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Interferon tau-3;
DE Short=IFN-tau-3;
DE AltName: Full=Antiluteolysin;
DE AltName: Full=Trophoblast antiluteolytic protein;
DE AltName: Full=Trophoblast protein 1;
DE Short=TP-1;
DE AltName: Full=Trophoblastin;
GN Name=IFNT3;
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], AND VARIANTS SER-87; 124-SER-GLN-125 AND
RP TYR-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 [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 -!- POLYMORPHISM: There seem to be two variants of IFN-tau 3: A/P8V1 (shown
CC here) and B/P8V3. {ECO:0000269|Ref.1}.
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; AF158817; AAD44969.1; -; mRNA.
DR EMBL; AF158819; AAD44971.1; -; mRNA.
DR AlphaFoldDB; P56832; -.
DR SMR; P56832; -.
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; Hormone; Pregnancy;
KW Reference proteome; Secreted.
FT CHAIN 1..172
FT /note="Interferon tau-3"
FT /id="PRO_0000154309"
FT DISULFID 1..99
FT /evidence="ECO:0000250"
FT DISULFID 29..139
FT /evidence="ECO:0000250"
FT VARIANT 87
FT /note="T -> S (in IFN-tau3B)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 124..125
FT /note="FE -> SQ (in IFN-tau3B)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 130
FT /note="L -> Y (in IFN-tau3B)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 172 AA; 19867 MW; 7BFF1F036545C8E2 CRC64;
CYLSERLMLD ARENLKLLDR MNRLSPHSCL QDRKDFGLPQ EMVEGDQLQK DQAFPVLYEM
LQQSFNLFYT EHSSAAWDTT LLEQLCTGLQ QQLDHLDTCR GQVMGEEDSE LGNMDPIVTV
KKYFEGIYDL LQEKGYSDCA WEIVRVEMMR ALTVSTTLQK RLTKMGGDLN SP
