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IFNT1_BOVIN
ID   IFNT1_BOVIN             Reviewed;         195 AA.
AC   P15696; P15694; Q28126; Q28127; Q28128; Q28191; Q95NE2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 135.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (IFN-TAU1A AND IFN-TAU1D).
RX   PubMed=2521687; DOI=10.1210/mend-3-1-127;
RA   Imakawa K., Hansen T.R., Malathy P.-V., Anthony R.V., Polites H.G.,
RA   Marotti K.R., Roberts R.M.;
RT   "Molecular cloning and characterization of complementary deoxyribonucleic
RT   acids corresponding to bovine trophoblast protein-1: a comparison with
RT   ovine trophoblast protein-1 and bovine interferon-alpha II.";
RL   Mol. Endocrinol. 3:127-139(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (IFN-TAU1C).
RC   TISSUE=Trophoblast;
RX   PubMed=2378676; DOI=10.1677/jme.0.0040275;
RA   Stewart H.J., McCann S.H., Flint A.P.F.;
RT   "Structure of an interferon-alpha 2 gene expressed in the bovine conceptus
RT   early in gestation.";
RL   J. Mol. Endocrinol. 4:275-282(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IFN-TAU1A; IFN-TAU1B AND IFN-TAU1D).
RX   PubMed=1704373; DOI=10.1016/s0021-9258(18)49954-1;
RA   Hansen T.R., Leaman D.W., Cross J.C., Mathialagan N., Bixby J.A.,
RA   Roberts R.M.;
RT   "The genes for the trophoblast interferons and the related interferon-alpha
RT   II possess distinct 5'-promoter and 3'-flanking sequences.";
RL   J. Biol. Chem. 266:3060-3067(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (IFN-TAU1C).
RC   TISSUE=Trophoblast;
RA   Stewart H.J.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE (INF-TAU1A).
RA   Roberts R.M.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE (INF-TAU1C).
RA   Chung Y.G., Seidel G.E. Jr.;
RT   "Cloning bovine interferon-tau genes and characterizing their
RT   transcriptional expression during early pregnancy.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 24-195 (IFN-TAU1C).
RA   Larson S.F., Liu L., Winkelman G.L., Kubisch H.M., Bixby J.A.,
RA   Roberts R.M., Ealy A.D.;
RT   "The expressed genes for bovine interferon-tau: identification and
RT   expression during conceptus development.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
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.
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 bovine
CC       conceptus between days 15 and 25 of pregnancy.
CC   -!- POLYMORPHISM: There seems to be four variants of IFN-tau 1: A, B (shown
CC       here), C and D.
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; M31557; AAA50458.2; -; mRNA.
DR   EMBL; M31556; AAA50457.1; -; mRNA.
DR   EMBL; X65539; CAA46506.1; -; Genomic_DNA.
DR   EMBL; M60903; AAB67325.1; -; Genomic_DNA.
DR   EMBL; M60913; AAA62712.1; -; Genomic_DNA.
DR   EMBL; M60908; AAA62711.1; -; Genomic_DNA.
DR   EMBL; AF238612; AAG14169.1; -; Genomic_DNA.
DR   EMBL; AF196320; AAF08671.2; -; mRNA.
DR   PIR; A39505; A39505.
DR   PIR; B39505; B39505.
DR   PIR; S23751; S23751.
DR   RefSeq; NP_001015511.3; NM_001015511.3.
DR   RefSeq; XP_015319926.1; XM_015464440.1.
DR   RefSeq; XP_015327911.1; XM_015472425.1.
DR   AlphaFoldDB; P15696; -.
DR   SMR; P15696; -.
DR   STRING; 9913.ENSBTAP00000047689; -.
DR   PaxDb; P15696; -.
DR   PRIDE; P15696; -.
DR   GeneID; 317698; -.
DR   KEGG; bta:317698; -.
DR   CTD; 317698; -.
DR   eggNOG; ENOG502T289; Eukaryota.
DR   InParanoid; P15696; -.
DR   OrthoDB; 1358010at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR   GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR   GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR   GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
DR   GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
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:0000305"
FT   CHAIN           24..195
FT                   /note="Interferon tau-1"
FT                   /id="PRO_0000016412"
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   VARIANT         29
FT                   /note="D -> N (in IFN-tau1D)"
FT   VARIANT         88
FT                   /note="F -> L (in IFN-tau1A)"
FT   VARIANT         169
FT                   /note="V -> M (in IFN-tau1C and IFN-tau1D)"
FT   CONFLICT        18
FT                   /note="P -> Q (in Ref. 1; AAA50458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="R -> E (in Ref. 1; AAA50457)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  22134 MW;  FF98CFA54AE86902 CRC64;
     MAFVLSLLMA LVLVSYGPGR SLGCYLSEDH MLGARENLRL LARMNRLSPH PCLQDRKDFG
     LPQEMVEGNQ LQKDQAISVL HEMLQQCFNL FYTEHSSAAW NTTLLEQLCT GLQQQLEDLD
     ACLGPVMGEK DSDMGRMGPI LTVKKYFQGI HVYLKEKEYS DCAWEIIRVE MMRALSSSTT
     LQKRLRKMGG DLNSL
 
 
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