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IFNL3_CHICK
ID   IFNL3_CHICK             Reviewed;         186 AA.
AC   B4ER10; B2L226;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Interferon lambda-3;
DE            Short=IFN-lambda-3;
DE   AltName: Full=Interleukin-28B;
DE            Short=IL-28B;
DE   Flags: Precursor;
GN   Name=IFNL3; Synonyms=IFNL, IL28, IL28B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Spleen;
RX   PubMed=18593329; DOI=10.1089/jir.2007.0117;
RA   Karpala A.J., Morris K.R., Broadway M.M., McWaters P.G., O'Neil T.E.,
RA   Goossens K.E., Lowenthal J.W., Bean A.G.;
RT   "Molecular cloning, expression, and characterization of chicken IFN-
RT   lambda.";
RL   J. Interferon Cytokine Res. 28:341-350(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=24371053; DOI=10.1128/jvi.02764-13;
RA   Reuter A., Soubies S., Hartle S., Schusser B., Kaspers B., Staeheli P.,
RA   Rubbenstroth D.;
RT   "Antiviral activity of lambda interferon in chickens.";
RL   J. Virol. 88:2835-2843(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kaiser P., Rothwell L., Hu T.J.;
RT   "Characterisation of chicken interferon-lambda.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cao W., Chen W., Liu Y., Bu Z.;
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [6]
RP   REVIEW.
RX   PubMed=23751330; DOI=10.1016/j.dci.2013.05.020;
RA   Goossens K.E., Ward A.C., Lowenthal J.W., Bean A.G.;
RT   "Chicken interferons, their receptors and interferon-stimulated genes.";
RL   Dev. Comp. Immunol. 41:370-376(2013).
CC   -!- FUNCTION: Cytokine which plays a critical role in the antiviral host
CC       defense, predominantly in the epithelial tissues. Acts as a ligand for
CC       the heterodimeric class II cytokine receptor composed of IL10RB and
CC       IFNLR1, and receptor engagement leads to the activation of the JAK/STAT
CC       signaling pathway resulting in the expression of IFN-stimulated genes
CC       (ISG), which mediate the antiviral state. Has a restricted receptor
CC       distribution and therefore restricted targets: is primarily active in
CC       epithelial cells and this cell type-selective action is because of the
CC       epithelial cell-specific expression of its receptor IFNLR1. Exhibits
CC       antiviral activity against the H5N1 influenza A virus. Induces the
CC       expression of the antiviral MX protein in epithelial-rich tissues, such
CC       as intestine, trachea and lung. {ECO:0000269|PubMed:18593329,
CC       ECO:0000269|PubMed:24371053}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lambda interferon family. {ECO:0000305}.
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DR   EMBL; EF587763; ABU82742.1; -; mRNA.
DR   EMBL; KF680102; AHF20239.1; -; mRNA.
DR   EMBL; KF680103; AHF20240.1; -; mRNA.
DR   EMBL; AM773754; CAO79598.1; -; mRNA.
DR   EMBL; EU399904; ACC68984.1; -; mRNA.
DR   EMBL; AADN03016676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADN03020056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001121968.1; NM_001128496.1.
DR   RefSeq; XP_015144667.1; XM_015289181.1.
DR   AlphaFoldDB; B4ER10; -.
DR   SMR; B4ER10; -.
DR   STRING; 9031.ENSGALP00000041975; -.
DR   PaxDb; B4ER10; -.
DR   Ensembl; ENSGALT00000076823; ENSGALP00000052417; ENSGALG00000052146.
DR   Ensembl; ENSGALT00000090407; ENSGALP00000064877; ENSGALG00000047344.
DR   Ensembl; ENSGALT00000091564; ENSGALP00000066790; ENSGALG00000050947.
DR   GeneID; 770778; -.
DR   KEGG; gga:101751261; -.
DR   KEGG; gga:770778; -.
DR   CTD; 770778; -.
DR   VEuPathDB; HostDB:LOC112532795; -.
DR   eggNOG; ENOG502SSDC; Eukaryota.
DR   GeneTree; ENSGT00390000014310; -.
DR   HOGENOM; CLU_120266_0_0_1; -.
DR   OMA; HWLQKLE; -.
DR   OrthoDB; 1429532at2759; -.
DR   Reactome; R-GGA-449836; Other interleukin signaling.
DR   Reactome; R-GGA-8854691; Interleukin-20 family signaling.
DR   PRO; PR:B4ER10; -.
DR   Proteomes; UP000000539; Chromosome 7.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0045918; P:negative regulation of cytolysis; IDA:AgBase.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
DR   GO; GO:0050778; P:positive regulation of immune response; IEA:InterPro.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:AgBase.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR   Gene3D; 1.20.1250.60; -; 1.
DR   InterPro; IPR038326; IFN-lambda_sf.
DR   InterPro; IPR029177; INF_lambda.
DR   PANTHER; PTHR31943; PTHR31943; 1.
DR   Pfam; PF15177; IL28A; 1.
PE   2: Evidence at transcript level;
KW   Antiviral defense; Cytokine; Disulfide bond; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..186
FT                   /note="Interferon lambda-3"
FT                   /id="PRO_0000429980"
FT   DISULFID        31..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        178..185
FT                   /evidence="ECO:0000250"
FT   CONFLICT        150
FT                   /note="K -> E (in Ref. 1; ABU82742, 2; AHF20239 and 4;
FT                   ACC68984)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   186 AA;  21007 MW;  8AF223E182999133 CRC64;
     MVCYGVTIIL VGTLGSLLVG AFPQVTPKKS CSLSKYQFPA PLELKAVWRM KEQFEDIMLL
     TNRKCNTRLF HRKWDIAELS VPDRITLVEA ELDLTITVLT NPTTQRLAET CQQPLAFLTQ
     VQEDLRDCLA LEAPSHQPSG KLRHWLQKLK TAKKKETAGC LEASAILHIF QVLNDLRCAA
     QREDCT
 
 
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