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INLR1_CHICK
ID   INLR1_CHICK             Reviewed;         567 AA.
AC   K9JA28; K9J9W8; W0FB28;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Interferon lambda receptor 1;
DE            Short=IFN-lambda R1;
DE   AltName: Full=Cytokine receptor class-II member 12;
DE   AltName: Full=Cytokine receptor family 2 member 12;
DE            Short=CRF2-12;
DE   AltName: Full=Interleukin-28 receptor subunit alpha;
DE            Short=IL-28 receptor subunit alpha;
DE            Short=IL-28R-alpha;
DE            Short=IL-28RA;
DE   Flags: Precursor;
GN   Name=IFNLR1; Synonyms=IL28RA;
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] (ISOFORMS 1 AND 2), AND FUNCTION.
RC   TISSUE=Lung;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Goossens K.E., Bean A.G., Lowenthal J.W.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine
CC       ligands IFNL2 and IFNL3 and mediates their antiviral activity. The
CC       ligand/receptor complex stimulate the activation of the JAK/STAT
CC       signaling pathway leading to the expression of IFN-stimulated genes
CC       (ISG), which contribute to the antiviral state. Determines the cell
CC       type specificity of the lambda interferon action. Shows a more
CC       restricted pattern of expression in the epithelial tissues thereby
CC       limiting responses to lambda interferons primarily to epithelial cells
CC       of the respiratory, gastrointestinal, and reproductive tracts.
CC       {ECO:0000269|PubMed:24371053}.
CC   -!- SUBUNIT: Heterodimer with IL10RB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=K9JA28-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=K9JA28-2; Sequence=VSP_055397, VSP_055398;
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC       {ECO:0000305}.
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DR   EMBL; KF680104; AHF20241.1; -; mRNA.
DR   EMBL; KF680105; AHF20242.1; -; mRNA.
DR   EMBL; FJ947118; ADB82986.1; -; mRNA.
DR   EMBL; FJ947119; ADB82987.1; -; mRNA.
DR   EMBL; JH374927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K9JA28; -.
DR   SMR; K9JA28; -.
DR   STRING; 9031.ENSGALP00000039657; -.
DR   PaxDb; K9JA28; -.
DR   Ensembl; ENSGALT00000098112; ENSGALP00000068923; ENSGALG00000004231. [K9JA28-1]
DR   VEuPathDB; HostDB:geneid_419694; -.
DR   VEuPathDB; HostDB:LOC121107463; -.
DR   eggNOG; ENOG502S4B0; Eukaryota.
DR   GeneTree; ENSGT00510000048978; -.
DR   OMA; GYEHTHY; -.
DR   OrthoDB; 762389at2759; -.
DR   Reactome; R-GGA-449836; Other interleukin signaling.
DR   Reactome; R-GGA-8854691; Interleukin-20 family signaling.
DR   PRO; PR:K9JA28; -.
DR   Proteomes; UP000000539; Chromosome 23.
DR   Bgee; ENSGALG00000004231; Expressed in colon and 11 other tissues.
DR   ExpressionAtlas; K9JA28; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0034342; P:response to type III interferon; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR   Pfam; PF09294; Interfer-bind; 1.
DR   Pfam; PF01108; Tissue_fac; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Antiviral defense; Disulfide bond; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..567
FT                   /note="Interferon lambda receptor 1"
FT                   /id="PRO_0000429981"
FT   TOPO_DOM        23..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..121
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..215
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         223..246
FT                   /note="EWKFPFSATIPVFVLLILLTSASI -> MTFLRKDVLRYQMRLQNIKEFHQN
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:24371053, ECO:0000303|Ref.2"
FT                   /id="VSP_055397"
FT   VAR_SEQ         247..567
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:24371053, ECO:0000303|Ref.2"
FT                   /id="VSP_055398"
FT   CONFLICT        124
FT                   /note="L -> P (in Ref. 1; AHF20242)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  64663 MW;  0E5AE2A73DB3DB4A CRC64;
     MSAWRIRVLA TLCFLWQPRV HGQLPPPQNV TLLSKDFDMI LTWTPGEGSP PDVLYTVRYE
     SKTRMDKWIK VPHCRNIHSV SCNLTCVIPN FFIKFRAQVK ATSGRFHSPW VKSQFKEYHL
     DVELAPPLLN VNVKENVIHV NATFPMAICV ESLPWMYDFN LWEAGSEDKK QYKSIFRKKA
     VTIDTTALRG NYCFNARSSI QSIDFKHSKF SQPVCMQLNY EGEWKFPFSA TIPVFVLLIL
     LTSASIIWLL KQDAKHKKMP QTLDLSNCKI AGPTFCCELR ENEFLTDCLI CTDKPMSQGK
     KNKTLAQNNQ MWMASFLPSS SSEEEEEEEE EDSSSFIPYT EMLQFPRKHF NFQTPRTADA
     ETILDSTSGV LSVVGGSTLD LSALGFSFFP IRKNEMDTSG SQGNEKASHS HSSSLGRISL
     TDVRFPGPRE HGQHGTDSND CLEVSLLHTL MNSSCTRLPA DEHCLYKKDH DFTICYQKPT
     LDQPVQVSEN PLLNEDPSME KFIYLQTLQV AEDEGFASDC DSGNFTEGTP PASTVLSDEL
     RISDMEKRYD KKFKFKGYQH SHYMRRS
 
 
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