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I22R1_MOUSE
ID   I22R1_MOUSE             Reviewed;         581 AA.
AC   Q80XZ4; B2RU51; Q3URP9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Interleukin-22 receptor subunit alpha-1;
DE            Short=IL-22 receptor subunit alpha-1;
DE            Short=IL-22R-alpha-1;
DE            Short=IL-22RA1;
DE   Flags: Precursor;
GN   Name=Il22ra1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=12618864; DOI=10.1038/sj.gene.6363934;
RA   Tachiiri A., Imamura R., Wang Y., Fukui M., Umemura M., Suda T.;
RT   "Genomic structure and inducible expression of the IL-22 receptor alpha
RT   chain in mice.";
RL   Genes Immun. 4:153-159(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the receptor for IL20, IL22 and IL24. Component
CC       of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling
CC       via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and
CC       Akt kinases pathways. Component of one of the receptor for IL20 and
CC       IL24 formed by IL22RA1 and IL20RB also signaling through STATs
CC       activation. Mediates IL24 antiangiogenic activity as well as IL24
CC       inhibitory effect on endothelial cell tube formation and
CC       differentiation. {ECO:0000269|PubMed:12618864}.
CC   -!- SUBUNIT: Heterodimer with IL10RB and with IL20RB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, liver and lung.
CC       {ECO:0000269|PubMed:12618864}.
CC   -!- INDUCTION: By LPS stimulation in the liver.
CC       {ECO:0000269|PubMed:12618864}.
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC       {ECO:0000305}.
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DR   EMBL; AY103454; AAM52222.1; -; mRNA.
DR   EMBL; AK141289; BAE24639.1; -; mRNA.
DR   EMBL; AL662911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC140972; AAI40973.1; -; mRNA.
DR   EMBL; BC140973; AAI40974.1; -; mRNA.
DR   CCDS; CCDS18789.1; -.
DR   RefSeq; NP_839988.1; NM_178257.2.
DR   PDB; 6WEO; X-ray; 2.60 A; 1/4/7/A/B/F/I/M/P/S/V/Y=24-224.
DR   PDBsum; 6WEO; -.
DR   AlphaFoldDB; Q80XZ4; -.
DR   SMR; Q80XZ4; -.
DR   STRING; 10090.ENSMUSP00000099605; -.
DR   GlyGen; Q80XZ4; 2 sites.
DR   iPTMnet; Q80XZ4; -.
DR   PhosphoSitePlus; Q80XZ4; -.
DR   jPOST; Q80XZ4; -.
DR   PaxDb; Q80XZ4; -.
DR   PRIDE; Q80XZ4; -.
DR   ProteomicsDB; 266938; -.
DR   Antibodypedia; 15695; 452 antibodies from 35 providers.
DR   DNASU; 230828; -.
DR   Ensembl; ENSMUST00000102546; ENSMUSP00000099605; ENSMUSG00000037157.
DR   GeneID; 230828; -.
DR   KEGG; mmu:230828; -.
DR   UCSC; uc008vgx.2; mouse.
DR   CTD; 58985; -.
DR   MGI; MGI:2663588; Il22ra1.
DR   VEuPathDB; HostDB:ENSMUSG00000037157; -.
DR   eggNOG; ENOG502S4IS; Eukaryota.
DR   GeneTree; ENSGT00940000161366; -.
DR   HOGENOM; CLU_033634_0_0_1; -.
DR   InParanoid; Q80XZ4; -.
DR   OMA; CQQITRK; -.
DR   OrthoDB; 1078220at2759; -.
DR   PhylomeDB; Q80XZ4; -.
DR   TreeFam; TF334107; -.
DR   Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR   BioGRID-ORCS; 230828; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q80XZ4; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q80XZ4; protein.
DR   Bgee; ENSMUSG00000037157; Expressed in jejunum and 25 other tissues.
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:0042015; F:interleukin-20 binding; IPI:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..581
FT                   /note="Interleukin-22 receptor subunit alpha-1"
FT                   /id="PRO_0000324321"
FT   TOPO_DOM        16..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..581
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          18..115
FT                   /note="Fibronectin type-III 1"
FT   DOMAIN          141..221
FT                   /note="Fibronectin type-III 2"
FT   REGION          343..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..217
FT                   /evidence="ECO:0000250"
FT   CONFLICT        335
FT                   /note="L -> M (in Ref. 2; BAE24639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="S -> Y (in Ref. 2; BAE24639)"
FT                   /evidence="ECO:0000305"
FT   STRAND          26..33
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          52..59
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          72..80
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          92..100
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          143..147
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   HELIX           156..159
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          164..172
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          175..190
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          196..205
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   TURN            206..209
FT                   /evidence="ECO:0007829|PDB:6WEO"
FT   STRAND          215..220
FT                   /evidence="ECO:0007829|PDB:6WEO"
SQ   SEQUENCE   581 AA;  63795 MW;  A2BF8692BB8AA93B CRC64;
     MKTLLTILTV GSLAAHTTVD TSGLLQHVKF QSSNFENILT WDGGPASTSD TVYSVEYKKY
     GERKWLAKAG CQRITQKFCN LTMETRNHTE FYYAKVTAVS AGGPPVTKMT DRFSSLQHTT
     IKPPDVTCIP KVRSIQMLVH PTLTPVLSED GHQLTLEEIF HDLFYRLELH VNHTYQMHLE
     GKQREYEFLG LTPDTEFLGS ITILTPILSK ESAPYVCRVK TLPDRTWAYS FSGAVLFSMG
     FLVGLLCYLG YKYITKPPVP PNSLNVQRVL TFQPLRFIQE HVLIPVLDLS GPSSLPQPIQ
     YSQVVVSGPR EPPGAVWRQS LSDLTYVGQS DVSILQPTNV PAQQTLSPPS YAPKAVPEVQ
     PPSYAPQVAS DAKALFYSPQ QGMKTRPATY DPQDILDSCP ASYAVCVEDS GKDSTPGILS
     TPKYLKTKGQ LQEDTLVRSC LPGDLSLQKV TSLGEGETQR PKSLPSPLGF CTDRGPDLHT
     LRSEEPETPR YLKGALSLLS SVQIEGHPVS LPLHVHSVSC SPSDEGPSPW GLLDSLVCPK
     DEGPAVETEA MCPSAAASEL EQSTELDSLF KGLALTVQWE S
 
 
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