ID   I22R1_BOVIN             Reviewed;         581 AA.
AC   Q3SYS8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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   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 [LARGE SCALE MRNA].
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with IL10RB and with IL20RB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC       {ECO:0000305}.
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DR   EMBL; BC103413; AAI03414.1; -; mRNA.
DR   RefSeq; NP_001029483.1; NM_001034311.2.
DR   AlphaFoldDB; Q3SYS8; -.
DR   SMR; Q3SYS8; -.
DR   STRING; 9913.ENSBTAP00000001455; -.
DR   PaxDb; Q3SYS8; -.
DR   PRIDE; Q3SYS8; -.
DR   GeneID; 508044; -.
DR   KEGG; bta:508044; -.
DR   CTD; 58985; -.
DR   eggNOG; ENOG502S4IS; Eukaryota.
DR   InParanoid; Q3SYS8; -.
DR   OrthoDB; 1078220at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   CDD; cd00063; FN3; 1.
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   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   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_0000324319"
FT   TOPO_DOM        16..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..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          354..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   581 AA;  63776 MW;  E5AD32AE1DFBC329 CRC64;
     MRTLLTILAA GSLLAHITED TSDLLQHVKF QSSNFENILT WDGRPESPPD TVYSVQYKTY
     GEEEWLEKEG CQRITQKSCN LTMETSNLTE LYYARVTATD GAGRSATKMT NRFSSLQHTS
     IKPPDVTCIP KVRSIQMIVH PTYTPIRAQN GHQLTLENIF QDLLYHLKLR INHTYQMHLE
     GKQREFEFVG LTPDTEFLGT IMICIPNLFK ESTPYMCRVK TLPDRTWTYS FSGAFLFSLG
     FLVAGLCYLS YRYITKPPPP PSSLNVQHIL PFRPLQFIQE HTLIPVFDLS GSGGLAQPVQ
     YSEVKVSNPT EPPGPPPRHS LPEIAYLGQP DLPVLRPSGG PPHQALPVLS YAPQAAPEGR
     PSSYAPQGAL EAKPPSYTPQ AVSETQLPSY TPRATPDNWP PSYGMCGEGS GRDSPPVTRS
     GPKHLGTKGQ LQKEVPAGSC SPTGLSLQEV TPLAMEDPQE AKSSHQCLRV HTDSDSDSDT
     IGQREPGTRS SLKGQLPLLS SVQIEGHPGC LPLQTPSLPC SPTDKGPSPW GLLESLVCPS
     DEDPVSKTEA ESPGLQAPDL ESPTELDSLF RGLALTVQWE S