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I17RB_MOUSE
ID   I17RB_MOUSE             Reviewed;         499 AA.
AC   Q9JIP3; Q9JIP2;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Interleukin-17 receptor B;
DE            Short=IL-17 receptor B;
DE            Short=IL-17RB;
DE   AltName: Full=IL-17 receptor homolog 1;
DE            Short=IL-17ER;
DE            Short=IL-17Rh1;
DE            Short=IL17Rh1;
DE   AltName: Full=Interleukin-17B receptor;
DE            Short=IL-17B receptor;
DE   Flags: Precursor;
GN   Name=Il17rb; Synonyms=Evi27, Il17br;
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] (ISOFORMS 1 AND 2).
RX   PubMed=10815801; DOI=10.1038/sj.onc.1203577;
RA   Tian E., Sawyer J.R., Largaespada D.A., Jenkins N.A., Copeland N.G.,
RA   Shaughnessy J.D. Jr.;
RT   "Evi27 encodes a novel membrane protein with homology to the IL17
RT   receptor.";
RL   Oncogene 19:2098-2109(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
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: Receptor for the pro-inflammatory cytokines IL17B and IL17E.
CC       May play a role in controlling the growth and/or differentiation of
CC       hematopoietic cells.
CC   -!- SUBUNIT: Interacts with DAZAP2. Interacts with TRAF3IP2.
CC       {ECO:0000250|UniProtKB:Q9NRM6}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JIP3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JIP3-2; Sequence=VSP_001742, VSP_001743;
CC   -!- TISSUE SPECIFICITY: Liver and testis. Expressed at lower level in
CC       kidney and lung. Expressed in selected T-cell, B-cell and myeloid cell
CC       lines.
CC   -!- MISCELLANEOUS: Evi27 is a common site of retroviral integration in Bxh2
CC       murine myeloid leukemias, localized near the Il17rb gene. Proviral
CC       integrations result in increased expression of Il17rb on the cell
CC       surface.
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DR   EMBL; AF208108; AAF86049.1; -; mRNA.
DR   EMBL; AF208109; AAF86050.1; -; mRNA.
DR   EMBL; BC026546; AAH26546.1; -; mRNA.
DR   CCDS; CCDS36845.1; -. [Q9JIP3-1]
DR   RefSeq; NP_062529.2; NM_019583.3. [Q9JIP3-1]
DR   PDB; 3VBC; X-ray; 1.80 A; A=325-486.
DR   PDBsum; 3VBC; -.
DR   AlphaFoldDB; Q9JIP3; -.
DR   SMR; Q9JIP3; -.
DR   BioGRID; 206146; 2.
DR   IntAct; Q9JIP3; 1.
DR   STRING; 10090.ENSMUSP00000016110; -.
DR   GlyGen; Q9JIP3; 4 sites.
DR   iPTMnet; Q9JIP3; -.
DR   PhosphoSitePlus; Q9JIP3; -.
DR   PaxDb; Q9JIP3; -.
DR   PRIDE; Q9JIP3; -.
DR   ProteomicsDB; 273070; -. [Q9JIP3-1]
DR   ProteomicsDB; 273071; -. [Q9JIP3-2]
DR   ABCD; Q9JIP3; 6 sequenced antibodies.
DR   Antibodypedia; 1155; 502 antibodies from 34 providers.
DR   DNASU; 50905; -.
DR   Ensembl; ENSMUST00000016110; ENSMUSP00000016110; ENSMUSG00000015966. [Q9JIP3-1]
DR   GeneID; 50905; -.
DR   KEGG; mmu:50905; -.
DR   UCSC; uc007sun.1; mouse. [Q9JIP3-1]
DR   CTD; 55540; -.
DR   MGI; MGI:1355292; Il17rb.
DR   VEuPathDB; HostDB:ENSMUSG00000015966; -.
DR   eggNOG; ENOG502RD98; Eukaryota.
DR   GeneTree; ENSGT00940000161145; -.
DR   HOGENOM; CLU_037593_0_0_1; -.
DR   InParanoid; Q9JIP3; -.
DR   OMA; HKYMVVY; -.
DR   BioGRID-ORCS; 50905; 4 hits in 73 CRISPR screens.
DR   PRO; PR:Q9JIP3; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9JIP3; protein.
DR   Bgee; ENSMUSG00000015966; Expressed in secondary oocyte and 95 other tissues.
DR   ExpressionAtlas; Q9JIP3; baseline and differential.
DR   Genevisible; Q9JIP3; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; ISS:MGI.
DR   GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:MGI.
DR   GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:MGI.
DR   Gene3D; 2.60.40.2150; -; 1.
DR   Gene3D; 2.60.40.2160; -; 1.
DR   InterPro; IPR039465; IL-17_rcpt-like.
DR   InterPro; IPR032356; IL17R_fnIII_D1.
DR   InterPro; IPR038683; IL17RA/B_FnIII-like_1_sf.
DR   InterPro; IPR043046; IL17RA/B_FnIII-like_2_sf.
DR   InterPro; IPR013568; SEFIR_dom.
DR   PANTHER; PTHR15583; PTHR15583; 1.
DR   Pfam; PF16556; IL17R_fnIII_D1; 1.
DR   Pfam; PF08357; SEFIR; 1.
DR   PROSITE; PS51534; SEFIR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..499
FT                   /note="Interleukin-17 receptor B"
FT                   /id="PRO_0000011033"
FT   TOPO_DOM        18..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..499
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          328..474
FT                   /note="SEFIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         163..218
FT                   /note="LNHVMKYKKQCTEAGSLWDPDITACKKNEKMVEVNFTTNPLGNRYTILIQRD
FT                   TTLG -> TRENTEVTSGVFPAAKHQALRISAPFPLQFPPGPEDSVILPPQPLASLFHD
FT                   FVKLT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10815801"
FT                   /id="VSP_001742"
FT   VAR_SEQ         219..499
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10815801"
FT                   /id="VSP_001743"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           342..354
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           367..373
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           375..385
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   STRAND          387..393
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           419..427
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           428..430
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   STRAND          440..444
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           455..459
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   STRAND          462..464
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   TURN            465..468
FT                   /evidence="ECO:0007829|PDB:3VBC"
FT   HELIX           469..478
FT                   /evidence="ECO:0007829|PDB:3VBC"
SQ   SEQUENCE   499 AA;  55617 MW;  C66440430E3C31F3 CRC64;
     MLLVLLILAA SCRSALPREP TIQCGSETGP SPEWMVQHTL TPGDLRDLQV ELVKTSVAAE
     EFSILMNISW ILRADASIRL LKATKICVSG KNNMNSYSCV RCNYTEAFQS QTRPSGGKWT
     FSYVGFPVEL STLYLISAHN IPNANMNEDS PSLSVNFTSP GCLNHVMKYK KQCTEAGSLW
     DPDITACKKN EKMVEVNFTT NPLGNRYTIL IQRDTTLGFS RVLENKLMRT SVAIPVTEES
     EGAVVQLTPY LHTCGNDCIR REGTVVLCSE TSAPIPPDDN RRMLGGWLPL FLVLLVAVWV
     LAAGIYLTWR QGRSTKTSFP ISTMLLPLIK VLVVYPSEIC FHHTVCRFTD FLQNYCRSEV
     ILEKWQKKKI AEMGPVQWLT TQKQAADKVV FLLPSDVPTL CDSACGHNEG SARENSQDLF
     PLAFNLFCSD FSSQTHLHKY LVVYLGGADL KGDYNALSVC PQYHLMKDAT AFHTELLKAT
     QSMSVKKRSQ ACHDSCSPL
 
 
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