ID A3KN55_BOVIN Unreviewed; 498 AA.
AC A3KN55; F1N245;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=IL17RB protein {ECO:0000313|EMBL:AAI33637.1};
DE SubName: Full=Interleukin 17 receptor B {ECO:0000313|Ensembl:ENSBTAP00000069042.1};
GN Name=IL17RB {ECO:0000313|EMBL:AAI33637.1,
GN ECO:0000313|Ensembl:ENSBTAP00000069042.1};
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 {ECO:0000313|EMBL:AAI33637.1};
RN [1] {ECO:0000313|EMBL:AAI33637.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI33637.1};
RC TISSUE=Fetal spinal column {ECO:0000313|EMBL:AAI33637.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000069042.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069042.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:7WG3}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 18-272, AND DISULFIDE BONDS.
RX PubMed=36288706; DOI=10.1016/j.celrep.2022.111555;
RA Lee W.H., Chen X., Liu I.J., Lee J.H., Hu C.M., Wu H.C., Wang S.K.,
RA Lee W.H., Ma C.;
RT "Structural basis of interleukin-17B receptor in complex with a
RT neutralizing antibody for guiding humanization and affinity maturation.";
RL Cell Rep. 41:111555-111555(2022).
RN [4] {ECO:0000313|Ensembl:ENSBTAP00000069042.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069042.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC133636; AAI33637.1; -; mRNA.
DR PDB; 7WG3; X-ray; 2.19 A; I/J/K/L=18-272.
DR STRING; 9913.ENSBTAP00000069042; -.
DR PaxDb; 9913-ENSBTAP00000014846; -.
DR Ensembl; ENSBTAT00000072099.1; ENSBTAP00000069042.1; ENSBTAG00000011178.6.
DR VEuPathDB; HostDB:ENSBTAG00000011178; -.
DR eggNOG; ENOG502RD98; Eukaryota.
DR GeneTree; ENSGT00940000161145; -.
DR HOGENOM; CLU_037593_0_0_1; -.
DR OMA; HKYMVVY; -.
DR TreeFam; TF329644; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000011178; Expressed in myometrium and 100 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030368; F:interleukin-17 receptor activity; IBA:GO_Central.
DR Gene3D; 3.40.50.11530; -; 1.
DR Gene3D; 2.60.40.2160; Interleukin-17 receptor A/B, fibronectin-III-like domain 1; 1.
DR Gene3D; 2.60.40.2150; Interleukin-17 receptor A/B, fibronectin-III-like domain 2; 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; INTERLEUKIN-17 RECEPTOR; 1.
DR PANTHER; PTHR15583:SF11; INTERLEUKIN-17 RECEPTOR B; 1.
DR Pfam; PF16556; IL17R_fnIII_D1; 1.
DR Pfam; PF16578; IL17R_fnIII_D2; 1.
DR Pfam; PF08357; SEFIR; 1.
DR PROSITE; PS51534; SEFIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7WG3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 287..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 328..473
FT /note="SEFIR"
FT /evidence="ECO:0000259|PROSITE:PS51534"
FT CARBOHYD 37
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 39
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 41
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 41
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 67
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 93
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 101
FT /note="N-acetyl-D-glucosamine 5"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 103
FT /note="N-acetyl-D-glucosamine 5"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 156
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 156
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 183
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 183
FT /note="N-acetyl-D-glucosamine 6"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 185
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 195
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 197
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:7WG3"
FT CARBOHYD 229
FT /note="N-acetyl-D-glucosamine 6"
FT /evidence="ECO:0007829|PDB:7WG3"
FT DISULFID 24..102
FT /evidence="ECO:0007829|PDB:7WG3"
FT DISULFID 87..99
FT /evidence="ECO:0007829|PDB:7WG3"
FT DISULFID 162..173
FT /evidence="ECO:0007829|PDB:7WG3"
FT DISULFID 187..268
FT /evidence="ECO:0007829|PDB:7WG3"
FT DISULFID 254..258
FT /evidence="ECO:0007829|PDB:7WG3"
SQ SEQUENCE 498 AA; 55469 MW; 53ED35628E0C1036 CRC64;
MSLVLLSLAA LCCGAVPPEP TIQCGSEPGP SPEWMVRHTL TPGDLRDLRV ETIKSNVDLE
DSPILMNISW ILRADASIRL LKATKICVMG KSHFQSYSCI RCNYTQAFQT QTRPSGGKWT
FSYVGFPVEL NTVYFIGAHN IPNANMNEDG PSMAVNFTSP GCLDHVMKYK KKCIEAGSLW
KPNITACKRS ANTVEVNFTT SPLGDRYMAL IQSTAVIGTS YVSEKELTRT SVVVHVTGES
EGAVVQLTPY FHTCGNDCIR QRGTVVQCPQ TGVSSPQDHD RSVLGGWLPL LLSALLVATW
VLVAGIYLIW RHERIKKTSF STTTLLPSIK VLVVYPSEIC FHHTVCYFTE FLQNRCRSEV
ILEKWQKKKI AEMGPVQWLT TQKEAADKVI FLLSNGNTTC DGNCDEKEGG PCESSRDLFH
LAFNLFCSDL RSQAHLHKYV VVYFREGDIA DSYRALSVCP TYRLTKDATG FCAELLRAKQ
HVSVGRRSRT CHYSCCSL
//
