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Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)

 IL3RB_HUMAN             Reviewed;         897 AA.
P32927; Q5JZI1; Q6ICE0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
17-JUN-2020, entry version 204.
RecName: Full=Cytokine receptor common subunit beta;
AltName: Full=CDw131;
AltName: Full=GM-CSF/IL-3/IL-5 receptor common beta subunit;
AltName: CD_antigen=CD131;
Flags: Precursor;
Name=CSF2RB; Synonyms=IL3RB, IL5RB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1702217; DOI=10.1073/pnas.87.24.9655;
Hayashida K., Kitamura T., Gorman D.M., Arai K., Yokota T., Miyajima A.;
"Molecular cloning of a second subunit of the receptor for human
granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution
of a high-affinity GM-CSF receptor.";
Proc. Natl. Acad. Sci. U.S.A. 87:9655-9659(1990).
[2]
SEQUENCE REVISION TO 454.
Kitamura T.;
Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH TMEM102.
PubMed=17828305; DOI=10.1038/sj.onc.1210778;
Kao C.J., Chiang Y.J., Chen P.H., Lin K.R., Hwang P.I., Yang-Yen H.F.,
Yen J.J.;
"CBAP interacts with the un-liganded common beta-subunit of the GM-CSF/IL-
3/IL-5 receptor and induces apoptosis via mitochondrial dysfunction.";
Oncogene 27:1397-1403(2008).
[7]
INVOLVEMENT IN SMDP5.
PubMed=21075760; DOI=10.1136/jmg.2010.082586;
Tanaka T., Motoi N., Tsuchihashi Y., Tazawa R., Kaneko C., Nei T.,
Yamamoto T., Hayashi T., Tagawa T., Nagayasu T., Kuribayashi F.,
Ariyoshi K., Nakata K., Morimoto K.;
"Adult-onset hereditary pulmonary alveolar proteinosis caused by a single-
base deletion in CSF2RB.";
J. Med. Genet. 48:205-209(2011).
[8]
STRUCTURE BY NMR OF 338-438.
PubMed=10736232; DOI=10.1006/jmbi.2000.3610;
Mulhern T.D., Lopez A.F., D'Andrea R.J., Gaunt C., Vandeleur L.,
Vadas M.A., Booker G.W., Bagley C.J.;
"The solution structure of the cytokine-binding domain of the common beta-
chain of the receptors for granulocyte-macrophage colony-stimulating
factor, interleukin-3 and interleukin-5.";
J. Mol. Biol. 297:989-1001(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 338-438.
PubMed=10753826;
Rossjohn J., McKinstry W.J., Woodcock J.M., McClure B.J., Hercus T.R.,
Parker M.W., Lopez A.F., Bagley C.J.;
"Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common
beta-chain bound to an antagonist.";
Blood 95:2491-2498(2000).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-437.
PubMed=11207369; DOI=10.1016/s0092-8674(01)00213-6;
Carr P.D., Gustin S.E., Church A.P., Murphy J.M., Ford S.C., Mann D.A.,
Woltring D.M., Walker I., Ollis D.L., Young I.G.;
"Structure of the complete extracellular domain of the common beta subunit
of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer
configuration.";
Cell 104:291-300(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS, SUBUNIT,
AND GLYCOSYLATION AT ASN-58 AND ASN-191.
PubMed=16754968; DOI=10.1107/s1744309106016812;
Carr P.D., Conlan F., Ford S., Ollis D.L., Young I.G.;
"An improved resolution structure of the human beta common receptor
involved in IL-3, IL-5 and GM-CSF signalling which gives better definition
of the high-affinity binding epitope.";
Acta Crystallogr. F 62:509-513(2006).
[12]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-438 IN COMPLEX WITH CSF2RA AND
CSF2, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191, AND DISULFIDE BONDS.
PubMed=18692472; DOI=10.1016/j.cell.2008.05.053;
Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M., Powell J.,
Ramshaw H., Woodcock J.M., Xu Y., Guthridge M., McKinstry W.J., Lopez A.F.,
Parker M.W.;
"The structure of the GM-CSF receptor complex reveals a distinct mode of
cytokine receptor activation.";
Cell 134:496-507(2008).
[13]
VARIANT THR-603.
PubMed=9410898; DOI=10.1172/jci119758;
Dirksen U., Nishinakamura R., Groneck P., Hattenhorst U., Nogee L.,
Murray R., Burdach S.;
"Human pulmonary alveolar proteinosis associated with a defect in GM-
CSF/IL-3/IL-5 receptor common beta chain expression.";
J. Clin. Invest. 100:2211-2217(1997).
-!- FUNCTION: High affinity receptor for interleukin-3, interleukin-5 and
granulocyte-macrophage colony-stimulating factor.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
is common to the IL3, IL5 and GM-CSF receptors. The signaling GM-CSF
receptor complex is a dodecamer of two head-to-head hexamers of two
alpha, two beta, and two ligand subunits. Interacts with TMEM102; this
interaction occurs preferentially in the absence of CSF2. Interacts
with FCER1G; this interaction is direct. Interacts with LYN.
{ECO:0000250|UniProtKB:P26955}.
-!- INTERACTION:
P32927; P04141: CSF2; NbExp=2; IntAct=EBI-1809771, EBI-1809826;
P32927; P05113: IL5; NbExp=2; IntAct=EBI-1809771, EBI-2435811;
P32927; Q01344: IL5RA; NbExp=3; IntAct=EBI-1809771, EBI-1759442;
P32927; P05556: ITGB1; NbExp=5; IntAct=EBI-1809771, EBI-703066;
P32927; O60674: JAK2; NbExp=4; IntAct=EBI-1809771, EBI-518647;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P32927-1; Sequence=Displayed;
Name=2;
IsoId=P32927-2; Sequence=VSP_032798;
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-surface
receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: May be phosphorylated by LYN. {ECO:0000250}.
-!- DISEASE: Pulmonary surfactant metabolism dysfunction 5 (SMDP5)
[MIM:614370]: A rare lung disorder due to impaired surfactant
homeostasis. It is characterized by alveolar filling with floccular
material that stains positive using the periodic acid-Schiff method and
is derived from surfactant phospholipids and protein components.
Excessive lipoproteins accumulation in the alveoli results in severe
respiratory distress. {ECO:0000269|PubMed:21075760}. Note=The disease
is caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
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EMBL; M59941; AAA18171.1; -; mRNA.
EMBL; CR456428; CAG30314.1; -; mRNA.
EMBL; AL008637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60125.1; -; Genomic_DNA.
EMBL; CH471095; EAW60126.1; -; Genomic_DNA.
CCDS; CCDS13936.1; -. [P32927-1]
PIR; A39255; A39255.
RefSeq; NP_000386.1; NM_000395.2. [P32927-1]
RefSeq; XP_005261397.1; XM_005261340.3. [P32927-2]
PDB; 1C8P; NMR; -; A=338-438.
PDB; 1EGJ; X-ray; 2.80 A; A=338-438.
PDB; 1GH7; X-ray; 3.00 A; A/B=25-437.
PDB; 2GYS; X-ray; 2.70 A; A/B=25-437.
PDB; 2NA8; NMR; -; A=432-473.
PDB; 2NA9; NMR; -; A=432-473.
PDB; 4NKQ; X-ray; 3.30 A; A=25-438.
PDB; 5DWU; X-ray; 3.97 A; A=17-240, B=241-443.
PDBsum; 1C8P; -.
PDBsum; 1EGJ; -.
PDBsum; 1GH7; -.
PDBsum; 2GYS; -.
PDBsum; 2NA8; -.
PDBsum; 2NA9; -.
PDBsum; 4NKQ; -.
PDBsum; 5DWU; -.
SMR; P32927; -.
BioGRID; 107826; 17.
CORUM; P32927; -.
DIP; DIP-127N; -.
ELM; P32927; -.
IntAct; P32927; 16.
MINT; P32927; -.
STRING; 9606.ENSP00000384053; -.
ChEMBL; CHEMBL2364169; -.
DrugBank; DB05264; NPI 32101.
DrugBank; DB05943; Resatorvid.
DrugBank; DB00020; Sargramostim.
DrugCentral; P32927; -.
iPTMnet; P32927; -.
PhosphoSitePlus; P32927; -.
BioMuta; CSF2RB; -.
DMDM; 1345923; -.
MassIVE; P32927; -.
PaxDb; P32927; -.
PeptideAtlas; P32927; -.
PRIDE; P32927; -.
ProteomicsDB; 54888; -. [P32927-1]
ProteomicsDB; 54889; -. [P32927-2]
ABCD; P32927; 2 sequenced antibodies.
Antibodypedia; 4136; 706 antibodies.
DNASU; 1439; -.
Ensembl; ENST00000403662; ENSP00000384053; ENSG00000100368. [P32927-1]
Ensembl; ENST00000406230; ENSP00000385271; ENSG00000100368. [P32927-2]
GeneID; 1439; -.
KEGG; hsa:1439; -.
UCSC; uc003aqa.5; human. [P32927-1]
CTD; 1439; -.
DisGeNET; 1439; -.
EuPathDB; HostDB:ENSG00000100368.13; -.
GeneCards; CSF2RB; -.
HGNC; HGNC:2436; CSF2RB.
HPA; ENSG00000100368; Tissue enhanced (blood, placenta).
MalaCards; CSF2RB; -.
MIM; 138981; gene.
MIM; 614370; phenotype.
neXtProt; NX_P32927; -.
OpenTargets; ENSG00000100368; -.
Orphanet; 264675; Hereditary pulmonary alveolar proteinosis.
PharmGKB; PA26939; -.
eggNOG; ENOG410IGEX; Eukaryota.
eggNOG; ENOG4112BQP; LUCA.
GeneTree; ENSGT00510000048963; -.
HOGENOM; CLU_015884_0_0_1; -.
InParanoid; P32927; -.
KO; K04738; -.
OMA; WVLPMWV; -.
PhylomeDB; P32927; -.
TreeFam; TF337996; -.
Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-5688849; Defective CSF2RB causes pulmonary surfactant metabolism dysfunction 5 (SMDP5).
Reactome; R-HSA-5688890; Defective CSF2RA causes pulmonary surfactant metabolism dysfunction 4 (SMDP4).
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P32927; -.
SIGNOR; P32927; -.
BioGRID-ORCS; 1439; 5 hits in 786 CRISPR screens.
ChiTaRS; CSF2RB; human.
EvolutionaryTrace; P32927; -.
GenomeRNAi; 1439; -.
Pharos; P32927; Tclin.
PRO; PR:P32927; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; P32927; protein.
Bgee; ENSG00000100368; Expressed in blood and 169 other tissues.
ExpressionAtlas; P32927; baseline and differential.
Genevisible; P32927; HS.
GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; TAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0036016; P:cellular response to interleukin-3; IEA:GOC.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0038156; P:interleukin-3-mediated signaling pathway; IEA:GOC.
GO; GO:0038043; P:interleukin-5-mediated signaling pathway; IEA:GOC.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011365; IL3_rcpt_beta.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF09240; IL6Ra-bind; 1.
Pfam; PF09294; Interfer-bind; 1.
PIRSF; PIRSF001956; IL3R_beta_c; 1.
SMART; SM00060; FN3; 2.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1..16
/evidence="ECO:0000255"
CHAIN 17..897
/note="Cytokine receptor common subunit beta"
/id="PRO_0000010862"
TOPO_DOM 17..443
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 444..460
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 461..897
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 133..240
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 339..436
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
MOTIF 425..429
/note="WSXWS motif"
MOTIF 474..482
/note="Box 1 motif"
MOD_RES 766
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P26955"
CARBOHYD 58
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16754968,
ECO:0000269|PubMed:18692472"
CARBOHYD 191
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16754968,
ECO:0000269|PubMed:18692472"
CARBOHYD 346
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 35..45
DISULFID 75..96
DISULFID 86..91
DISULFID 250..260
DISULFID 289..306
VAR_SEQ 285
/note="G -> GSAVLLR (in isoform 2)"
/evidence="ECO:0000303|PubMed:15461802"
/id="VSP_032798"
VARIANT 249
/note="E -> Q (in dbSNP:rs16845)"
/id="VAR_042521"
VARIANT 603
/note="P -> T (in dbSNP:rs1801122)"
/evidence="ECO:0000269|PubMed:9410898"
/id="VAR_014801"
VARIANT 647
/note="G -> V (in dbSNP:rs1801115)"
/id="VAR_014802"
VARIANT 652
/note="V -> M (in dbSNP:rs1801114)"
/id="VAR_014803"
VARIANT 696
/note="P -> S (in dbSNP:rs16997517)"
/id="VAR_042522"
HELIX 28..32
/evidence="ECO:0000244|PDB:2GYS"
STRAND 34..37
/evidence="ECO:0000244|PDB:2GYS"
STRAND 39..50
/evidence="ECO:0000244|PDB:2GYS"
HELIX 51..54
/evidence="ECO:0000244|PDB:2GYS"
STRAND 59..66
/evidence="ECO:0000244|PDB:2GYS"
STRAND 69..72
/evidence="ECO:0000244|PDB:2GYS"
STRAND 75..77
/evidence="ECO:0000244|PDB:2GYS"
STRAND 88..99
/evidence="ECO:0000244|PDB:2GYS"
STRAND 108..117
/evidence="ECO:0000244|PDB:2GYS"
STRAND 121..126
/evidence="ECO:0000244|PDB:2GYS"
HELIX 127..129
/evidence="ECO:0000244|PDB:2GYS"
STRAND 137..144
/evidence="ECO:0000244|PDB:2GYS"
STRAND 147..153
/evidence="ECO:0000244|PDB:2GYS"
STRAND 162..164
/evidence="ECO:0000244|PDB:4NKQ"
HELIX 166..168
/evidence="ECO:0000244|PDB:2GYS"
STRAND 169..177
/evidence="ECO:0000244|PDB:2GYS"
HELIX 182..184
/evidence="ECO:0000244|PDB:1GH7"
STRAND 186..197
/evidence="ECO:0000244|PDB:2GYS"
TURN 199..201
/evidence="ECO:0000244|PDB:2GYS"
STRAND 207..216
/evidence="ECO:0000244|PDB:2GYS"
STRAND 218..221
/evidence="ECO:0000244|PDB:1GH7"
STRAND 233..236
/evidence="ECO:0000244|PDB:2GYS"
STRAND 246..252
/evidence="ECO:0000244|PDB:2GYS"
STRAND 254..265
/evidence="ECO:0000244|PDB:2GYS"
HELIX 266..269
/evidence="ECO:0000244|PDB:2GYS"
STRAND 274..279
/evidence="ECO:0000244|PDB:2GYS"
STRAND 292..295
/evidence="ECO:0000244|PDB:2GYS"
TURN 298..300
/evidence="ECO:0000244|PDB:2GYS"
STRAND 301..309
/evidence="ECO:0000244|PDB:2GYS"
TURN 313..315
/evidence="ECO:0000244|PDB:2GYS"
STRAND 318..325
/evidence="ECO:0000244|PDB:2GYS"
STRAND 330..333
/evidence="ECO:0000244|PDB:2GYS"
HELIX 334..336
/evidence="ECO:0000244|PDB:2GYS"
STRAND 337..339
/evidence="ECO:0000244|PDB:1GH7"
STRAND 344..348
/evidence="ECO:0000244|PDB:2GYS"
STRAND 350..352
/evidence="ECO:0000244|PDB:1GH7"
STRAND 355..359
/evidence="ECO:0000244|PDB:2GYS"
STRAND 365..367
/evidence="ECO:0000244|PDB:1C8P"
STRAND 370..377
/evidence="ECO:0000244|PDB:2GYS"
STRAND 379..381
/evidence="ECO:0000244|PDB:2GYS"
HELIX 383..385
/evidence="ECO:0000244|PDB:1GH7"
STRAND 388..393
/evidence="ECO:0000244|PDB:2GYS"
STRAND 395..398
/evidence="ECO:0000244|PDB:2GYS"
STRAND 405..407
/evidence="ECO:0000244|PDB:1GH7"
STRAND 409..416
/evidence="ECO:0000244|PDB:2GYS"
STRAND 418..420
/evidence="ECO:0000244|PDB:1GH7"
STRAND 432..436
/evidence="ECO:0000244|PDB:1EGJ"
HELIX 442..466
/evidence="ECO:0000244|PDB:2NA8"
SEQUENCE 897 AA; 97336 MW; 3398E37FDB8F393A CRC64;
MVLAQGLLSM ALLALCWERS LAGAEETIPL QTLRCYNDYT SHITCRWADT QDAQRLVNVT
LIRRVNEDLL EPVSCDLSDD MPWSACPHPR CVPRRCVIPC QSFVVTDVDY FSFQPDRPLG
TRLTVTLTQH VQPPEPRDLQ ISTDQDHFLL TWSVALGSPQ SHWLSPGDLE FEVVYKRLQD
SWEDAAILLS NTSQATLGPE HLMPSSTYVA RVRTRLAPGS RLSGRPSKWS PEVCWDSQPG
DEAQPQNLEC FFDGAAVLSC SWEVRKEVAS SVSFGLFYKP SPDAGEEECS PVLREGLGSL
HTRHHCQIPV PDPATHGQYI VSVQPRRAEK HIKSSVNIQM APPSLNVTKD GDSYSLRWET
MKMRYEHIDH TFEIQYRKDT ATWKDSKTET LQNAHSMALP ALEPSTRYWA RVRVRTSRTG
YNGIWSEWSE ARSWDTESVL PMWVLALIVI FLTIAVLLAL RFCGIYGYRL RRKWEEKIPN
PSKSHLFQNG SAELWPPGSM SAFTSGSPPH QGPWGSRFPE LEGVFPVGFG DSEVSPLTIE
DPKHVCDPPS GPDTTPAASD LPTEQPPSPQ PGPPAASHTP EKQASSFDFN GPYLGPPHSR
SLPDILGQPE PPQEGGSQKS PPPGSLEYLC LPAGGQVQLV PLAQAMGPGQ AVEVERRPSQ
GAAGSPSLES GGGPAPPALG PRVGGQDQKD SPVAIPMSSG DTEDPGVASG YVSSADLVFT
PNSGASSVSL VPSLGLPSDQ TPSLCPGLAS GPPGAPGPVK SGFEGYVELP PIEGRSPRSP
RNNPVPPEAK SPVLNPGERP ADVSPTSPQP EGLLVLQQVG DYCFLPGLGP GPLSLRSKPS
SPGPGPEIKN LDQAFQVKKP PGQAVPQVPV IQLFKALKQQ DYLSLPPWEV NKPGEVC


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Pathways :
WP2292: Chemokine signaling pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP1655: Geraniol degradation
WP809: TGF-beta Receptor Signaling Pathway
WP1566: Citrate cycle (TCA cycle)
WP1367: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP1045: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP1614: 1- and 2-Methylnaphthalene degradation
WP566: canonical wnt - zebrafish
WP2328: Allograft rejection
WP143: Fatty Acid Beta Oxidation
WP1941: Peroxisomal beta-oxidation of tetracosanoyl-CoA
WP305: Glucocorticoid Metabolism
WP581: EPO Receptor Signaling
WP949: Toll-like receptor signaling pathway
WP1004: Kit Receptor Signaling Pathway
WP126: Fatty Acid Beta Oxidation 1
WP1680: Oxidative phosphorylation
WP23: B Cell Receptor Signaling Pathway
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[CSF2RB IL3RB IL5RB] Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)
[Csf2rb Aic2b Csf2rb1 Il3rb1] Cytokine receptor common subunit beta (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[Il2rg] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[IL5RA IL5R] Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CDw125) (CD antigen CD125)
[IL3RA IL3R] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (CD antigen CD123)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[IL13RA1 IL13R IL13RA] Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[IL6ST] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[IL31RA CRL3 GPL UNQ6368/PRO21073/PRO21384] Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (Cytokine receptor-like 3) (GLM-R) (hGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (ZcytoR17)
[Il6st] Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[IFNLR1 IL28RA LICR2] Interferon lambda receptor 1 (IFN-lambda receptor 1) (IFN-lambda-R1) (Cytokine receptor class-II member 12) (Cytokine receptor family 2 member 12) (CRF2-12) (Interleukin-28 receptor subunit alpha) (IL-28 receptor subunit alpha) (IL-28R-alpha) (IL-28RA) (Likely interleukin or cytokine receptor 2) (LICR2)
[CSF2RA CSF2R CSF2RY] Granulocyte-macrophage colony-stimulating factor receptor subunit alpha (GM-CSF-R-alpha) (GMCSFR-alpha) (GMR-alpha) (CDw116) (CD antigen CD116)
[IL7R] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CDw127) (CD antigen CD127)
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[Csf2rb2 Ai2ca Il3r Il3rb2] Interleukin-3 receptor class 2 subunit beta (IL-3 receptor class 2 subunit beta) (IL-3R class 2 subunit beta) (Colony-stimulating factor 2 receptor subunit beta-2) (Interleukin-3 receptor class II beta chain)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL2RG] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[OSMR OSMRB] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Il5ra Il5r] Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CD antigen CD125)
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[Ptprc Ly-5] Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (Lymphocyte antigen 5) (Ly-5) (T200) (CD antigen CD45)
[Osmr Osmrb] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)

Bibliography :