IL31RA
entrez
133396
canonical
uniprot
Q8NI17
canonical
ensembl
ENSG00000164509
resolver
ensp
ENSP00000297015
resolver
ensp
ENSP00000347047
resolver
ensp
ENSP00000351935
resolver
ensp
ENSP00000380048
resolver
ensp
ENSP00000427533
resolver
ensp
ENSP00000498630
resolver
genesymbol
IL31RA
resolver
genesymbol_syn
CRL3
resolver
genesymbol_syn
GPL
resolver
hgnc
HGNC:18969
resolver
uniprot
A6NIF8
resolver
uniprot
B4DNJ2
resolver
uniprot
Q2TBA1
resolver
uniprot
Q6EBC3
resolver
uniprot
Q6EBC4
resolver
uniprot
Q6EBC5
resolver
uniprot
Q6EBC6
resolver
uniprot
Q6UWL8
resolver
uniprot
Q8WYJ0
resolver
uniprot_entry
B4DNJ2_HUMAN
resolver
uniprot_entry
IL31R_HUMAN
resolver
uniprot_sec
A6NIF8
resolver
uniprot_sec
Q2TBA1
resolver
uniprot_sec
Q6EBC3
resolver
uniprot_sec
Q6EBC4
resolver
uniprot_sec
Q6EBC5
resolver
uniprot_sec
Q6EBC6
resolver
uniprot_sec
Q6UWL8
resolver
uniprot_sec
Q8WYJ0
resolver
amino_acid_sequence
MMWTWALWMLPSLCKFSLAALPAKPENISCVYYYRKNLTCTWSPGKETSYTQYTVKRTYAFGEKHDNCTTNSSTSENRASCSFFLPRITIPDNYTIEVEAENGDGVIKSHMTYWRLENIAKTEPPKIFRVKPVLGIKRMIQIEWIKPELAPVSSDLKYTLRFRTVNSTSWMEVNFAKNRKDKNQTYNLTGLQPFTEYVIALRCAVKESKFWSDWSQEKMGMTEEEAPCGLELWRVLKPAEADGRRPVRLLWKKARGAPVLEKTLGYNIWYYPESNTNLTETMNTTNQQLELHLGGESFWVSMISYNSLGKSPVATLRIPAIQEKSFQCIEVMQACVAEDQLVVKWQSSALDVNTWMIEWFPDVDSEPTTLSWESVSQATNWTIQQDKLKPFWCYNISVYPMLHDKVGEPYSIQAYAKEGVPSEGPETKVENIGVKTVTITWKEIPKSERKGIICNYTIFYQAEGGKGFSKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSINFKTLSFSVFEIILITSLIGGGLLILIILTVAYGLKKPNKLTHLCWPTVPNPAESSIATWHGDDFKDKLNLKESDDSVNTEDRILKPCSTPSDKLVIDKLVVNFGNVLQEIFTDEARTGQENNLGGEKNGYVTCPFRPDCPLGKSFEELPVSPEIPPRKSQYLRSRMPEGTRPEAKEQLLFSGQSLVPDHLCEEGAPNPYLKNSVTAREFLVSEKLPEHTKGEV
uniprot
proteins
disease_involvement
DISEASE: Amyloidosis, primary localized cutaneous, 2 (PLCA2) [MIM:613955]: A primary amyloidosis characterized by localized cutaneous amyloid deposition. This condition usually presents with itching (especially on the lower legs) and visible changes of skin hyperpigmentation and thickening that may be exacerbated by chronic scratching and rubbing. Primary localized cutaneous amyloidosis is often divided into macular and lichen subtypes although many affected individuals often show both variants coexisting. Lichen amyloidosis characteristically presents as a pruritic eruption of grouped hyperkeratotic papules with a predilection for the shins, calves, ankles and dorsa of feet and thighs. Papules may coalesce to form hyperkeratotic plaques that can resemble lichen planus, lichen simplex or nodular prurigo. Macular amyloidosis is characterized by small pigmented macules that may merge to produce macular hyperpigmentation, sometimes with a reticulate or rippled pattern. In macular and lichen amyloidosis, amyloid is deposited in the papillary dermis in association with grouped colloid bodies, thought to represent degenerate basal keratinocytes. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins. {ECO:0000269|PubMed:19690585}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Functions as a membrane-bound signal-transducing subunit of the IL31 receptor complex (heterodimer composed of OSMR and IL31RA) which binds IL31 (PubMed:15184896, PubMed:15194700, PubMed:15627637). Functionally, IL31 signaling via OSMR/IL31RA is particularly important in skin immunity (PubMed:15184896). Mechanistically, ligand binding induces heterodimerization with OSMR, activating JAK1 and JAK2 (and to a lesser extent TYK2) associated with the intracellular domains of IL31RA and OSMR (PubMed:15194700, PubMed:15627637). These kinases phosphorylate tyrosine residues on IL31RA and OSMR, creating docking sites for STAT1, STAT3, and STAT5B, which are then phosphorylated and activated (Probable) (PubMed:11877449, PubMed:15194700, PubMed:15627637). In addition, the IL31 receptor complex activates the MAPK pathway (MAPK3/ERK1-MAPK1/ERK2) via recruitment of the adapter protein SHC1 (PubMed:15194700, PubMed:15627637). Mediates IL31-induced itch, probably in a manner dependent on cation channels TRPA1 and TRPV1 (By similarity). Positively regulates numbers and cycling status of immature subsets of myeloid progenitor cells in bone marrow in vivo and enhances myeloid progenitor cell survival in vitro (By similarity). {ECO:0000250|UniProtKB:Q8K5B1, ECO:0000269|PubMed:11877449, ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637, ECO:0000305|PubMed:14504285}.
uniprot
proteins
mass_dalton
82954
uniprot
proteins
mutagenesis
MUTAGEN 639; /note="Y->A: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-670 and A-708."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637"; MUTAGEN 639; /note="Y->F: Abrogates STAT5 activation. Mild effect on STAT1 activation. No effect on STAT3 activation."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637"; MUTAGEN 670; /note="Y->A: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-708."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637"; MUTAGEN 670; /note="Y->F: No effect on STAT3 and STAT5 activation. Mild effect on STAT1 activation."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637"; MUTAGEN 708; /note="Y->A: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-670."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637"; MUTAGEN 708; /note="Y->F: Abrogates STAT3 activation. Loss of interaction with STAT3. Mild effect on STAT1 activation. No effect on STAT5 activation."; /evidence="ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:14504285}.
uniprot
proteins
protein_family
Type 2 subfamily
uniprot
proteins
protein_family
Type I cytokine receptor family
uniprot
proteins
pubmed
11877449
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14504285
uniprot
proteins
pubmed
15184896
uniprot
proteins
pubmed
15194700
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15627637
uniprot
proteins
pubmed
16461143
uniprot
proteins
pubmed
18439099
uniprot
proteins
pubmed
19690585
uniprot
proteins
pubmed
21261663
uniprot
proteins
pubmed
24373353
uniprot
proteins
sequence_length
732
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}; Single-pass type I membrane protein {ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8K5B1}. Cell projection, axon {ECO:0000250|UniProtKB:Q8K5B1}.
uniprot
proteins
transmembrane_region
TRANSMEM 520..540; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins