IL5_FELCA
ID IL5_FELCA Reviewed; 134 AA.
AC O77515; O62740;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Interleukin-5;
DE Short=IL-5;
DE AltName: Full=Eosinophil differentiation factor;
DE AltName: Full=T-cell replacing factor;
DE Short=TRF;
DE Flags: Precursor;
GN Name=IL5;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9781459;
RA Padrid P.A., Qin Y., Wells T.N.C., Solway J., Camoretti-Mercado B.;
RT "Sequence and structural analysis of feline interleukin-5 cDNA.";
RL Am. J. Vet. Res. 59:1263-1269(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-128.
RX PubMed=10391845; DOI=10.1128/cdli.6.4.471-478.1999;
RA Harley R., Helps C.R., Harbour D.A., Gruffydd-Jones T.J., Day M.J.;
RT "Cytokine mRNA expression in lesions in cats with chronic
RT gingivostomatitis.";
RL Clin. Diagn. Lab. Immunol. 6:471-478(1999).
CC -!- FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes
CC and NK cells that plays an important role in the survival,
CC differentiation, and chemotaxis of eosinophils. Acts also on activated
CC and resting B-cells to induce immunoglobulin production, growth, and
CC differentiation (By similarity). Mechanistically, exerts its biological
CC effects through a receptor composed of IL5RA subunit and the cytokine
CC receptor common subunit beta/CSF2RB. Binding to the receptor leads to
CC activation of various kinases including LYN, SYK and JAK2 and thereby
CC propagates signals through the RAS-MAPK and JAK-STAT5 pathways
CC respectively (By similarity). {ECO:0000250|UniProtKB:P04401,
CC ECO:0000250|UniProtKB:P05113}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with IL5RA. Interacts
CC with CSF2RB. {ECO:0000250|UniProtKB:P04401,
CC ECO:0000250|UniProtKB:P05113}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04401}.
CC -!- SIMILARITY: Belongs to the IL-5 family. {ECO:0000305}.
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DR EMBL; AF025436; AAC64505.1; -; mRNA.
DR EMBL; AF051372; AAC05752.1; -; mRNA.
DR RefSeq; NP_001009845.2; NM_001009845.2.
DR AlphaFoldDB; O77515; -.
DR SMR; O77515; -.
DR STRING; 9685.ENSFCAP00000012354; -.
DR Ensembl; ENSFCAT00000072428; ENSFCAP00000058090; ENSFCAG00000013321.
DR GeneID; 493803; -.
DR KEGG; fca:493803; -.
DR CTD; 3567; -.
DR VGNC; VGNC:102233; IL5.
DR eggNOG; ENOG502RWD8; Eukaryota.
DR GeneTree; ENSGT00390000016991; -.
DR HOGENOM; CLU_156269_0_0_1; -.
DR InParanoid; O77515; -.
DR OMA; RWRVKKF; -.
DR OrthoDB; 1469027at2759; -.
DR TreeFam; TF338422; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000013321; Expressed in testis.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005137; F:interleukin-5 receptor binding; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000186; IL-5.
DR Pfam; PF02025; IL5; 1.
DR PRINTS; PR00432; INTERLEUKIN5.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..134
FT /note="Interleukin-5"
FT /id="PRO_0000015558"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63
FT /note="Interchain (with C-105)"
FT /evidence="ECO:0000250|UniProtKB:P05113"
FT DISULFID 105
FT /note="Interchain (with C-63)"
FT /evidence="ECO:0000250|UniProtKB:P05113"
FT CONFLICT 104..105
FT /note="KC -> NF (in Ref. 2; AAC05752)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..111
FT /note="ERWR -> KKWK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="K -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="V -> F (in Ref. 2; AAC05752)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..126
FT /note="VI -> LL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15224 MW; 87D18DB8F8CAC820 CRC64;
MRMLLHLSLL ALGAAYVSAI AVQSPMNRLV AETLALLSTH RTLLIGDGNL MIPTPEHNNH
QLCIEEVFQG IDTLKNRTVP GDAVEKLFRN LSLIKEHIDR QKKKCGGERW RVKKFLDYLQ
VFLGVINTEW TMES
