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IL4_SHEEP
ID   IL4_SHEEP               Reviewed;         135 AA.
AC   P30368; Q95MZ6;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Interleukin-4;
DE            Short=IL-4;
DE   AltName: Full=B-cell stimulatory factor 1;
DE            Short=BSF-1;
DE   AltName: Full=Lymphocyte stimulatory factor 1;
DE   Flags: Precursor;
GN   Name=IL4; Synonyms=IL-4;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8444353; DOI=10.1016/0378-1119(93)90408-u;
RA   Seow H.F., Rothel J.S., Wood P.R.;
RT   "Cloning and sequencing an ovine interleukin-4-encoding cDNA.";
RL   Gene 124:291-293(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10805377; DOI=10.1089/107999000312360;
RA   Chaplin P.J., Casey G., De Rose R., Buchan G., Wood P.R., Scheerlinck J.P.;
RT   "The expression and biologic effects of ovine interleukin-4 on T and B cell
RT   proliferation.";
RL   J. Interferon Cytokine Res. 20:419-425(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-119.
RX   PubMed=1457812; DOI=10.3109/10425179209034004;
RA   Engwerda C.R., Sandeman M.;
RT   "The isolation and sequence of sheep interleukin 4.";
RL   DNA Seq. 3:111-113(1992).
CC   -!- FUNCTION: Participates in at least several B-cell activation processes
CC       as well as of other cell types. It is a costimulator of DNA-synthesis.
CC       It induces the expression of class II MHC molecules on resting B-cells.
CC       It enhances both secretion and cell surface expression of IgE and IgG1.
CC       It also regulates the expression of the low affinity Fc receptor for
CC       IgE (CD23) on both lymphocytes and monocytes. Positively regulates
CC       IL31RA expression in macrophages. Stimulates autophagy in dendritic
CC       cells by interfering with mTORC1 signaling and through the induction of
CC       RUFY4. {ECO:0000250|UniProtKB:P07750}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
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DR   EMBL; M96845; AAA31552.1; -; mRNA.
DR   EMBL; AF172168; AAD49370.1; -; mRNA.
DR   EMBL; Z11897; CAA77950.1; -; mRNA.
DR   PIR; JU0139; JU0139.
DR   RefSeq; NP_001009313.2; NM_001009313.2.
DR   AlphaFoldDB; P30368; -.
DR   SMR; P30368; -.
DR   STRING; 9940.ENSOARP00000015980; -.
DR   GeneID; 101122781; -.
DR   KEGG; oas:101122781; -.
DR   CTD; 3565; -.
DR   eggNOG; KOG3886; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
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:0005136; F:interleukin-4 receptor binding; IEA:InterPro.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISS:UniProtKB.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR002354; IL-4.
DR   InterPro; IPR001325; IL-4/IL-13.
DR   InterPro; IPR018096; IL-4/IL-13_CS.
DR   PANTHER; PTHR47401; PTHR47401; 1.
DR   Pfam; PF00727; IL4; 1.
DR   PIRSF; PIRSF001941; Interleukin_4; 1.
DR   PRINTS; PR00431; INTERLEUKIN4.
DR   SMART; SM00190; IL4_13; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00838; INTERLEUKIN_4_13; 1.
PE   2: Evidence at transcript level;
KW   B-cell activation; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..135
FT                   /note="Interleukin-4"
FT                   /id="PRO_0000015543"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..105
FT                   /evidence="ECO:0000250"
FT   CONFLICT        38
FT                   /note="L -> P (in Ref. 1; AAA31552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="R -> Q (in Ref. 1; AAA31552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="V -> A (in Ref. 1; AAA31552)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="A -> T (in Ref. 1; AAA31552)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   135 AA;  15136 MW;  DFA6086C522C55A4 CRC64;
     MGLTSQLIPA LVCLLVCTSH FVHGHKCDIT LEEIIKTLNI LTSRKNSCME LPVADVFAAP
     KNATEKETFC RAGIELRRIY RSHMCLNKFL GGLDRNLSSL ASKTCSVNEA KTSTSTLRDL
     LERLKTIMRE KYSKC
 
 
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