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IL4_MERUN
ID   IL4_MERUN               Reviewed;         143 AA.
AC   P47966;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
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;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Mai Z., Klei T.R.;
RT   "Full length cDNA isolation of gerbil (Meriones unguiculatus) Th1 and Th2
RT   cell cytokines by PCR method as well as their characterization.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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; L37779; AAA65678.1; -; mRNA.
DR   AlphaFoldDB; P47966; -.
DR   SMR; P47966; -.
DR   Ensembl; ENSMUGT00000025290; ENSMUGP00000022035; ENSMUGG00000018505.
DR   OrthoDB; 1495672at2759; -.
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   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..143
FT                   /note="Interleukin-4"
FT                   /id="PRO_0000015536"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..88
FT                   /evidence="ECO:0000255"
FT   DISULFID        70..115
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   143 AA;  16106 MW;  492DDF1AAFF8452D CRC64;
     MGLSPQLAAV LLCLLVCTGN YARRQDREAG LREIIHNLDQ VLKKETPCTE MFVPDVLIAT
     KNTTEKGLLC RATRVLRKFY FPREVTPCLK NNSGVLSILR KLCRSISTLH PQESCSVSTP
     TLTTLNDFLG RLRGIMQMKN WQG
 
 
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