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IL4_CAPHI
ID   IL4_CAPHI               Reviewed;         135 AA.
AC   P79155;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 90.
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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Beyer J.C., Cheevers W.P.;
RT   "Nucleotide sequence of caprine interferon-gamma, interleukin-2 and
RT   interleukin-4 cDNAs.";
RL   Submitted (DEC-1996) 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; U34273; AAB38526.1; -; mRNA.
DR   RefSeq; NP_001272610.1; NM_001285681.1.
DR   AlphaFoldDB; P79155; -.
DR   SMR; P79155; -.
DR   STRING; 9925.ENSCHIP00000020527; -.
DR   GeneID; 100860814; -.
DR   KEGG; chx:100860814; -.
DR   CTD; 3565; -.
DR   OrthoDB; 1495672at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
DR   GO; GO:0048295; P:positive regulation of isotype switching to IgE isotypes; ISS:UniProtKB.
DR   GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; ISS:UniProtKB.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISS:UniProtKB.
DR   GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; ISS:UniProtKB.
DR   GO; GO:0042325; P:regulation of phosphorylation; 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_0000015527"
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        27..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..105
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15137 MW;  E1A9CE3B4779905A CRC64;
     MGLTSQLIPA LVCLLVCTSH FVHGHKCDIT LEEIIKMLNI LTSQKNSCME LPVADVFAAP
     KNATEKETFC RAGIELRRIY RNHMCLNKFL GGLDRNLSSL ASKTCSVNEA KTSTSTLRDL
     LERLKTIMKE KYSKC
 
 
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