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P29456 (IL10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-10

Short name=IL-10
Alternative name(s):
Cytokine synthesis inhibitory factor
Short name=CSIF
Gene names
Name:Il10
Synonyms:Il-10
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the IL-10 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular response to estradiol stimulus

Inferred from expression pattern. Source: RGD

immune response

Inferred from mutant phenotype Ref.2. Source: RGD

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype. Source: RGD

negative regulation of cytokine secretion involved in immune response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from direct assay. Source: RGD

negative regulation of interleukin-6 production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nitric oxide biosynthetic process

Inferred from direct assay. Source: RGD

negative regulation of tumor necrosis factor biosynthetic process

Inferred from direct assay. Source: RGD

positive regulation of B cell apoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

receptor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sensory perception of pain

Inferred from direct assay. Source: RGD

response to activity

Inferred from expression pattern. Source: RGD

response to carbon monoxide

Inferred from expression pattern. Source: RGD

response to drug

Inferred from expression pattern. Source: RGD

response to glucocorticoid stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

response to inactivity

Inferred from expression pattern. Source: RGD

response to insulin stimulus

Inferred from expression pattern. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern. Source: RGD

   Cellular componentextracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functioncytokine activity

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-10 receptor binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 178160Interleukin-10
PRO_0000015372

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 126 By similarity
Disulfide bond80 ↔ 132 By similarity

Experimental info

Sequence conflict21P → L in CAA43090. Ref.2
Sequence conflict651L → V in CAA43090. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29456 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 0225AA6C63DAB70B

FASTA17820,426
        10         20         30         40         50         60 
MPGSALLCCL LLLAGVKTSK GHSIRGDNNC THFPVSQTHM LRELRAAFSQ VKTFFQKKDQ 

        70         80         90        100        110        120 
LDNILLTDSL LQDFKGYLGC QALSEMIKFY LVEVMPQAEN HGPEIKEHLN SLGEKLKTLW 

       130        140        150        160        170 
IQLRRCHRFL PCENKSKAVE QVKNDFNKLQ DKGVYKAMNE FDIFINCIEA YVTLKMKN 

« Hide

References

[1]"Synthesis and characterization of rat interleukin-10 (IL-10) cDNA clones from the RNA of cultured OX8-OX22-thoracic duct T cells."
Goodman R.E., Oblak J., Bell R.G.
Biochem. Biophys. Res. Commun. 189:1-7(1992) [PubMed: 1280414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of rat cytokine synthesis inhibitory factor (IL-10) cDNA and expression in spleen and macrophages."
Feng L., Tang W.W., Chang J.C.C., Wilson C.B.
Biochem. Biophys. Res. Commun. 192:452-458(1993) [PubMed: 8484757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02926 mRNA. Translation: AAA41425.1.
X60675 mRNA. Translation: CAA43090.1.
IPIIPI00326111.
PIRJN0475.
RefSeqNP_036986.2. NM_012854.2.
UniGeneRn.9868.

3D structure databases

ProteinModelPortalP29456.
SMRP29456. Positions 25-178.
ModBaseSearch...

Protein-protein interaction databases

STRINGP29456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006246; ENSRNOP00000006246; ENSRNOG00000004647.
GeneID25325.
KEGGrno:25325.
UCSCNM_012854. rat.

Organism-specific databases

CTD3586.
RGD2886. Il10.

Phylogenomic databases

eggNOGroNOG16135.
GeneTreeENSGT00510000048535.
HOVERGENHBG004110.
InParanoidP29456.
OMAKGYLGCQ.
OrthoDBEOG4F1X4G.
PhylomeDBP29456.

Gene expression databases

ArrayExpressP29456.
GenevestigatorP29456.
GermOnlineENSRNOG00000004647. Rattus norvegicus.

Family and domain databases

InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR020443. Interleukin-10/19/20/24.
IPR020423. Interleukin-10_CS.
IPR000098. Interleukin_10.
[Graphical view]
Gene3DG3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.
KOK05443.
PANTHERPTHR11585. Interleukin_10. 1 hit.
PfamPF00726. IL10. 1 hit.
[Graphical view]
PRINTSPR01294. INTRLEUKIN10.
SMARTSM00188. IL10. 1 hit.
[Graphical view]
SUPFAMSSF47266. 4_helix_cytokine. 1 hit.
PROSITEPS00520. INTERLEUKIN_10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606181.

Entry information

Entry nameIL10_RAT
AccessionPrimary (citable) accession number: P29456
Secondary accession number(s): Q63263
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families