Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30882 (CCL5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
C-C motif chemokine 5
Alternative name(s):
MuRantes
SIS-delta
Small-inducible cytokine A5
T-cell-specific protein RANTES
Gene names
Name:Ccl5
Synonyms:Scya5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length91 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils.

Subcellular location

Secreted.

Tissue specificity

T-cell and macrophage specific.

Sequence similarities

Belongs to the intercrine beta (chemokine CC) family.

Ontologies

Keywords
   Biological processChemotaxis
Inflammatory response
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from electronic annotation. Source: Ensembl

activation of phospholipase D activity

Inferred from sequence or structural similarity. Source: BHF-UCL

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular protein complex assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

eosinophil chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

exocytosis

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from mutant phenotype PubMed 23696660. Source: MGI

leukocyte cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of G-protein coupled receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of macrophage apoptotic process

Inferred from mutant phenotype PubMed 16208318. Source: BHF-UCL

negative regulation of viral genome replication

Inferred from sequence or structural similarity. Source: BHF-UCL

neutrophil activation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T cell apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T cell chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell-cell adhesion mediated by integrin

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cellular biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of chemokine (C-X-C motif) ligand 2 production

Non-traceable author statement PubMed 21293018. Source: BHF-UCL

positive regulation of defense response to virus by host

Inferred by curator PubMed 16208318. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 23696660. Source: MGI

positive regulation of homotypic cell-cell adhesion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of macrophage chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of monocyte chemotaxis

Inferred from direct assay PubMed 19779041. Source: BHF-UCL

positive regulation of natural killer cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: GOC

positive regulation of smooth muscle cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein tetramerization

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of T cell activation

Inferred from sequence or structural similarity. Source: BHF-UCL

response to cytokine

Inferred from direct assay Ref.1. Source: MGI

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: MGI

extracellular space

Inferred from direct assay PubMed 21148126PubMed 23460747. Source: MGI

   Molecular_functionCCR1 chemokine receptor binding

Inferred from direct assay PubMed 15557190. Source: BHF-UCL

CCR5 chemokine receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

chemoattractant activity

Inferred from electronic annotation. Source: Ensembl

chemokine activity

Inferred from sequence or structural similarity. Source: BHF-UCL

chemokine receptor antagonist activity

Inferred from sequence or structural similarity. Source: BHF-UCL

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: Ensembl

phospholipase activator activity

Inferred from electronic annotation. Source: Ensembl

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase activity

Inferred from electronic annotation. Source: Ensembl

protein self-association

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor signaling protein tyrosine kinase activator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 9168C-C motif chemokine 5
PRO_0000005179

Amino acid modifications

Disulfide bond33 ↔ 57 By similarity
Disulfide bond34 ↔ 73 By similarity

Experimental info

Sequence conflict191T → A in AAB22330. Ref.2
Sequence conflict411A → E in AAA40029. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30882 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 5DFD66F4684FE1C8

FASTA9110,071
        10         20         30         40         50         60 
MKISAAALTI ILTAAALCTP APASPYGSDT TPCCFAYLSL ALPRAHVKEY FYTSSKCSNL 

        70         80         90 
AVVFVTRRNR QVCANPEKKW VQEYINYLEM S 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNA from renal tubular epithelium encoding murine Rantes."
Heeger P., Wolf G., Meyers C., Sun M.J., O'Farrell S.C., Krensky A.M., Neilson E.G.
Kidney Int. 41:220-225(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and expression of the murine RANTES cytokine: structural and functional conservation between mouse and man."
Schall T.J., Simpson N.J., Mak J.Y.
Eur. J. Immunol. 22:1477-1481(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning, genomic organization, and chromosomal localization of the Scya5 gene encoding the murine chemokine RANTES."
Danoff T.M., Lalley P.A., Chang Y.S., Heeger P.S., Neilson E.G.
J. Immunol. 152:1182-1189(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NIH Swiss.
[4]"Definition of a lipopolysaccharide-responsive element in the 5'-flanking regions of MuRantes and crg-2."
Shin H.S., Drysdale B.E., Shin M.L., Noble P.W., Fisher S.N., Paznekas W.A.
Mol. Cell. Biol. 14:2914-2925(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[5]"Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for eae7, a locus controlling susceptibility to monophasic remitting/nonrelapsing experimental allergic encephalomyelitis."
Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., Blankenhorn E.P.
J. Immunol. 163:2262-2266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B10.S/J, BALB/cJ, DBA/2J, NOD/LtJ and SJL/J.
Tissue: Spleen.
[6]"Organization of the mouse CC chemokine cluster containing the genes for C10, MRP-2 and RANTES."
Nomiyama H.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/Sv.
[7]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77747 mRNA. Translation: AAA40029.1.
S37648 mRNA. Translation: AAB22330.1.
U02298 Unassigned DNA. Translation: AAA18302.1.
X70675 Genomic DNA. Translation: CAA50011.1.
AF065944 mRNA. Translation: AAC17511.1.
AF065945 mRNA. Translation: AAC17512.1.
AF065946 mRNA. Translation: AAC17513.1.
AF065947 mRNA. Translation: AAC17514.1.
AF128187 mRNA. Translation: AAF22528.1.
AB051897 Genomic DNA. Translation: BAB18731.1.
AK003101 mRNA. Translation: BAB22566.1.
BC033508 mRNA. Translation: AAH33508.1.
PIRA46539. I48875.
RefSeqNP_038681.2. NM_013653.3.
UniGeneMm.284248.

3D structure databases

ProteinModelPortalP30882.
SMRP30882. Positions 28-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000039600.

PTM databases

PhosphoSiteP30882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035938; ENSMUSP00000039600; ENSMUSG00000035042.
GeneID20304.
KEGGmmu:20304.
UCSCuc007kpi.2. mouse.

Organism-specific databases

CTD6352.
MGIMGI:98262. Ccl5.

Phylogenomic databases

eggNOGNOG38896.
HOGENOMHOG000036685.
HOVERGENHBG017871.
InParanoidP30882.
KOK12499.
OMAQEYFYTS.
OrthoDBEOG7CVQ1F.
PhylomeDBP30882.
TreeFamTF334888.

Gene expression databases

ArrayExpressP30882.
BgeeP30882.
CleanExMM_CCL5.
GenevestigatorP30882.

Family and domain databases

InterProIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamPF00048. IL8. 1 hit.
[Graphical view]
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298055.
PROP30882.
SOURCESearch...

Entry information

Entry nameCCL5_MOUSE
AccessionPrimary (citable) accession number: P30882
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 123 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot