Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C-C motif chemokine 6

Gene

Ccl6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

CCL6(22-95) and CCL6(23-95) are potent chemoattractants.1 Publication

GO - Biological processi

  1. cell chemotaxis Source: Ensembl
  2. immune response Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Chemotaxis

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_229705. Formyl peptide receptors bind formyl peptides and many other ligands.
REACT_250376. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
C-C motif chemokine 6
Alternative name(s):
Protein C10
Small-inducible cytokine A6
Cleaved into the following 2 chains:
Gene namesi
Name:Ccl6
Synonyms:C10, Scya6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98263. Ccl6.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 11695C-C motif chemokine 6PRO_0000005182Add
BLAST
Chaini43 – 11674CCL6(22-95)PRO_0000041844Add
BLAST
Chaini44 – 11673CCL6(23-95)PRO_0000041845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 73By similarity
Disulfide bondi51 ↔ 89By similarity
Disulfide bondi60 ↔ 100By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP27784.
PRIDEiP27784.

PTM databases

PhosphoSiteiP27784.

Expressioni

Tissue specificityi

Expressed in myelopoietic bone marrow cultures stimulated by GM-CSF.

Inductioni

Associated with stimuli that promote myeloid differentiation.

Gene expression databases

BgeeiP27784.
CleanExiMM_CCL6.
GenevestigatoriP27784.

Structurei

3D structure databases

ProteinModelPortaliP27784.
SMRiP27784. Positions 45-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG26004.
GeneTreeiENSGT00730000110278.
HOGENOMiHOG000036685.
HOVERGENiHBG017871.
InParanoidiP27784.
KOiK05510.
OMAiKEDRRYN.
OrthoDBiEOG79KPHQ.
PhylomeDBiP27784.
TreeFamiTF334888.

Family and domain databases

InterProiIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNSKTAISF FILVAVLGSQ AGLIQEMEKE DRRYNPPIIH QGFQDTSSDC
60 70 80 90 100
CFSYATQIPC KRFIYYFPTS GGCIKPGIIF ISRRGTQVCA DPSDRRVQRC
110
LSTLKQGPRS GNKVIA
Length:116
Mass (Da):12,984
Last modified:August 1, 1992 - v1
Checksum:i2B483B5DE8417082
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431F → V in AAH02073 (PubMed:15489334).Curated
Sequence conflicti93 – 931S → R in BAB25734 (PubMed:16141072).Curated
Sequence conflicti111 – 1111G → R in AAH02073 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58004 mRNA. Translation: AAA37329.1.
AF128188 mRNA. Translation: AAF22529.1.
AF128189 mRNA. Translation: AAF22530.1.
AF128190 mRNA. Translation: AAF22531.1.
AF128191 mRNA. Translation: AAF22532.1.
AF128192 mRNA. Translation: AAF22533.1.
AB051897 Genomic DNA. Translation: BAB18729.1.
AK002697 mRNA. Translation: BAB22291.1.
AK008547 mRNA. Translation: BAB25734.1.
AK150336 mRNA. Translation: BAE29478.1.
AK154553 mRNA. Translation: BAE32672.1.
AL596122 Genomic DNA. Translation: CAI25134.1.
BC002073 mRNA. Translation: AAH02073.1.
CCDSiCCDS25171.1.
PIRiI49555.
RefSeqiNP_033165.1. NM_009139.3.
UniGeneiMm.137.

Genome annotation databases

EnsembliENSMUST00000019071; ENSMUSP00000019071; ENSMUSG00000018927.
GeneIDi20305.
KEGGimmu:20305.
UCSCiuc007kpm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58004 mRNA. Translation: AAA37329.1.
AF128188 mRNA. Translation: AAF22529.1.
AF128189 mRNA. Translation: AAF22530.1.
AF128190 mRNA. Translation: AAF22531.1.
AF128191 mRNA. Translation: AAF22532.1.
AF128192 mRNA. Translation: AAF22533.1.
AB051897 Genomic DNA. Translation: BAB18729.1.
AK002697 mRNA. Translation: BAB22291.1.
AK008547 mRNA. Translation: BAB25734.1.
AK150336 mRNA. Translation: BAE29478.1.
AK154553 mRNA. Translation: BAE32672.1.
AL596122 Genomic DNA. Translation: CAI25134.1.
BC002073 mRNA. Translation: AAH02073.1.
CCDSiCCDS25171.1.
PIRiI49555.
RefSeqiNP_033165.1. NM_009139.3.
UniGeneiMm.137.

3D structure databases

ProteinModelPortaliP27784.
SMRiP27784. Positions 45-105.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP27784.

Proteomic databases

PaxDbiP27784.
PRIDEiP27784.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019071; ENSMUSP00000019071; ENSMUSG00000018927.
GeneIDi20305.
KEGGimmu:20305.
UCSCiuc007kpm.1. mouse.

Organism-specific databases

CTDi20305.
MGIiMGI:98263. Ccl6.

Phylogenomic databases

eggNOGiNOG26004.
GeneTreeiENSGT00730000110278.
HOGENOMiHOG000036685.
HOVERGENiHBG017871.
InParanoidiP27784.
KOiK05510.
OMAiKEDRRYN.
OrthoDBiEOG79KPHQ.
PhylomeDBiP27784.
TreeFamiTF334888.

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_229705. Formyl peptide receptors bind formyl peptides and many other ligands.
REACT_250376. G alpha (i) signalling events.

Miscellaneous databases

NextBioi298059.
PROiP27784.
SOURCEiSearch...

Gene expression databases

BgeeiP27784.
CleanExiMM_CCL6.
GenevestigatoriP27784.

Family and domain databases

InterProiIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel expression pattern of a new member of the MIP-1 family of cytokine-like genes."
    Orlofsky A., Berger M.S., Prystowsky M.B.
    Cell Regul. 2:403-412(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CBA/J.
    Tissue: Bone marrow.
  2. "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 [MRNA].
    Strain: B10.S/J, BALB/c, DBA/2J, NOD/LtJ and SJL/J.
    Tissue: Spleen.
  3. "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 [MRNA].
    Strain: 129/Sv.
  4. "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.
    , 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 and NOD.
    Tissue: Bone marrow and Pancreas.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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.
  7. "Proteolytic activation of alternative CCR1 ligands in inflammation."
    Berahovich R.D., Miao Z., Wang Y., Premack B., Howard M.C., Schall T.J.
    J. Immunol. 174:7341-7351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CCL6(22-95) AND CCL6(23-95), PROTEOLYTIC PROCESSING OF N-TERMINAL, FUNCTION.

Entry informationi

Entry nameiCCL6_MOUSE
AccessioniPrimary (citable) accession number: P27784
Secondary accession number(s): Q3U3W3
, Q5QNW1, Q99M24, Q9D830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 7, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.