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Q924I3 (ACKR4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Atypical chemokine receptor 4
Alternative name(s):
C-C chemokine receptor type 11
Short name=C-C CKR-11
Short name=CC-CKR-11
Short name=CCR-11
CC chemokine receptor-like 1
Short name=CCRL1
CCX CKR
Gene names
Name:Ackr4
Synonyms:Ccr11, Ccrl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus and inhibits spontaneous autoimmunity. Ref.2 Ref.5

Subunit structure

Forms heteromers with CXCR3. Interacts with ARRB1 and ARRB2 By similarity.

Subcellular location

Early endosome By similarity. Recycling endosome By similarity. Cell membrane; Multi-pass membrane protein By similarity. Note: Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via caveolae. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane By similarity.

Tissue specificity

Expressed in lung, heart, spleen, skeletal muscle, testis, astrocytes and microglia. Expressed by cortical thymic epithelial cells. Ref.1 Ref.2 Ref.5

Post-translational modification

The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated By similarity.

Disruption phenotype

Mice have a larger thymus with relatively fewer cortical thymic epithelial cells and this is associated with severe reductions in cortical CCL25 distribution and accumulation of DN2 thymocyte precursor cells in the medulla. The downstream effects materialize in reduced proportions of DN3 cells and significantly reduced numbers of cortical DN3 cells. Aberrant thymocyte development culminates in increased prevalence of spontaneous autoimmune-like disease, characterized by lymphocytic infiltration of peripheral organs. Ref.5

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Atypical chemokine receptor subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Atypical chemokine receptor 4
PRO_0000069297

Regions

Topological domain1 – 4141Extracellular Potential
Transmembrane42 – 6221Helical; Name=1; Potential
Topological domain63 – 7715Cytoplasmic Potential
Transmembrane78 – 9922Helical; Name=2; Potential
Topological domain100 – 11415Extracellular Potential
Transmembrane115 – 13521Helical; Name=3; Potential
Topological domain136 – 15419Cytoplasmic Potential
Transmembrane155 – 17521Helical; Name=4; Potential
Topological domain176 – 19924Extracellular Potential
Transmembrane200 – 22021Helical; Name=5; Potential
Topological domain221 – 24020Cytoplasmic Potential
Transmembrane241 – 26121Helical; Name=6; Potential
Topological domain262 – 28928Extracellular Potential
Transmembrane290 – 31021Helical; Name=7; Potential
Topological domain311 – 35040Cytoplasmic Potential

Amino acid modifications

Glycosylation61N-linked (GlcNAc...) Potential
Glycosylation191N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict501V → M in BAC27061. Ref.4
Sequence conflict2871V → L in AAL68400. Ref.2
Sequence conflict2871V → L in AAL68962. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q924I3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C5F7D9DC949CECCF

FASTA35039,531
        10         20         30         40         50         60 
MALELNQSAE YYYEENEMNY THDYSQYEVI CIKEEVRQFA KVFLPAFFTV AFVTGLAGNS 

        70         80         90        100        110        120 
VVVAIYAYYK KQRTKTDVYI LNLAVADLLL LITLPFWAVN AVHGWILGKM MCKVTSALYT 

       130        140        150        160        170        180 
VNFVSGMQFL ACISIDRYWA ITKAPSQSGA GRPCWIICCC VWMAAILLSI PQLVFYTVNQ 

       190        200        210        220        230        240 
NARCTPIFPH HLGTSLKASI QMLEIGIGFV VPFLIMGVCY ASTARALIKM PNIKKSRPLR 

       250        260        270        280        290        300 
VLLAVVVVFI VTQLPYNVVK FCQAIDAIYL LITSCDMSKR MDVAIQVTES IALFHSCLNP 

       310        320        330        340        350 
ILYVFMGASF KNYIMKVAKK YGSWRRQRQN VEEIPFDSEG PTEPTSSFTI 

« Hide

References

« Hide 'large scale' references
[1]"Astrocytes express functional chemokine receptors."
Dorf M.E., Berman M.A., Tanabe S., Heesen M., Luo Y.
J. Neuroimmunol. 111:109-121(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: BALB/c.
[2]"Characterization of mouse CCX-CKR, a receptor for the lymphocyte-attracting chemokines TECK/mCCL25, SLC/mCCL21 and MIP-3beta/mCCL19: comparison to human CCX-CKR."
Townson J.R., Nibbs R.J.
Eur. J. Immunol. 32:1230-1241(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CHEMOKINES BINDING, TISSUE SPECIFICITY.
[3]"RANTES and eotaxin stimulate chemotaxis, chemokine/cytokine synthesis, and receptor modulation in murine astrocytes."
Luo Y., Berman M.A., Fischer F.R., Abromson-Leeman S.R., Kuziel W.A., Gerard C., Dorf M.E.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[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. 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: Head and Thymus.
[5]"CCX-CKR deficiency alters thymic stroma impairing thymocyte development and promoting autoimmunity."
Bunting M.D., Comerford I., Seach N., Hammett M.V., Asquith D.L., Koerner H., Boyd R.L., Nibbs R.J., McColl S.R.
Blood 121:118-128(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF306532 mRNA. Translation: AAK81712.1.
AY072796 mRNA. Translation: AAL68400.1.
AY072938 mRNA. Translation: AAL68962.1.
AK030643 mRNA. Translation: BAC27061.1.
AK042430 mRNA. Translation: BAC31258.1.
RefSeqNP_663746.2. NM_145700.2.
XP_006511797.1. XM_006511734.1.
XP_006511798.1. XM_006511735.1.
UniGeneMm.269254.

3D structure databases

ProteinModelPortalQ924I3.
SMRQ924I3. Positions 39-322.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ924I3.

Proteomic databases

PRIDEQ924I3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076147; ENSMUSP00000075507; ENSMUSG00000079355.
GeneID252837.
KEGGmmu:252837.
UCSCuc009rhh.2. mouse.

Organism-specific databases

CTD51554.
MGIMGI:2181676. Ackr4.

Phylogenomic databases

eggNOGNOG148788.
GeneTreeENSGT00730000110640.
HOGENOMHOG000234122.
HOVERGENHBG106917.
InParanoidQ924I3.
KOK04186.
OMALEICIGF.
OrthoDBEOG7GJ6DG.
PhylomeDBQ924I3.
TreeFamTF330966.

Gene expression databases

BgeeQ924I3.
CleanExMM_CCRL1.
GenevestigatorQ924I3.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR005383. Chemokine_CCRL1.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF35. PTHR24227:SF35. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00657. CCCHEMOKINER.
PR01558. CHEMOKINER11.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio387341.
PROQ924I3.
SOURCESearch...

Entry information

Entry nameACKR4_MOUSE
AccessionPrimary (citable) accession number: Q924I3
Secondary accession number(s): Q8C0M1, Q8QZW9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 95 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

MGD cross-references

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries