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ACKR4_MOUSE
ID   ACKR4_MOUSE             Reviewed;         350 AA.
AC   Q924I3; Q8C0M1; Q8QZW9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Atypical chemokine receptor 4;
DE   AltName: Full=C-C chemokine receptor type 11;
DE            Short=C-C CKR-11;
DE            Short=CC-CKR-11;
DE            Short=CCR-11;
DE   AltName: Full=CC chemokine receptor-like 1;
DE            Short=CCRL1;
DE   AltName: Full=CCX CKR;
GN   Name=Ackr4; Synonyms=Ccr11, Ccrl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=11063828; DOI=10.1016/s0165-5728(00)00371-4;
RA   Dorf M.E., Berman M.A., Tanabe S., Heesen M., Luo Y.;
RT   "Astrocytes express functional chemokine receptors.";
RL   J. Neuroimmunol. 111:109-121(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CHEMOKINES BINDING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11981810;
RX   DOI=10.1002/1521-4141(200205)32:5<1230::aid-immu1230>3.0.co;2-l;
RA   Townson J.R., Nibbs R.J.;
RT   "Characterization of mouse CCX-CKR, a receptor for the lymphocyte-
RT   attracting chemokines TECK/mCCL25, SLC/mCCL21 and MIP-3beta/mCCL19:
RT   comparison to human CCX-CKR.";
RL   Eur. J. Immunol. 32:1230-1241(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Luo Y., Berman M.A., Fischer F.R., Abromson-Leeman S.R., Kuziel W.A.,
RA   Gerard C., Dorf M.E.;
RT   "RANTES and eotaxin stimulate chemotaxis, chemokine/cytokine synthesis, and
RT   receptor modulation in murine astrocytes.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=23152546; DOI=10.1182/blood-2012-06-434886;
RA   Bunting M.D., Comerford I., Seach N., Hammett M.V., Asquith D.L.,
RA   Koerner H., Boyd R.L., Nibbs R.J., McColl S.R.;
RT   "CCX-CKR deficiency alters thymic stroma impairing thymocyte development
RT   and promoting autoimmunity.";
RL   Blood 121:118-128(2013).
CC   -!- FUNCTION: Atypical chemokine receptor that controls chemokine levels
CC       and localization via high-affinity chemokine binding that is uncoupled
CC       from classic ligand-driven signal transduction cascades, resulting
CC       instead in chemokine sequestration, degradation, or transcytosis. Also
CC       known as interceptor (internalizing receptor) or chemokine-scavenging
CC       receptor or chemokine decoy receptor. Acts as a receptor for chemokines
CC       CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not
CC       activate G-protein-mediated signal transduction but instead induces
CC       beta-arrestin recruitment, leading to ligand internalization. Plays an
CC       important role in controlling the migration of immune and cancer cells
CC       that express chemokine receptors CCR7 and CCR9, by reducing the
CC       availability of CCL19, CCL21, and CCL25 through internalization.
CC       Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell
CC       development in the thymus and inhibits spontaneous autoimmunity.
CC       {ECO:0000269|PubMed:11981810, ECO:0000269|PubMed:23152546}.
CC   -!- SUBUNIT: Forms heteromers with CXCR3. Interacts with ARRB1 and ARRB2
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome
CC       {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Predominantly localizes to endocytic vesicles, and
CC       upon stimulation by the ligand is internalized via caveolae. Once
CC       internalized, the ligand dissociates from the receptor, and is targeted
CC       to degradation while the receptor is recycled back to the cell membrane
CC       (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, heart, spleen, skeletal muscle,
CC       testis, astrocytes and microglia. Expressed by cortical thymic
CC       epithelial cells. {ECO:0000269|PubMed:11063828,
CC       ECO:0000269|PubMed:11981810, ECO:0000269|PubMed:23152546}.
CC   -!- PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be
CC       phosphorylated. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice have a larger thymus with relatively fewer
CC       cortical thymic epithelial cells and this is associated with severe
CC       reductions in cortical CCL25 distribution and accumulation of DN2
CC       thymocyte precursor cells in the medulla. The downstream effects
CC       materialize in reduced proportions of DN3 cells and significantly
CC       reduced numbers of cortical DN3 cells. Aberrant thymocyte development
CC       culminates in increased prevalence of spontaneous autoimmune-like
CC       disease, characterized by lymphocytic infiltration of peripheral
CC       organs. {ECO:0000269|PubMed:23152546}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00521}.
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DR   EMBL; AF306532; AAK81712.1; -; mRNA.
DR   EMBL; AY072796; AAL68400.1; -; mRNA.
DR   EMBL; AY072938; AAL68962.1; -; mRNA.
DR   EMBL; AK030643; BAC27061.1; -; mRNA.
DR   EMBL; AK042430; BAC31258.1; -; mRNA.
DR   CCDS; CCDS23459.1; -.
DR   RefSeq; NP_663746.2; NM_145700.2.
DR   RefSeq; XP_006511797.1; XM_006511734.3.
DR   RefSeq; XP_006511798.1; XM_006511735.3.
DR   AlphaFoldDB; Q924I3; -.
DR   SMR; Q924I3; -.
DR   STRING; 10090.ENSMUSP00000075507; -.
DR   GlyGen; Q924I3; 2 sites.
DR   PhosphoSitePlus; Q924I3; -.
DR   PaxDb; Q924I3; -.
DR   PRIDE; Q924I3; -.
DR   Antibodypedia; 17718; 249 antibodies from 28 providers.
DR   DNASU; 252837; -.
DR   Ensembl; ENSMUST00000076147; ENSMUSP00000075507; ENSMUSG00000079355.
DR   Ensembl; ENSMUST00000188000; ENSMUSP00000140792; ENSMUSG00000079355.
DR   Ensembl; ENSMUST00000219146; ENSMUSP00000152036; ENSMUSG00000079355.
DR   GeneID; 252837; -.
DR   KEGG; mmu:252837; -.
DR   UCSC; uc009rhh.2; mouse.
DR   CTD; 51554; -.
DR   MGI; MGI:2181676; Ackr4.
DR   VEuPathDB; HostDB:ENSMUSG00000079355; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234667; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; Q924I3; -.
DR   OMA; YNVVKLC; -.
DR   OrthoDB; 839817at2759; -.
DR   PhylomeDB; Q924I3; -.
DR   TreeFam; TF330966; -.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   BioGRID-ORCS; 252837; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Ccrl2; mouse.
DR   PRO; PR:Q924I3; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q924I3; protein.
DR   Bgee; ENSMUSG00000079355; Expressed in lip and 84 other tissues.
DR   Genevisible; Q924I3; MM.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR   GO; GO:0004950; F:chemokine receptor activity; ISS:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   InterPro; IPR005383; ACKR4.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR01558; CHEMOKINER11.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..350
FT                   /note="Atypical chemokine receptor 4"
FT                   /id="PRO_0000069297"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..77
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..99
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        50
FT                   /note="V -> M (in Ref. 4; BAC27061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="V -> L (in Ref. 2; AAL68400/AAL68962)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  39531 MW;  C5F7D9DC949CECCF CRC64;
     MALELNQSAE YYYEENEMNY THDYSQYEVI CIKEEVRQFA KVFLPAFFTV AFVTGLAGNS
     VVVAIYAYYK KQRTKTDVYI LNLAVADLLL LITLPFWAVN AVHGWILGKM MCKVTSALYT
     VNFVSGMQFL ACISIDRYWA ITKAPSQSGA GRPCWIICCC VWMAAILLSI PQLVFYTVNQ
     NARCTPIFPH HLGTSLKASI QMLEIGIGFV VPFLIMGVCY ASTARALIKM PNIKKSRPLR
     VLLAVVVVFI VTQLPYNVVK FCQAIDAIYL LITSCDMSKR MDVAIQVTES IALFHSCLNP
     ILYVFMGASF KNYIMKVAKK YGSWRRQRQN VEEIPFDSEG PTEPTSSFTI
 
 
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