ID ARRC_MOUSE Reviewed; 381 AA. AC Q9EQP6; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 133. DE RecName: Full=Arrestin-C; DE AltName: Full=Cone arrestin; DE Short=cArr; DE AltName: Full=Retinal cone arrestin-3; GN Name=Arr3; 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]. RC TISSUE=Retina; RX PubMed=12135752; DOI=10.1016/s0014-5793(02)03014-4; RA Zhu X., Ma B., Babu S., Murage J., Knox B.E., Craft C.M.; RT "Mouse cone arrestin gene characterization: promoter targets expression to RT cone photoreceptors."; RL FEBS Lett. 524:116-122(2002). RN [2] RP PROTEIN SEQUENCE OF 310-319, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [3] RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=28151698; DOI=10.1369/0022155416689675; RA Zalis M.C., Johansson S., Englund-Johansson U.; RT "Immunocytochemical Profiling of Cultured Mouse Primary Retinal Cells."; RL J. Histochem. Cytochem. 65:223-239(2017). CC -!- FUNCTION: May play a role in an as yet undefined retina-specific signal CC transduction. Could bind to photoactivated-phosphorylated red/green CC opsins. CC -!- SUBUNIT: Homodimer; disulfide-linked in response to retinal CC illumination (By similarity). Interacts with CXCR4; the interaction is CC dependent on the C-terminal phosphorylation of CXCR4 and modulates the CC calcium ion mobilization activity of CXCR4 (By similarity). Interacts CC with GPR84 (By similarity). {ECO:0000250|UniProtKB:P36575, CC ECO:0000250|UniProtKB:Q9N0H5}. CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment CC {ECO:0000269|PubMed:28151698}. Cell projection, cilium, photoreceptor CC outer segment {ECO:0000269|PubMed:28151698}. CC -!- TISSUE SPECIFICITY: Inner and outer segments, and the inner plexiform CC regions of the retina. CC -!- DEVELOPMENTAL STAGE: At postnatal day 11 (P11) expressed in the soma CC and photoreceptor processes of the retinal inner segment, outer CC segment, outer plexiform layer, and inner plexiform layer. Expression CC in the inner plexiform layer is lost at P22. CC {ECO:0000269|PubMed:28151698}. CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF156979; AAG38954.1; -; mRNA. DR CCDS; CCDS41075.1; -. DR RefSeq; NP_573468.1; NM_133205.3. DR AlphaFoldDB; Q9EQP6; -. DR SMR; Q9EQP6; -. DR BioGRID; 228402; 4. DR STRING; 10090.ENSMUSP00000109398; -. DR iPTMnet; Q9EQP6; -. DR PhosphoSitePlus; Q9EQP6; -. DR MaxQB; Q9EQP6; -. DR PaxDb; 10090-ENSMUSP00000109398; -. DR PeptideAtlas; Q9EQP6; -. DR ProteomicsDB; 277235; -. DR Antibodypedia; 27367; 261 antibodies from 33 providers. DR DNASU; 170735; -. DR Ensembl; ENSMUST00000113769.8; ENSMUSP00000109398.2; ENSMUSG00000060890.12. DR GeneID; 170735; -. DR KEGG; mmu:170735; -. DR UCSC; uc009twd.2; mouse. DR AGR; MGI:2159617; -. DR CTD; 407; -. DR MGI; MGI:2159617; Arr3. DR VEuPathDB; HostDB:ENSMUSG00000060890; -. DR eggNOG; KOG3865; Eukaryota. DR GeneTree; ENSGT00950000182887; -. DR HOGENOM; CLU_033484_0_0_1; -. DR InParanoid; Q9EQP6; -. DR OMA; FHGEDIP; -. DR OrthoDB; 3059077at2759; -. DR PhylomeDB; Q9EQP6; -. DR TreeFam; TF314260; -. DR BioGRID-ORCS; 170735; 0 hits in 77 CRISPR screens. DR PRO; PR:Q9EQP6; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q9EQP6; Protein. DR Bgee; ENSMUSG00000060890; Expressed in retinal neural layer and 21 other cell types or tissues. DR ExpressionAtlas; Q9EQP6; baseline and differential. DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0002046; F:opsin binding; IDA:MGI. DR GO; GO:0051219; F:phosphoprotein binding; IDA:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0006897; P:endocytosis; IDA:MGI. DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central. DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0007601; P:visual perception; IBA:GO_Central. DR Gene3D; 2.60.40.640; -; 1. DR Gene3D; 2.60.40.840; -; 1. DR InterPro; IPR000698; Arrestin. DR InterPro; IPR014752; Arrestin-like_C. DR InterPro; IPR011021; Arrestin-like_N. DR InterPro; IPR011022; Arrestin_C-like. DR InterPro; IPR017864; Arrestin_CS. DR InterPro; IPR014753; Arrestin_N. DR InterPro; IPR014756; Ig_E-set. DR PANTHER; PTHR11792; ARRESTIN; 1. DR PANTHER; PTHR11792:SF19; ARRESTIN-C; 1. DR Pfam; PF02752; Arrestin_C; 1. DR Pfam; PF00339; Arrestin_N; 1. DR PRINTS; PR00309; ARRESTIN. DR SMART; SM01017; Arrestin_C; 1. DR SUPFAM; SSF81296; E set domains; 2. DR PROSITE; PS00295; ARRESTINS; 1. DR Genevisible; Q9EQP6; MM. PE 1: Evidence at protein level; KW Cell projection; Direct protein sequencing; Disulfide bond; KW Reference proteome; Sensory transduction; Vision. FT CHAIN 1..381 FT /note="Arrestin-C" FT /id="PRO_0000205204" SQ SEQUENCE 381 AA; 41921 MW; 3BEAC282EC438920 CRC64; MSTVFKKTSS NGKFSIYLGK RDFVDDVDTV EPIDGVVLVD PEYLEGRKLF VRLTCAFRYG RDDLDVIGLT FRKDLYVQTK QVAPAEPTSI QGPLTALQER LLHKLGVNAY PFTLQMVANL PCSVTLQPGP EDSGKPCGVD FEVKSFCAEN LEEKIPKSDS VQLVVRKVQF SALEPGPGPS AQTIRSFFLS SQPLQLQAWM DREVHYHGEA ISVHVSINNY TNKVIRRIKI AVVQTTDVVL YSLDKYTKTV FVQEFTETVA ANSSFSQTFA VTPLLAANCQ KQGLALDGKL KHEDTNLASS TILRPGMNKE LLGILVSYKV RVNLVVSYGG ILGGLPASDV GVELPVILIH PKPSPGERAV ATSSEDIVIE EFMQHNSQTQ S //