ARRC_MOUSE
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 03-AUG-2022, entry version 125.
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).
CC {ECO:0000250|UniProtKB:P36575, 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; Q9EQP6; -.
DR PeptideAtlas; Q9EQP6; -.
DR PRIDE; Q9EQP6; -.
DR ProteomicsDB; 277235; -.
DR Antibodypedia; 27367; 243 antibodies from 33 providers.
DR DNASU; 170735; -.
DR Ensembl; ENSMUST00000113769; ENSMUSP00000109398; ENSMUSG00000060890.
DR GeneID; 170735; -.
DR KEGG; mmu:170735; -.
DR UCSC; uc009twd.2; mouse.
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; SMDREVH; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; Q9EQP6; -.
DR TreeFam; TF314260; -.
DR BioGRID-ORCS; 170735; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9EQP6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9EQP6; protein.
DR Bgee; ENSMUSG00000060890; Expressed in retinal neural layer and 19 other tissues.
DR ExpressionAtlas; Q9EQP6; baseline and differential.
DR Genevisible; Q9EQP6; MM.
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; IPR033042; ARR3.
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; PTHR11792; 1.
DR PANTHER; PTHR11792:SF19; PTHR11792:SF19; 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; SSF81296; 2.
DR PROSITE; PS00295; ARRESTINS; 1.
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
