ID   ARRC_RAT                Reviewed;          92 AA.
AC   P36576;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Arrestin-C;
DE   AltName: Full=Cone arrestin;
DE            Short=cArr;
DE   AltName: Full=Retinal cone arrestin-3;
DE   Flags: Fragment;
GN   Name=Arr3; Synonyms=Car;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX   PubMed=8308033; DOI=10.1016/s0021-9258(17)41820-5;
RA   Craft C.M., Whitmore D.H., Wiechmann A.F.;
RT   "Cone arrestin identified by targeting expression of a functional family.";
RL   J. Biol. Chem. 269:4613-4619(1994).
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:0000250|UniProtKB:Q9EQP6}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:Q9EQP6}.
CC   -!- TISSUE SPECIFICITY: Retina and pineal gland.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; U03628; AAA17552.1; -; mRNA.
DR   PIR; I70113; I70113.
DR   AlphaFoldDB; P36576; -.
DR   SMR; P36576; -.
DR   STRING; 10116.ENSRNOP00000068038; -.
DR   jPOST; P36576; -.
DR   PaxDb; P36576; -.
DR   UCSC; RGD:621385; rat.
DR   RGD; 621385; Arr3.
DR   eggNOG; KOG3865; Eukaryota.
DR   InParanoid; P36576; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR   GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0002046; F:opsin binding; ISO:RGD.
DR   GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR   GO; GO:0009968; P:negative regulation of signal transduction; TAS:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEP:RGD.
DR   Gene3D; 2.60.40.640; -; 1.
DR   InterPro; IPR033042; ARR3.
DR   InterPro; IPR000698; Arrestin.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11792; PTHR11792; 1.
DR   PANTHER; PTHR11792:SF19; PTHR11792:SF19; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Disulfide bond; Reference proteome; Sensory transduction;
KW   Vision.
FT   CHAIN           <1..92
FT                   /note="Arrestin-C"
FT                   /id="PRO_0000205205"
FT   NON_TER         1
SQ   SEQUENCE   92 AA;  9878 MW;  88F0C948643C83B9 CRC64;
     LKHEDTNLAS STILRPGMNK ELLGILVSYK VKVNLMVSYG GILGGLPASD VGVELPLILI
     HPKPPHGERA VATSSEDIVV EEFTQQNSQT QS