ARRS_CANLF
ID ARRS_CANLF Reviewed; 405 AA.
AC Q28281;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=S-arrestin;
DE AltName: Full=48 kDa protein;
DE AltName: Full=Retinal S-antigen;
DE Short=S-AG;
DE AltName: Full=Rod photoreceptor arrestin;
GN Name=SAG; Synonyms=ARR, SAG1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle X Briard; TISSUE=Retina;
RX PubMed=9088745; DOI=10.1076/ceyr.16.3.270.15413;
RA Veske A., Nafstroem K., Finckh U., Sargan D.R., Nilsson S.E.G., Gal A.;
RT "Isolation of canine retinal arrestin cDNA and exclusion of three candidate
RT genes for Swedish Briard retinal dystrophy.";
RL Curr. Eye Res. 16:270-274(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-14; VAL-101; THR-103;
RP TYR-257 AND GLU-377.
RX PubMed=12123530; DOI=10.1186/1471-2156-3-12;
RA Dekomien G., Epplen J.T.;
RT "Screening of the arrestin gene in dogs afflicted with generalized
RT progressive retinal atrophy.";
RL BMC Genet. 3:12-12(2002).
CC -!- FUNCTION: Binds to photoactivated, phosphorylated RHO and terminates
CC RHO signaling via G-proteins by competing with G-proteins for the same
CC binding site on RHO. May play a role in preventing light-dependent
CC degeneration of retinal photoreceptor cells.
CC {ECO:0000250|UniProtKB:P20443}.
CC -!- SUBUNIT: Monomer. Homodimer. Homotetramer. Interacts with RHO (via the
CC phosphorylated C-terminus). {ECO:0000250|UniProtKB:P10523}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000250|UniProtKB:P20443}. Membrane
CC {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor
CC outer segments in light-exposed retina. Evenly distributed throughout
CC rod photoreceptor cells in dark-adapted retina (By similarity).
CC Predominantly dectected at the proximal region of photoreceptor outer
CC segments, near disk membranes. {ECO:0000250|UniProtKB:P08168,
CC ECO:0000250|UniProtKB:P10523}.
CC -!- DOMAIN: The C-terminus interferes with binding to non-phosphorylated
CC RHO. Interaction with phosphorylated RHO triggers displacement of the
CC C-terminus and leads to a conformation change that mediates high-
CC affinity RHO binding. {ECO:0000250|UniProtKB:P08168}.
CC -!- DISEASE: Note=Defects in SAG may be the cause of generalized
CC progressive retinal atrophy (gPRA) in some breeds.
CC {ECO:0000305|PubMed:12123530}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; X98460; CAA67100.1; -; mRNA.
DR EMBL; AJ426068; CAD19827.1; -; Genomic_DNA.
DR EMBL; AJ426069; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426070; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426071; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426072; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426073; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426074; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426075; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426076; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426077; CAD19827.1; JOINED; Genomic_DNA.
DR EMBL; AJ426078; CAD19827.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001003230.1; NM_001003230.1.
DR AlphaFoldDB; Q28281; -.
DR SMR; Q28281; -.
DR STRING; 9612.ENSCAFP00000017366; -.
DR PaxDb; Q28281; -.
DR GeneID; 403906; -.
DR KEGG; cfa:403906; -.
DR CTD; 6295; -.
DR eggNOG; KOG3865; Eukaryota.
DR InParanoid; Q28281; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; PTHR11792; 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 2: Evidence at transcript level;
KW Cell projection; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..405
FT /note="S-arrestin"
FT /id="PRO_0000205185"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15887"
FT VARIANT 14
FT /note="H -> C (requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:12123530"
FT VARIANT 101
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:12123530"
FT VARIANT 103
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:12123530"
FT VARIANT 257
FT /note="D -> Y"
FT /evidence="ECO:0000269|PubMed:12123530"
FT VARIANT 377
FT /note="A -> E"
FT /evidence="ECO:0000269|PubMed:12123530"
SQ SEQUENCE 405 AA; 45177 MW; CDDE31B82FEDEBE6 CRC64;
MAASGKTSKS ASNHVIFKKI SRDKSVTIYL GKRDYIDHVE QVEPVDGIVL VDPELVKGKK
VYVSLTCAFR YGQEDIDVIG LSFRRDLYFS QVQVFPPVEA AGAPTKLQES LMKKLGGNTY
PFLLTFPDYL PCSVMLQPAP QDMGKCCGVD FEVKAFARDS TEDEEDKVPK KSSVRLLIRK
VQHAPSKMGP QPRAEAAWQF FMSDKPLHLA VSLSKEIYFH GEPITVTVTV TNNTEKTVKK
IKALVEQVAN VVLYSSDYYT KPVAQEETQE KVPPNSTLTT TLTLVPLLAN NRERRGIALD
GKIKHEDTNL ASSTIIKEGI DRTVLGILVS YHIKVKLTVS GFLGELTSSE VATEVPFRLM
HPQPEDPATA KESFQDANLV FEEFARQNLK DFAEEGKKDR EAMDE
