ID ARRS_RAT Reviewed; 403 AA.
AC P15887;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 24-JAN-2024, entry version 151.
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;
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=2714438; DOI=10.1016/0014-5793(89)81358-4;
RA Abe T., Yamaki K., Tsuda M., Singh V.K., Suzuki S., McKinnon R.,
RA Klein D.C., Donoso L.A., Shinohara T.;
RT "Rat pineal S-antigen: sequence analysis reveals presence of alpha-
RT transducin homologous sequence.";
RL FEBS Lett. 247:307-311(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2373176; DOI=10.1016/0014-4835(90)90178-w;
RA Abe T., Shinohara T.;
RT "S-antigen from the rat retina and pineal gland have identical sequences.";
RL Exp. Eye Res. 51:111-112(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX PubMed=2213004; DOI=10.1111/j.1471-4159.1990.tb04927.x;
RA Craft C.M., Whitmore D.H., Donoso L.A.;
RT "Differential expression of mRNA and protein encoding retinal and pineal S-
RT antigen during the light/dark cycle.";
RL J. Neurochem. 55:1461-1473(1990).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 -!- TISSUE SPECIFICITY: Retina and pineal gland.
CC {ECO:0000269|PubMed:2213004}.
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 -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; X51781; CAA36076.1; -; mRNA.
DR EMBL; X15353; CAA33412.1; -; mRNA.
DR EMBL; M60737; AAA42107.1; -; mRNA.
DR PIR; S03960; S03960.
DR RefSeq; NP_037155.2; NM_013023.2.
DR RefSeq; XP_008765418.1; XM_008767196.2.
DR AlphaFoldDB; P15887; -.
DR SMR; P15887; -.
DR STRING; 10116.ENSRNOP00000024733; -.
DR iPTMnet; P15887; -.
DR PhosphoSitePlus; P15887; -.
DR jPOST; P15887; -.
DR PaxDb; 10116-ENSRNOP00000024733; -.
DR DNASU; 25539; -.
DR Ensembl; ENSRNOT00000085770.2; ENSRNOP00000071579.1; ENSRNOG00000018185.7.
DR Ensembl; ENSRNOT00055013948; ENSRNOP00055011188; ENSRNOG00055008233.
DR Ensembl; ENSRNOT00060017383; ENSRNOP00060013507; ENSRNOG00060010282.
DR Ensembl; ENSRNOT00065035425; ENSRNOP00065028533; ENSRNOG00065020862.
DR GeneID; 25539; -.
DR KEGG; rno:25539; -.
DR UCSC; RGD:3619; rat.
DR AGR; RGD:3619; -.
DR CTD; 6295; -.
DR RGD; 3619; Sag.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR InParanoid; P15887; -.
DR OMA; QPAPQDM; -.
DR OrthoDB; 3059077at2759; -.
DR PhylomeDB; P15887; -.
DR TreeFam; TF314260; -.
DR Reactome; R-RNO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:P15887; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018185; Expressed in pancreas and 8 other cell types or tissues.
DR ExpressionAtlas; P15887; baseline and differential.
DR Genevisible; P15887; RN.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA: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:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
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; ARRESTIN; 1.
DR PANTHER; PTHR11792:SF15; S-ARRESTIN; 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.
PE 1: Evidence at protein level;
KW Cell projection; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..403
FT /note="S-arrestin"
FT /id="PRO_0000205189"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT CONFLICT 109
FT /note="L -> R (in Ref. 3; CAA33412/AAA42107)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> R (in Ref. 3; AAA42107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44950 MW; 7DD1ED8596C42219 CRC64;
MAACVKTNKS HVIFKKVSRD KSVTIYLGKR DYIDHVSQVE PVDGVVLVDP ELVKGKKVYV
TLTCAFRYGQ EDIDVIGLTF RRDLYFSRVQ VYPPVGAMSA PTQLQLSLLK KLGDNTYPFL
LTFPDYLPCS VMLQPAPQDV GKSCGVDFEV KAFATDITDA EEDKIPKKSS VRLLIRKVQH
APPEMGPQPC AEASWQFFMS DKPLHLSVSL SKEIYFHGEP IPVTVTVTNN TEKVVKKIKV
SVEQIANVVL YSSDYYVKPV ASEETQEKVQ PNSTLTKTLV LVPLLANNRE RRGIALDGKI
KHEDTNLASS TIIKEGIDRT VMGILVSYHI KVKLTVSGFL GELTSSEVAT EVPFRLMHPQ
PEDPAKESVQ DENLVFEEFA RQNLKDTGEN TEGKKDEDAG QDE
//
