ARRS_MOUSE
ID ARRS_MOUSE Reviewed; 403 AA.
AC P20443; Q91W62;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 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].
RX PubMed=2977355; DOI=10.1016/0378-1119(88)90308-3;
RA Tsuda M., Syed M., Bugra K., Whelan J.P., McGinnis J.F., Shinohara T.;
RT "Structural analysis of mouse S-antigen.";
RL Gene 73:11-20(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9333241; DOI=10.1038/39068;
RA Xu J., Dodd R.L., Makino C.L., Simon M.I., Baylor D.A., Chen J.;
RT "Prolonged photoresponses in transgenic mouse rods lacking arrestin.";
RL Nature 389:505-509(1997).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16421323; DOI=10.1523/jneurosci.3301-05.2006;
RA Burns M.E., Mendez A., Chen C.K., Almuete A., Quillinan N., Simon M.I.,
RA Baylor D.A., Chen J.;
RT "Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin
RT splice variants.";
RL J. Neurosci. 26:1036-1044(2006).
RN [5]
RP SUBUNIT, AND MUTAGENESIS OF PHE-86; PHE-198 AND ALA-349.
RX PubMed=21288033; DOI=10.1021/bi1018607;
RA Kim M., Hanson S.M., Vishnivetskiy S.A., Song X., Cleghorn W.M.,
RA Hubbell W.L., Gurevich V.V.;
RT "Robust self-association is a common feature of mammalian visual arrestin-
RT 1.";
RL Biochemistry 50:2235-2242(2011).
RN [6] {ECO:0007744|PDB:4ZWJ}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 10-392 IN COMPLEX WITH RHO, AND
RP MUTAGENESIS OF 374-LEU--PHE-376.
RX PubMed=26200343; DOI=10.1038/nature14656;
RA Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A.,
RA White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H.,
RA Zhang C., Moeller A., West G.M., Pascal B.D., Van Eps N., Caro L.N.,
RA Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J.,
RA Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A.,
RA Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H.,
RA Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H.,
RA Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J.,
RA Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H.,
RA Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P.,
RA Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C.,
RA Cherezov V., Melcher K., Xu H.E.;
RT "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray
RT laser.";
RL Nature 523:561-567(2015).
RN [7] {ECO:0007744|PDB:5W0P}
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 10-392 IN COMPLEX WITH RHO.
RX PubMed=28753425; DOI=10.1016/j.cell.2017.07.002;
RA Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y.,
RA Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N.,
RA Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V.,
RA Griffin P.R., Ernst O.P., Melcher K., Xu H.E.;
RT "Identification of Phosphorylation Codes for Arrestin Recruitment by G
RT Protein-Coupled Receptors.";
RL Cell 170:457-469(2017).
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 (PubMed:9333241, PubMed:16421323). May play a role
CC in preventing light-dependent degeneration of retinal photoreceptor
CC cells (PubMed:16421323). {ECO:0000269|PubMed:16421323,
CC ECO:0000269|PubMed:9333241}.
CC -!- SUBUNIT: Monomer. Homodimer. Homotetramer (PubMed:21288033). Interacts
CC with RHO (via the phosphorylated C-terminus) (PubMed:26200343,
CC PubMed:28753425). {ECO:0000269|PubMed:21288033,
CC ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC segment {ECO:0000269|PubMed:16421323}. Membrane
CC {ECO:0000269|PubMed:16421323}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16421323}. 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: Detected in retina (at protein level).
CC {ECO:0000269|PubMed:16421323, ECO:0000269|PubMed:9333241}.
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 -!- DISRUPTION PHENOTYPE: The morphology of the retina is not affected when
CC mice are kept in constant darkness. When mice are exposed to
CC alternating 12 hour light and dark cycles, the rod photoreceptor outer
CC segments are about 25% shorter than in wild-type, and the photoreceptor
CC outer segments appear somewhat disordered (PubMed:9333241). After one
CC year exposure to alternating 12 hour light and dark cycles, there are
CC clear signs of photoreceptor degeneration with about 50% reduction in
CC the number of photoreceptor nuclei in the outer layer of the retina
CC (PubMed:16421323). Rod photoreceptor cells show normal flash
CC sensitivity, but display prolonged RHO signaling, due to a strongly
CC decreased rate of deactivation (PubMed:9333241, PubMed:16421323).
CC {ECO:0000269|PubMed:16421323, ECO:0000269|PubMed:9333241}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; M24086; AAA40090.1; -; mRNA.
DR EMBL; BC016498; AAH16498.1; -; mRNA.
DR CCDS; CCDS35656.1; -.
DR PIR; JS0066; JS0066.
DR RefSeq; NP_033144.1; NM_009118.2.
DR PDB; 4ZWJ; X-ray; 3.30 A; A/B/C/D=10-392.
DR PDB; 5DGY; X-ray; 7.70 A; A/B/C/D=10-392.
DR PDB; 5W0P; X-ray; 3.01 A; A/B/C/D=10-392.
DR PDBsum; 4ZWJ; -.
DR PDBsum; 5DGY; -.
DR PDBsum; 5W0P; -.
DR AlphaFoldDB; P20443; -.
DR SMR; P20443; -.
DR BioGRID; 203065; 1.
DR IntAct; P20443; 1.
DR STRING; 10090.ENSMUSP00000076948; -.
DR iPTMnet; P20443; -.
DR PhosphoSitePlus; P20443; -.
DR PaxDb; P20443; -.
DR PRIDE; P20443; -.
DR ProteomicsDB; 281805; -.
DR Antibodypedia; 11899; 271 antibodies from 24 providers.
DR DNASU; 20215; -.
DR Ensembl; ENSMUST00000077772; ENSMUSP00000076948; ENSMUSG00000056055.
DR GeneID; 20215; -.
DR KEGG; mmu:20215; -.
DR UCSC; uc007bxp.1; mouse.
DR CTD; 6295; -.
DR MGI; MGI:98227; Sag.
DR VEuPathDB; HostDB:ENSMUSG00000056055; -.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_0_0_1; -.
DR InParanoid; P20443; -.
DR OMA; GHYQDAN; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; P20443; -.
DR TreeFam; TF314260; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 20215; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sag; mouse.
DR PRO; PR:P20443; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P20443; protein.
DR Bgee; ENSMUSG00000056055; Expressed in retinal neural layer and 53 other tissues.
DR ExpressionAtlas; P20443; baseline and differential.
DR Genevisible; P20443; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; 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:0030507; F:spectrin binding; ISO: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; 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 1: Evidence at protein level;
KW 3D-structure; Cell projection; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..403
FT /note="S-arrestin"
FT /id="PRO_0000205187"
FT REGION 11..19
FT /note="Interaction with RHO"
FT /evidence="ECO:0000269|PubMed:28753425"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15887"
FT MUTAGEN 86
FT /note="F->A: Abrogates tetramerization, reduces
FT dimerization, does not affect binding to microtubules and
FT to phosphorylated light-activated rhodopsin; when
FT associated with A-198, or with A-198 and V-349."
FT /evidence="ECO:0000269|PubMed:21288033"
FT MUTAGEN 198
FT /note="F->A: Abrogates tetramerization, reduces
FT dimerization, does not affect binding to microtubules and
FT to phosphorylated light-activated rhodopsin; when
FT associated with A-86, or with A-86 and V-349."
FT /evidence="ECO:0000269|PubMed:21288033"
FT MUTAGEN 349
FT /note="A->V: Abrogates tetramerization, reduces
FT dimerization, does not affect binding to microtubules and
FT to phosphorylated light-activated rhodopsin; when
FT associated with A-86 and A-198."
FT /evidence="ECO:0000269|PubMed:21288033"
FT MUTAGEN 374..376
FT /note="LVF->AAA: Strongly increases affinity for RHO."
FT /evidence="ECO:0000269|PubMed:26200343"
FT CONFLICT 391
FT /note="T -> P (in Ref. 2; AAH16498)"
FT /evidence="ECO:0000305"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 19..28
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 57..69
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 144..157
FT /evidence="ECO:0007829|PDB:5W0P"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:4ZWJ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 235..265
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:5W0P"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 323..337
FT /evidence="ECO:0007829|PDB:5W0P"
FT STRAND 345..358
FT /evidence="ECO:0007829|PDB:5W0P"
SQ SEQUENCE 403 AA; 44930 MW; 2D4CFEAF81C5FC6D CRC64;
MAACGKTNKS HVIFKKVSRD KSVTIYLGKR DYVDHVSQVE PVDGVVLVDP ELVKGKKVYV
TLTCAFRYGQ EDIDVMGLTF RRDLYFSRVQ VYPPVGAMSV LTQLQESLLK KLGDNTYPFL
LTFPDYLPCS VMLQPAPQDV GKSCGVDFEV KAFASDITDP EEDKIPKKSS VRLLIRKVQH
APPEMGPQPS AEASWQFFMS DKPLNLSVSL SKEIYFHGEP IPVTVTVTNN TDKVVKKIKV
SVEQIANVVL YSSDYYVKPV ASEETQEKVQ PNSTLTKTLV LVPLLANNRE RRGIALDGKI
KHEDTNLASS TIIKEGIDRT VMGILVSYHI KVKLTVSGFL GELTSSEVAT EVPFRLMHPQ
PEDPAKESVQ DENLVFEEFA RQNLKDTGEN TEGKKDEDAG QDE
