ARRS_BOVIN
ID ARRS_BOVIN Reviewed; 404 AA.
AC P08168;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=S-arrestin;
DE AltName: Full=48 kDa protein;
DE AltName: Full=Retinal S-antigen {ECO:0000303|PubMed:3478675};
DE Short=S-AG;
DE AltName: Full=Rod photoreceptor arrestin;
DE Contains:
DE RecName: Full=S-arrestin short form;
GN Name=SAG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND ACETYLATION AT MET-1.
RC TISSUE=Retina;
RX PubMed=3478675; DOI=10.1073/pnas.84.20.6975;
RA Shinohara T., Dietzschold B., Craft C.M., Wistow G., Early J.J.,
RA Donoso L.A., Horwitz J., Tao R.;
RT "Primary and secondary structure of bovine retinal S antigen (48-kDa
RT protein).";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6975-6979(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Retina;
RX PubMed=2950857; DOI=10.1016/0006-291x(87)91499-9;
RA Yamaki K., Takahashi Y., Sakuragi S., Matsubara K.;
RT "Molecular cloning of the S-antigen cDNA from bovine retina.";
RL Biochem. Biophys. Res. Commun. 142:904-910(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), ALTERNATIVE SPLICING, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=7515057; DOI=10.1016/s0021-9258(17)40691-0;
RA Smith W.C., Milam A.H., Dugger D., Arendt A., Hargrave P.A., Palczewski K.;
RT "A splice variant of arrestin. Molecular cloning and localization in bovine
RT retina.";
RL J. Biol. Chem. 269:15407-15410(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-404 (ISOFORM A).
RX PubMed=3080338; DOI=10.1016/0014-5793(86)80207-1;
RA Wistow G.J., Katial A., Craft C.M., Shinohara T.;
RT "Sequence analysis of bovine retinal S-antigen. Relationships with alpha-
RT transducin and G-proteins.";
RL FEBS Lett. 196:23-28(1986).
RN [5]
RP PROTEIN SEQUENCE OF 1-12 AND 198-229.
RX PubMed=2910351; DOI=10.1016/0167-4838(89)90160-x;
RA Tsunasawa S., Shichi H.;
RT "The amino acid sequence of S-antigen: N-terminus and uveitogenic
RT peptides.";
RL Biochim. Biophys. Acta 994:191-193(1989).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE
RP SPLICING, IDENTIFICATION OF ISOFORM B, FUNCTION, INTERACTION WITH RHO,
RP SUBCELLULAR LOCATION (ISOFORM B), AND TISSUE SPECIFICITY.
RX PubMed=8003967; DOI=10.1002/pro.5560030215;
RA Palczewski K., Buczylko J., Ohguro H., Annan R.S., Carr S.A., Crabb J.W.,
RA Kaplan M.W., Johnson R.S., Walsh K.A.;
RT "Characterization of a truncated form of arrestin isolated from bovine rod
RT outer segments.";
RL Protein Sci. 3:314-324(1994).
RN [7]
RP SUBUNIT, AND MUTAGENESIS OF PHE-85 AND PHE-197.
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 [8] {ECO:0007744|PDB:1AYR}
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=9495348; DOI=10.1038/36147;
RA Granzin J., Wilden U., Choe H.W., Labahn J., Krafft B., Buldt G.;
RT "X-ray crystal structure of arrestin from bovine rod outer segments.";
RL Nature 391:918-921(1998).
RN [9] {ECO:0007744|PDB:1CF1}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), INTERACTION WITH RHO, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF ARG-175 AND ASP-296.
RX PubMed=10219246; DOI=10.1016/s0092-8674(00)80735-7;
RA Hirsch J.A., Schubert C., Gurevich V.V., Sigler P.B.;
RT "The 2.8 A crystal structure of visual arrestin: a model for arrestin's
RT regulation.";
RL Cell 97:257-269(1999).
RN [10] {ECO:0007744|PDB:3UGU, ECO:0007744|PDB:3UGX}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-369, AND DOMAIN.
RX PubMed=22306737; DOI=10.1016/j.jmb.2012.01.028;
RA Granzin J., Cousin A., Weirauch M., Schlesinger R., Buldt G.,
RA Batra-Safferling R.;
RT "Crystal structure of p44, a constitutively active splice variant of visual
RT arrestin.";
RL J. Mol. Biol. 416:611-618(2012).
RN [11] {ECO:0007744|PDB:4J2Q}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-369, DOMAIN, AND INTERACTION
RP WITH RHO.
RX PubMed=23604253; DOI=10.1038/nature12133;
RA Kim Y.J., Hofmann K.P., Ernst O.P., Scheerer P., Choe H.W., Sommer M.E.;
RT "Crystal structure of pre-activated arrestin p44.";
RL Nature 497:142-146(2013).
RN [12] {ECO:0007744|PDB:4PXF}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 67-77 IN COMPLEX WITH RHO, AND
RP FUNCTION.
RX PubMed=25205354; DOI=10.1038/ncomms5801;
RA Szczepek M., Beyriere F., Hofmann K.P., Elgeti M., Kazmin R., Rose A.,
RA Bartl F.J., von Stetten D., Heck M., Sommer M.E., Hildebrand P.W.,
RA Scheerer P.;
RT "Crystal structure of a common GPCR-binding interface for G protein and
RT arrestin.";
RL Nat. Commun. 5:4801-4801(2014).
RN [13] {ECO:0007744|PDB:4ZRG}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF MUTANT GLU-175, MUTAGENESIS OF
RP ARG-175, SUBUNIT, AND DOMAIN.
RX PubMed=26510463; DOI=10.1038/srep15808;
RA Granzin J., Stadler A., Cousin A., Schlesinger R., Batra-Safferling R.;
RT "Structural evidence for the role of polar core residue Arg175 in arrestin
RT activation.";
RL Sci. Rep. 5:15808-15808(2015).
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:8003967, PubMed:25205354). May play a role
CC in preventing light-dependent degeneration of retinal photoreceptor
CC cells (By similarity). {ECO:0000250|UniProtKB:P20443,
CC ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:8003967}.
CC -!- SUBUNIT: Monomer (PubMed:21288033). Homodimer (PubMed:21288033,
CC PubMed:10219246, PubMed:26510463). Homotetramer (PubMed:21288033,
CC PubMed:10219246). Self-association is cooperative (PubMed:21288033).
CC Isoform A and isoform B interact with RHO (via phosphorylated C-
CC terminus) (PubMed:8003967, PubMed:10219246, PubMed:23604253,
CC PubMed:25205354). {ECO:0000269|PubMed:10219246,
CC ECO:0000269|PubMed:21288033, ECO:0000269|PubMed:23604253,
CC ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26510463,
CC ECO:0000269|PubMed:8003967}.
CC -!- INTERACTION:
CC P08168-1; P02699: RHO; NbExp=23; IntAct=EBI-15575296, EBI-8592832;
CC P08168-1; P08168-1: SAG; NbExp=3; IntAct=EBI-15575296, EBI-15575296;
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:7515057}. 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 (PubMed:7515057). Evenly
CC distributed throughout rod photoreceptor cells in dark-adapted retina
CC (PubMed:7515057). Predominantly dectected at the proximal region of
CC photoreceptor outer segments, near disk membranes (By similarity).
CC {ECO:0000250|UniProtKB:P10523, ECO:0000269|PubMed:7515057}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:7515057,
CC ECO:0000269|PubMed:8003967}. Membrane {ECO:0000269|PubMed:8003967};
CC Peripheral membrane protein {ECO:0000269|PubMed:8003967}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P08168-1; Sequence=Displayed;
CC Name=B; Synonyms=p44;
CC IsoId=P08168-2; Sequence=VSP_000319, VSP_000320;
CC -!- TISSUE SPECIFICITY: Detected in retina, in rod photoreceptor cells (at
CC protein level) (PubMed:7515057, PubMed:8003967).
CC {ECO:0000269|PubMed:7515057, ECO:0000269|PubMed:8003967}.
CC -!- DOMAIN: The C-terminus of isoform A interferes with binding to non-
CC phosphorylated RHO. Interaction with phosphorylated RHO triggers
CC displacement of the C-terminus and leads to a conformation change that
CC mediates high-affinity RHO binding. Isoform B is C-terminally truncated
CC and is therefore already in the optimal conformation for RHO binding.
CC {ECO:0000269|PubMed:10219246, ECO:0000269|PubMed:22306737,
CC ECO:0000269|PubMed:23604253, ECO:0000269|PubMed:26510463}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; J02955; AAA30378.1; -; mRNA.
DR EMBL; M15115; AAA30377.1; -; mRNA.
DR EMBL; U08346; AAA20465.1; -; mRNA.
DR EMBL; X03454; CAA27179.1; -; mRNA.
DR PIR; B28404; A28404.
DR RefSeq; NP_851343.1; NM_181000.2. [P08168-2]
DR RefSeq; XP_010802144.1; XM_010803842.2. [P08168-1]
DR PDB; 1AYR; X-ray; 3.30 A; A/B/C/D=1-367.
DR PDB; 1CF1; X-ray; 2.80 A; A/B/C/D=2-404.
DR PDB; 3UGU; X-ray; 1.85 A; A=1-370.
DR PDB; 3UGX; X-ray; 2.65 A; A/B/C/D=1-404.
DR PDB; 4J2Q; X-ray; 3.00 A; A/B=1-369.
DR PDB; 4PXF; X-ray; 2.75 A; B=67-77.
DR PDB; 4ZRG; X-ray; 2.70 A; A=1-404.
DR PDB; 7F1W; X-ray; 3.10 A; A/B/C/D=1-404.
DR PDB; 7F1X; X-ray; 3.00 A; A/B/C/D=1-404.
DR PDB; 7JSM; X-ray; 2.50 A; A/B/C/D=1-404.
DR PDB; 7JTB; X-ray; 2.60 A; A/B/C/D=1-404.
DR PDB; 7JXA; X-ray; 2.40 A; A/B/C/D=1-404.
DR PDB; 7MOR; X-ray; 2.80 A; A/B/C/D=1-404.
DR PDB; 7MP0; X-ray; 2.60 A; A/B/C/D=1-404.
DR PDB; 7MP1; X-ray; 2.66 A; A/B/C/D=1-404.
DR PDB; 7MP2; X-ray; 3.00 A; A/B/C/D=1-404.
DR PDBsum; 1AYR; -.
DR PDBsum; 1CF1; -.
DR PDBsum; 3UGU; -.
DR PDBsum; 3UGX; -.
DR PDBsum; 4J2Q; -.
DR PDBsum; 4PXF; -.
DR PDBsum; 4ZRG; -.
DR PDBsum; 7F1W; -.
DR PDBsum; 7F1X; -.
DR PDBsum; 7JSM; -.
DR PDBsum; 7JTB; -.
DR PDBsum; 7JXA; -.
DR PDBsum; 7MOR; -.
DR PDBsum; 7MP0; -.
DR PDBsum; 7MP1; -.
DR PDBsum; 7MP2; -.
DR AlphaFoldDB; P08168; -.
DR BMRB; P08168; -.
DR SMR; P08168; -.
DR BioGRID; 158306; 1.
DR DIP; DIP-47525N; -.
DR IntAct; P08168; 3.
DR MINT; P08168; -.
DR STRING; 9913.ENSBTAP00000028633; -.
DR iPTMnet; P08168; -.
DR PaxDb; P08168; -.
DR Ensembl; ENSBTAT00000028633; ENSBTAP00000028633; ENSBTAG00000021480. [P08168-1]
DR GeneID; 280922; -.
DR KEGG; bta:280922; -.
DR CTD; 6295; -.
DR VEuPathDB; HostDB:ENSBTAG00000021480; -.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_1_1_1; -.
DR InParanoid; P08168; -.
DR OMA; GHYQDAN; -.
DR OrthoDB; 783081at2759; -.
DR TreeFam; TF314260; -.
DR EvolutionaryTrace; P08168; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021480; Expressed in retina and 68 other tissues.
DR ExpressionAtlas; P08168; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002046; F:opsin binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IDA: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..404
FT /note="S-arrestin"
FT /id="PRO_0000002309"
FT CHAIN 5..404
FT /note="S-arrestin short form"
FT /id="PRO_0000002311"
FT MOD_RES 1
FT /note="N-acetylmethionine; partial"
FT /evidence="ECO:0000269|PubMed:3478675"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15887"
FT VAR_SEQ 370
FT /note="F -> A (in isoform B)"
FT /evidence="ECO:0000305|PubMed:8003967"
FT /id="VSP_000319"
FT VAR_SEQ 371..404
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305|PubMed:8003967"
FT /id="VSP_000320"
FT MUTAGEN 85
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-197."
FT /evidence="ECO:0000269|PubMed:21288033"
FT MUTAGEN 175
FT /note="R->E: Strongly increases affinity for RHO by
FT breaking the interaction with D-296. Abolishes
FT oligomerization. No effect on affinity for RHO; when
FT associated with R-296."
FT /evidence="ECO:0000269|PubMed:10219246,
FT ECO:0000269|PubMed:26510463"
FT MUTAGEN 197
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-85."
FT /evidence="ECO:0000269|PubMed:21288033"
FT MUTAGEN 296
FT /note="D->R: Strongly increases affinity for RHO by
FT breaking the interaction with R-175. No effect on affinity
FT for RHO; when associated with E-175."
FT /evidence="ECO:0000269|PubMed:10219246"
FT CONFLICT 35
FT /note="V -> L (in Ref. 2; AAA30377)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> V (in Ref. 2; AAA30377)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> I (in Ref. 2; AAA30377)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="D -> H (in Ref. 2; AAA30377)"
FT /evidence="ECO:0000305"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1AYR"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3UGU"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 56..67
FT /evidence="ECO:0007829|PDB:3UGU"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4PXF"
FT STRAND 79..92
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1CF1"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 143..155
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3UGU"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 169..179
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 234..247
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:3UGU"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:7JXA"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:7JXA"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 322..335
FT /evidence="ECO:0007829|PDB:3UGU"
FT TURN 336..341
FT /evidence="ECO:0007829|PDB:7JXA"
FT STRAND 345..357
FT /evidence="ECO:0007829|PDB:3UGU"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:7JXA"
SQ SEQUENCE 404 AA; 45275 MW; 26B1D80B652AF1EF CRC64;
MKANKPAPNH VIFKKISRDK SVTIYLGKRD YIDHVERVEP VDGVVLVDPE LVKGKRVYVS
LTCAFRYGQE DIDVMGLSFR RDLYFSQVQV FPPVGASGAT TRLQESLIKK LGANTYPFLL
TFPDYLPCSV MLQPAPQDVG KSCGVDFEIK AFATHSTDVE EDKIPKKSSV RLLIRKVQHA
PRDMGPQPRA EASWQFFMSD KPLRLAVSLS KEIYYHGEPI PVTVAVTNST EKTVKKIKVL
VEQVTNVVLY SSDYYIKTVA AEEAQEKVPP NSSLTKTLTL VPLLANNRER RGIALDGKIK
HEDTNLASST IIKEGIDKTV MGILVSYQIK VKLTVSGLLG ELTSSEVATE VPFRLMHPQP
EDPDTAKESF QDENFVFEEF ARQNLKDAGE YKEEKTDQEA AMDE
