ID   ARRS_PIG                Reviewed;         405 AA.
AC   P79260;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 91.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=8690040; DOI=10.1006/exer.1996.0036;
RA   Singh A.K., Kumar G., Shinohara T., Shichi H.;
RT   "Porcine S-antigen: cDNA sequence and expression in retina, ciliary
RT   epithelium and iris.";
RL   Exp. Eye Res. 62:299-308(1996).
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 pigment epithelium.
CC       {ECO:0000269|PubMed:8690040}.
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; S82664; AAB46757.2; -; mRNA.
DR   RefSeq; NP_999244.1; NM_214079.1.
DR   AlphaFoldDB; P79260; -.
DR   SMR; P79260; -.
DR   STRING; 9823.ENSSSCP00000017271; -.
DR   PaxDb; P79260; -.
DR   PeptideAtlas; P79260; -.
DR   GeneID; 397151; -.
DR   KEGG; ssc:397151; -.
DR   CTD; 6295; -.
DR   eggNOG; KOG3865; Eukaryota.
DR   InParanoid; P79260; -.
DR   OrthoDB; 783081at2759; -.
DR   ChiTaRS; SAG; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central.
DR   GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cell projection; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..405
FT                   /note="S-arrestin"
FT                   /id="PRO_0000205188"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15887"
SQ   SEQUENCE   405 AA;  45103 MW;  F9C0C8658CBFA73E CRC64;
     MAANVQASKS TPNHVIFKKT SRDKSVTIYL GKRDYIDHVD QVEPVDGVVL VDPELVKGKR
     VYVSLTCAFR YGQEDIDVIG LSFRRDLYFS QVQVFPPVGA ASQTKLQESL IKKLGGHTYP
     FLLTFPDYLP CSVMLQPAPQ DVGKCCGVDF EVKAFATDSA DTGEDKIPKK SSVRLLIRKV
     QHAPLEMGPQ PHAEAAWQFF MSDKPLHLTV SLSKELYYHG EPIPVTVTVT NNTEKTVKKI
     KALVEQVANV VLYSSDYYIK PVATEETQQK VPPNSTLTTT LTLVPLLANN RERRGIADGK
     IKHEDTNLAS STIIKEGMDK TIMGILVSYQ IKVQLTVSGL LGELTSSEVA TEVPFRLMHP
     QPEDPEAMDS FQDENFVFEE FARQNLKDAG ELKEEKTDQE AAAHE