ID   ARRS_XENLA              Reviewed;         396 AA.
AC   P51477; Q6DJE8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=S-arrestin;
DE   AltName: Full=Retinal S-antigen;
DE            Short=S-AG;
DE   AltName: Full=Rod photoreceptor arrestin;
GN   Name=sag;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Sundareswaran S., Knox B.E.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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: Interacts with RHO (via the phosphorylated C-terminus).
CC       {ECO:0000250|UniProtKB:P08168}.
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}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; U41623; AAB88584.1; -; mRNA.
DR   EMBL; BC075231; AAH75231.1; -; mRNA.
DR   RefSeq; NP_001081898.1; NM_001088429.1.
DR   AlphaFoldDB; P51477; -.
DR   SMR; P51477; -.
DR   DNASU; 398109; -.
DR   GeneID; 398109; -.
DR   KEGG; xla:398109; -.
DR   CTD; 398109; -.
DR   Xenbase; XB-GENE-17335209; sag.L.
DR   OMA; GHYQDAN; -.
DR   OrthoDB; 783081at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
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   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; Reference proteome; Sensory transduction;
KW   Vision.
FT   CHAIN           1..396
FT                   /note="S-arrestin"
FT                   /id="PRO_0000205192"
FT   REGION          375..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  44624 MW;  3408A65280CE7C14 CRC64;
     MSGEKKSRHV MYKKTSRDKA VSVYLGKRDY VDHVDSVEPV DGVVLVDPDL LKGKKVYVTL
     TCAFRYGQED IDVIGLTFRK DLYYARTQIY PPVEDPKALT KVQERLMKKL GNNAFPFVLE
     FPDFLPCSVS LQPAPSDVGK ACGVDFEIKA FSTNNLEDRI HKKNSVRLMI RKIQYAPDQP
     GPKPRAETSW QFFMSDKPLH LTASLSKEVF YHGEPITVSV SVTNKSDKTV KKISASVEQV
     SNVVLYSSDY YIKTVALEES NEKVPSKASY NHTFSLLPLL AYNREKREIA LDGKLKHEDT
     NLASSTLLKE GTDRTVMGIL VDYKIKVTLT VSGLLGDMTS SEVSTELPFI LMHPNPDGGA
     KESEQEDDMV FEEFARDPLK GELQAEEKEE EEDDEK