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P10523

- ARRS_HUMAN

UniProt

P10523 - ARRS_HUMAN

Protein

S-arrestin

Gene

SAG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (27 Jun 2006)
      Previous versions | rss
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    Functioni

    Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase.

    GO - Molecular functioni

    1. protein phosphatase inhibitor activity Source: ProtInc

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. negative regulation of catalytic activity Source: GOC
    3. phototransduction, visible light Source: Reactome
    4. regulation of rhodopsin mediated signaling pathway Source: Reactome
    5. rhodopsin mediated signaling pathway Source: Reactome
    6. visual perception Source: UniProtKB-KW

    Keywords - Biological processi

    Sensory transduction, Vision

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    SignaLinkiP10523.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-arrestin
    Alternative name(s):
    48 kDa protein
    Retinal S-antigen
    Short name:
    S-AG
    Rod photoreceptor arrestin
    Gene namesi
    Name:SAG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10521. SAG.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Night blindness, congenital stationary, Oguchi type 1 (CSNBO1) [MIM:258100]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Congenital stationary night blindness Oguchi type is an autosomal recessive form associated with fundus discoloration and abnormally slow dark adaptation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Retinitis pigmentosa 47 (RP47) [MIM:613758]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Autoimmune uveitis, Congenital stationary night blindness, Retinitis pigmentosa

    Organism-specific databases

    MIMi258100. phenotype.
    613758. phenotype.
    Orphaneti215. Congenital stationary night blindness.
    75382. Oguchi disease.
    791. Retinitis pigmentosa.
    PharmGKBiPA34929.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405S-arrestinPRO_0000205186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi132 ↔ 147Curated
    Modified residuei234 – 2341PhosphothreonineBy similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiP10523.
    PRIDEiP10523.

    PTM databases

    PhosphoSiteiP10523.

    Expressioni

    Tissue specificityi

    Retina and pineal gland.

    Gene expression databases

    ArrayExpressiP10523.
    BgeeiP10523.
    CleanExiHS_SAG.
    GenevestigatoriP10523.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi112202. 3 interactions.
    IntActiP10523. 2 interactions.
    STRINGi9606.ENSP00000386444.

    Structurei

    3D structure databases

    ProteinModelPortaliP10523.
    SMRiP10523. Positions 14-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arrestin family.Curated

    Phylogenomic databases

    eggNOGiNOG330592.
    HOGENOMiHOG000231319.
    HOVERGENiHBG002399.
    InParanoidiP10523.
    OMAiKEIYFHG.
    PhylomeDBiP10523.
    TreeFamiTF314260.

    Family and domain databases

    Gene3Di2.60.40.640. 1 hit.
    2.60.40.840. 1 hit.
    InterProiIPR000698. Arrestin.
    IPR011021. Arrestin-like_N.
    IPR014752. Arrestin_C.
    IPR011022. Arrestin_C-like.
    IPR017864. Arrestin_CS.
    IPR014753. Arrestin_N.
    IPR014756. Ig_E-set.
    [Graphical view]
    PANTHERiPTHR11792. PTHR11792. 1 hit.
    PfamiPF02752. Arrestin_C. 1 hit.
    PF00339. Arrestin_N. 1 hit.
    [Graphical view]
    PRINTSiPR00309. ARRESTIN.
    SMARTiSM01017. Arrestin_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF81296. SSF81296. 2 hits.
    PROSITEiPS00295. ARRESTINS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGKTSKS EPNHVIFKKI SRDKSVTIYL GNRDYIDHVS QVQPVDGVVL    50
    VDPDLVKGKK VYVTLTCAFR YGQEDIDVIG LTFRRDLYFS RVQVYPPVGA 100
    ASTPTKLQES LLKKLGSNTY PFLLTFPDYL PCSVMLQPAP QDSGKSCGVD 150
    FEVKAFATDS TDAEEDKIPK KSSVRLLIRK VQHAPLEMGP QPRAEAAWQF 200
    FMSDKPLHLA VSLNKEIYFH GEPIPVTVTV TNNTEKTVKK IKAFVEQVAN 250
    VVLYSSDYYV KPVAMEEAQE KVPPNSTLTK TLTLLPLLAN NRERRGIALD 300
    GKIKHEDTNL ASSTIIKEGI DRTVLGILVS YQIKVKLTVS GFLGELTSSE 350
    VATEVPFRLM HPQPEDPAKE SYQDANLVFE EFARHNLKDA GEAEEGKRDK 400
    NDVDE 405
    Length:405
    Mass (Da):45,120
    Last modified:June 27, 2006 - v3
    Checksum:iCBBF65845A5F891E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761L → Y in CAA30984. (PubMed:3164688)Curated
    Sequence conflicti180 – 1801K → S in CAA30984. (PubMed:3164688)Curated
    Sequence conflicti197 – 1971A → T in CAA30984. (PubMed:3164688)Curated
    Sequence conflicti215 – 2151K → R in CAA30984. (PubMed:3164688)Curated
    Sequence conflicti244 – 2441F → C in CAA30984. (PubMed:3164688)Curated
    Sequence conflicti372 – 3721Y → I in CAA30984. (PubMed:3164688)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761I → V.2 Publications
    Corresponds to variant rs7565275 [ dbSNP | Ensembl ].
    VAR_008263
    Natural varianti84 – 841R → C.1 Publication
    Corresponds to variant rs115857633 [ dbSNP | Ensembl ].
    VAR_008264
    Natural varianti125 – 1251T → M.1 Publication
    Corresponds to variant rs137886124 [ dbSNP | Ensembl ].
    VAR_008265
    Natural varianti364 – 3641P → L.1 Publication
    Corresponds to variant rs112613526 [ dbSNP | Ensembl ].
    VAR_008266
    Natural varianti378 – 3781V → I.1 Publication
    Corresponds to variant rs200602069 [ dbSNP | Ensembl ].
    VAR_008267
    Natural varianti384 – 3841R → C.1 Publication
    VAR_008268
    Natural varianti403 – 4031V → A.2 Publications
    Corresponds to variant rs1046976 [ dbSNP | Ensembl ].
    VAR_048333
    Natural varianti403 – 4031V → I.
    Corresponds to variant rs1046974 [ dbSNP | Ensembl ].
    VAR_033524

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12453 mRNA. Translation: CAA30984.1.
    U70976
    , U70962, U70963, U70964, U70965, U70966, U70967, U70968, U70969, U70970, U70971, U70972, U70973, U70974, U70975 Genomic DNA. Translation: AAC50992.1.
    AC013726 Genomic DNA. Translation: AAY14861.1.
    DQ980620 mRNA. Translation: ABJ97141.1.
    CCDSiCCDS46545.1.
    PIRiA30357.
    RefSeqiNP_000532.2. NM_000541.4.
    XP_005246156.1. XM_005246099.1.
    UniGeneiHs.32721.

    Genome annotation databases

    EnsembliENST00000409110; ENSP00000386444; ENSG00000130561.
    GeneIDi6295.
    KEGGihsa:6295.
    UCSCiuc002vuh.2. human.

    Polymorphism databases

    DMDMi109940055.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Mutations of the SAG gene

    Retina International's Scientific Newsletter

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12453 mRNA. Translation: CAA30984.1 .
    U70976
    , U70962 , U70963 , U70964 , U70965 , U70966 , U70967 , U70968 , U70969 , U70970 , U70971 , U70972 , U70973 , U70974 , U70975 Genomic DNA. Translation: AAC50992.1 .
    AC013726 Genomic DNA. Translation: AAY14861.1 .
    DQ980620 mRNA. Translation: ABJ97141.1 .
    CCDSi CCDS46545.1.
    PIRi A30357.
    RefSeqi NP_000532.2. NM_000541.4.
    XP_005246156.1. XM_005246099.1.
    UniGenei Hs.32721.

    3D structure databases

    ProteinModelPortali P10523.
    SMRi P10523. Positions 14-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112202. 3 interactions.
    IntActi P10523. 2 interactions.
    STRINGi 9606.ENSP00000386444.

    PTM databases

    PhosphoSitei P10523.

    Polymorphism databases

    DMDMi 109940055.

    Proteomic databases

    PaxDbi P10523.
    PRIDEi P10523.

    Protocols and materials databases

    DNASUi 6295.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000409110 ; ENSP00000386444 ; ENSG00000130561 .
    GeneIDi 6295.
    KEGGi hsa:6295.
    UCSCi uc002vuh.2. human.

    Organism-specific databases

    CTDi 6295.
    GeneCardsi GC02P234247.
    GeneReviewsi SAG.
    HGNCi HGNC:10521. SAG.
    MIMi 181031. gene.
    258100. phenotype.
    613758. phenotype.
    neXtProti NX_P10523.
    Orphaneti 215. Congenital stationary night blindness.
    75382. Oguchi disease.
    791. Retinitis pigmentosa.
    PharmGKBi PA34929.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG330592.
    HOGENOMi HOG000231319.
    HOVERGENi HBG002399.
    InParanoidi P10523.
    OMAi KEIYFHG.
    PhylomeDBi P10523.
    TreeFami TF314260.

    Enzyme and pathway databases

    Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
    SignaLinki P10523.

    Miscellaneous databases

    GeneWikii SAG_(gene).
    GenomeRNAii 6295.
    NextBioi 24439.
    PROi P10523.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10523.
    Bgeei P10523.
    CleanExi HS_SAG.
    Genevestigatori P10523.

    Family and domain databases

    Gene3Di 2.60.40.640. 1 hit.
    2.60.40.840. 1 hit.
    InterProi IPR000698. Arrestin.
    IPR011021. Arrestin-like_N.
    IPR014752. Arrestin_C.
    IPR011022. Arrestin_C-like.
    IPR017864. Arrestin_CS.
    IPR014753. Arrestin_N.
    IPR014756. Ig_E-set.
    [Graphical view ]
    PANTHERi PTHR11792. PTHR11792. 1 hit.
    Pfami PF02752. Arrestin_C. 1 hit.
    PF00339. Arrestin_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00309. ARRESTIN.
    SMARTi SM01017. Arrestin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 2 hits.
    PROSITEi PS00295. ARRESTINS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of human retinal S-antigen reveals similarities with alpha-transducin."
      Yamaki K., Tsuda M., Shinohara T.
      FEBS Lett. 234:39-43(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-403.
      Tissue: Retina.
    2. Erratum
      Yamaki K., Tsuda M., Shinohara T.
      FEBS Lett. 236:507-507(1988)
    3. "Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness."
      Yamamoto S., Sippel K.C., Berson E.L., Dryja T.P.
      Nat. Genet. 15:175-178(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-403.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Mapping of transcription start sites of human retina expressed genes."
      Roni V., Carpio R., Wissinger B.
      BMC Genomics 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133.
      Tissue: Retina.
    6. "A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese."
      Fuchs S., Nakazawa M., Maw M., Tamai M., Oguchi Y., Gal A.
      Nat. Genet. 10:360-362(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CSNBO1, VARIANT VAL-76.
    7. "Arrestin gene mutations in autosomal recessive retinitis pigmentosa."
      Nakazawa M., Wada Y., Tamai M.
      Arch. Ophthalmol. 116:498-501(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RP47.
    8. "Robust self-association is a common feature of mammalian visual arrestin-1."
      Kim M., Hanson S.M., Vishnivetskiy S.A., Song X., Cleghorn W.M., Hubbell W.L., Gurevich V.V.
      Biochemistry 50:2235-2242(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "Evaluation of the human arrestin gene in patients with retinitis pigmentosa and stationary night blindness."
      Sippel K.C., DeStefano J.D., Berson E.L., Dryja T.P.
      Invest. Ophthalmol. Vis. Sci. 39:665-670(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-76; CYS-84; MET-125; LEU-364; ILE-378 AND CYS-384.

    Entry informationi

    Entry nameiARRS_HUMAN
    AccessioniPrimary (citable) accession number: P10523
    Secondary accession number(s): A0FDN6, Q53SV3, Q99858
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: June 27, 2006
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Arrestin binds calcium.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3