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Protein

S-arrestin

Gene

SAG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • protein phosphatase inhibitor activity Source: ProtInc

GO - Biological processi

  • cell surface receptor signaling pathway Source: ProtInc
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • rhodopsin mediated signaling pathway Source: ProtInc
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000130561-MONOMER.
ReactomeiR-HSA-2485179. Activation of the phototransduction cascade.
R-HSA-2514859. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10521. SAG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Night blindness, congenital stationary, Oguchi type 1 (CSNBO1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:258100
Retinitis pigmentosa 47 (RP47)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613758

Keywords - Diseasei

Autoimmune uveitis, Congenital stationary night blindness, Retinitis pigmentosa

Organism-specific databases

DisGeNETi6295.
MalaCardsiSAG.
MIMi258100. phenotype.
613758. phenotype.
OpenTargetsiENSG00000130561.
ENSG00000281857.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
791. Retinitis pigmentosa.
PharmGKBiPA34929.

Polymorphism and mutation databases

BioMutaiSAG.
DMDMi109940055.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051861 – 405S-arrestinAdd BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi132 ↔ 147Curated
Modified residuei234PhosphothreonineBy similarity1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP10523.
PeptideAtlasiP10523.
PRIDEiP10523.

PTM databases

iPTMnetiP10523.
PhosphoSitePlusiP10523.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

BgeeiENSG00000130561.
CleanExiHS_SAG.
ExpressionAtlasiP10523. baseline and differential.
GenevisibleiP10523. HS.

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi112202. 4 interactors.
IntActiP10523. 2 interactors.
STRINGi9606.ENSP00000386444.

Structurei

3D structure databases

ProteinModelPortaliP10523.
SMRiP10523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP10523.
KOiK19627.
OMAiKEIYFHG.
OrthoDBiEOG091G05M2.
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

        10         20         30         40         50
MAASGKTSKS EPNHVIFKKI SRDKSVTIYL GNRDYIDHVS QVQPVDGVVL
60 70 80 90 100
VDPDLVKGKK VYVTLTCAFR YGQEDIDVIG LTFRRDLYFS RVQVYPPVGA
110 120 130 140 150
ASTPTKLQES LLKKLGSNTY PFLLTFPDYL PCSVMLQPAP QDSGKSCGVD
160 170 180 190 200
FEVKAFATDS TDAEEDKIPK KSSVRLLIRK VQHAPLEMGP QPRAEAAWQF
210 220 230 240 250
FMSDKPLHLA VSLNKEIYFH GEPIPVTVTV TNNTEKTVKK IKAFVEQVAN
260 270 280 290 300
VVLYSSDYYV KPVAMEEAQE KVPPNSTLTK TLTLLPLLAN NRERRGIALD
310 320 330 340 350
GKIKHEDTNL ASSTIIKEGI DRTVLGILVS YQIKVKLTVS GFLGELTSSE
360 370 380 390 400
VATEVPFRLM HPQPEDPAKE SYQDANLVFE EFARHNLKDA GEAEEGKRDK

NDVDE
Length:405
Mass (Da):45,120
Last modified:June 27, 2006 - v3
Checksum:iCBBF65845A5F891E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti176L → Y in CAA30984 (PubMed:3164688).Curated1
Sequence conflicti180K → S in CAA30984 (PubMed:3164688).Curated1
Sequence conflicti197A → T in CAA30984 (PubMed:3164688).Curated1
Sequence conflicti215K → R in CAA30984 (PubMed:3164688).Curated1
Sequence conflicti244F → C in CAA30984 (PubMed:3164688).Curated1
Sequence conflicti372Y → I in CAA30984 (PubMed:3164688).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00826376I → V.2 PublicationsCorresponds to variant rs7565275dbSNPEnsembl.1
Natural variantiVAR_00826484R → C.1 PublicationCorresponds to variant rs115857633dbSNPEnsembl.1
Natural variantiVAR_008265125T → M.1 PublicationCorresponds to variant rs137886124dbSNPEnsembl.1
Natural variantiVAR_008266364P → L.1 PublicationCorresponds to variant rs112613526dbSNPEnsembl.1
Natural variantiVAR_008267378V → I.1 PublicationCorresponds to variant rs200602069dbSNPEnsembl.1
Natural variantiVAR_008268384R → C.1 Publication1
Natural variantiVAR_048333403V → A.2 PublicationsCorresponds to variant rs1046976dbSNPEnsembl.1
Natural variantiVAR_033524403V → I.Corresponds to variant rs1046974dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.32721.

Genome annotation databases

EnsembliENST00000409110; ENSP00000386444; ENSG00000130561.
ENST00000631149; ENSP00000486571; ENSG00000281857.
GeneIDi6295.
KEGGihsa:6295.
UCSCiuc002vuh.3. human.

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:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.32721.

3D structure databases

ProteinModelPortaliP10523.
SMRiP10523.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112202. 4 interactors.
IntActiP10523. 2 interactors.
STRINGi9606.ENSP00000386444.

PTM databases

iPTMnetiP10523.
PhosphoSitePlusiP10523.

Polymorphism and mutation databases

BioMutaiSAG.
DMDMi109940055.

Proteomic databases

PaxDbiP10523.
PeptideAtlasiP10523.
PRIDEiP10523.

Protocols and materials databases

DNASUi6295.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000409110; ENSP00000386444; ENSG00000130561.
ENST00000631149; ENSP00000486571; ENSG00000281857.
GeneIDi6295.
KEGGihsa:6295.
UCSCiuc002vuh.3. human.

Organism-specific databases

CTDi6295.
DisGeNETi6295.
GeneCardsiSAG.
GeneReviewsiSAG.
HGNCiHGNC:10521. SAG.
MalaCardsiSAG.
MIMi181031. gene.
258100. phenotype.
613758. phenotype.
neXtProtiNX_P10523.
OpenTargetsiENSG00000130561.
ENSG00000281857.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
791. Retinitis pigmentosa.
PharmGKBiPA34929.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP10523.
KOiK19627.
OMAiKEIYFHG.
OrthoDBiEOG091G05M2.
PhylomeDBiP10523.
TreeFamiTF314260.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000130561-MONOMER.
ReactomeiR-HSA-2485179. Activation of the phototransduction cascade.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiP10523.

Miscellaneous databases

ChiTaRSiSAG. human.
GeneWikiiSAG_(gene).
GenomeRNAii6295.
PROiP10523.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000130561.
CleanExiHS_SAG.
ExpressionAtlasiP10523. baseline and differential.
GenevisibleiP10523. HS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.