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Protein

S-arrestin

Gene

Sag

Organism
Mus musculus (Mouse)
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

  • opsin binding Source: MGI
  • phosphoprotein binding Source: MGI
  • spectrin binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_326042. Activation of the phototransduction cascade.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:98227. Sag.

Subcellular locationi

GO - Cellular componenti

  • photoreceptor inner segment Source: MGI
  • photoreceptor outer segment Source: MGI
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

S-antigen induces autoimmune uveitis.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-198, or with A-198 and V-349. 1 Publication
Mutagenesisi198 – 1981F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-86, or with A-86 and V-349. 1 Publication
Mutagenesisi349 – 3491A → V: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-86 and A-198. 1 Publication

Keywords - Diseasei

Autoimmune uveitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403S-arrestinPRO_0000205187Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi129 ↔ 144Curated
Modified residuei231 – 2311PhosphothreonineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP20443.
PRIDEiP20443.

PTM databases

PhosphoSiteiP20443.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

BgeeiP20443.
CleanExiMM_SAG.
ExpressionAtlasiP20443. baseline and differential.
GenevestigatoriP20443.

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi203065. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP20443.
SMRiP20443. Positions 11-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiNOG330592.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP20443.
OMAiKEIYFHG.
OrthoDBiEOG79W954.
PhylomeDBiP20443.
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.

P20443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAACGKTNKS HVIFKKVSRD KSVTIYLGKR DYVDHVSQVE PVDGVVLVDP
60 70 80 90 100
ELVKGKKVYV TLTCAFRYGQ EDIDVMGLTF RRDLYFSRVQ VYPPVGAMSV
110 120 130 140 150
LTQLQESLLK KLGDNTYPFL LTFPDYLPCS VMLQPAPQDV GKSCGVDFEV
160 170 180 190 200
KAFASDITDP EEDKIPKKSS VRLLIRKVQH APPEMGPQPS AEASWQFFMS
210 220 230 240 250
DKPLNLSVSL SKEIYFHGEP IPVTVTVTNN TDKVVKKIKV SVEQIANVVL
260 270 280 290 300
YSSDYYVKPV ASEETQEKVQ PNSTLTKTLV LVPLLANNRE RRGIALDGKI
310 320 330 340 350
KHEDTNLASS TIIKEGIDRT VMGILVSYHI KVKLTVSGFL GELTSSEVAT
360 370 380 390 400
EVPFRLMHPQ PEDPAKESVQ DENLVFEEFA RQNLKDTGEN TEGKKDEDAG

QDE
Length:403
Mass (Da):44,930
Last modified:February 1, 1991 - v1
Checksum:i2D4CFEAF81C5FC6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti391 – 3911T → P in AAH16498 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24086 mRNA. Translation: AAA40090.1.
BC016498 mRNA. Translation: AAH16498.1.
CCDSiCCDS35656.1.
PIRiJS0066.
RefSeqiNP_033144.1. NM_009118.2.
UniGeneiMm.1276.

Genome annotation databases

EnsembliENSMUST00000077772; ENSMUSP00000076948; ENSMUSG00000056055.
GeneIDi20215.
KEGGimmu:20215.
UCSCiuc007bxp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24086 mRNA. Translation: AAA40090.1.
BC016498 mRNA. Translation: AAH16498.1.
CCDSiCCDS35656.1.
PIRiJS0066.
RefSeqiNP_033144.1. NM_009118.2.
UniGeneiMm.1276.

3D structure databases

ProteinModelPortaliP20443.
SMRiP20443. Positions 11-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203065. 1 interaction.

PTM databases

PhosphoSiteiP20443.

Proteomic databases

MaxQBiP20443.
PRIDEiP20443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077772; ENSMUSP00000076948; ENSMUSG00000056055.
GeneIDi20215.
KEGGimmu:20215.
UCSCiuc007bxp.1. mouse.

Organism-specific databases

CTDi6295.
MGIiMGI:98227. Sag.

Phylogenomic databases

eggNOGiNOG330592.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP20443.
OMAiKEIYFHG.
OrthoDBiEOG79W954.
PhylomeDBiP20443.
TreeFamiTF314260.

Enzyme and pathway databases

ReactomeiREACT_311545. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_326042. Activation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSiSag. mouse.
NextBioi297813.
PROiP20443.
SOURCEiSearch...

Gene expression databases

BgeeiP20443.
CleanExiMM_SAG.
ExpressionAtlasiP20443. baseline and differential.
GenevestigatoriP20443.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  3. "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, MUTAGENESIS OF PHE-86; PHE-198 AND ALA-349.

Entry informationi

Entry nameiARRS_MOUSE
AccessioniPrimary (citable) accession number: P20443
Secondary accession number(s): Q91W62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 1, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Arrestin binds calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.