Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

ReactomeiR-MMU-2514859. Inactivation, recovery and regulation 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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
Mutagenesisi86F → 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 Publication1
Mutagenesisi198F → 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 Publication1
Mutagenesisi349A → 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 Publication1

Keywords - Diseasei

Autoimmune uveitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051871 – 403S-arrestinAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi129 ↔ 144Curated
Modified residuei231PhosphothreonineBy similarity1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP20443.
PRIDEiP20443.

PTM databases

iPTMnetiP20443.
PhosphoSitePlusiP20443.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

BgeeiENSMUSG00000056055.
CleanExiMM_SAG.
ExpressionAtlasiP20443. baseline and differential.
GenevisibleiP20443. MM.

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer.1 Publication

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi203065. 1 interactor.
STRINGi10090.ENSMUSP00000076948.

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 17Combined sources4
Beta strandi19 – 28Combined sources10
Beta strandi30 – 34Combined sources5
Beta strandi36 – 39Combined sources4
Beta strandi42 – 48Combined sources7
Turni50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi57 – 69Combined sources13
Helixi71 – 77Combined sources7
Beta strandi84 – 93Combined sources10
Helixi103 – 111Combined sources9
Beta strandi114 – 121Combined sources8
Beta strandi131 – 134Combined sources4
Beta strandi144 – 157Combined sources14
Turni159 – 162Combined sources4
Turni167 – 169Combined sources3
Beta strandi171 – 178Combined sources8
Beta strandi192 – 195Combined sources4
Beta strandi204 – 207Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi221 – 229Combined sources9
Beta strandi231 – 254Combined sources24
Beta strandi259 – 265Combined sources7
Beta strandi273 – 281Combined sources9
Turni285 – 288Combined sources4
Beta strandi294 – 297Combined sources4
Beta strandi300 – 302Combined sources3
Beta strandi323 – 337Combined sources15
Beta strandi345 – 358Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWJX-ray3.30A/B/C/D10-392[»]
5DGYX-ray7.70A/B/C/D10-392[»]
ProteinModelPortaliP20443.
SMRiP20443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP20443.
KOiK19627.
OMAiKEIYFHG.
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)DescriptionActionsGraphical viewLength
Sequence conflicti391T → P in AAH16498 (PubMed:15489334).Curated1

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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZWJX-ray3.30A/B/C/D10-392[»]
5DGYX-ray7.70A/B/C/D10-392[»]
ProteinModelPortaliP20443.
SMRiP20443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203065. 1 interactor.
STRINGi10090.ENSMUSP00000076948.

PTM databases

iPTMnetiP20443.
PhosphoSitePlusiP20443.

Proteomic databases

PaxDbiP20443.
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

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP20443.
KOiK19627.
OMAiKEIYFHG.
PhylomeDBiP20443.
TreeFamiTF314260.

Enzyme and pathway databases

ReactomeiR-MMU-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSiSag. mouse.
PROiP20443.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056055.
CleanExiMM_SAG.
ExpressionAtlasiP20443. baseline and differential.
GenevisibleiP20443. MM.

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_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: November 2, 2016
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.