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Protein

S-arrestin

Gene

Sag

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (PubMed:9333241, PubMed:16421323). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (PubMed:16421323).2 Publications

GO - Molecular functioni

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

GO - Biological processi

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:98227 Sag

Subcellular locationi

Keywords - Cellular componenti

Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

The morphology of the retina is not affected when mice are kept in constant darkness. When mice are exposed to alternating 12 hour light and dark cycles, the rod photoreceptor outer segments are about 25% shorter than in wild-type, and the photoreceptor outer segments appear somewhat disordered (PubMed:9333241). After one year exposure to alternating 12 hour light and dark cycles, there are clear signs of photoreceptor degeneration with about 50% reduction in the number of photoreceptor nuclei in the outer layer of the retina (PubMed:16421323). Rod photoreceptor cells show normal flash sensitivity, but display prolonged RHO signaling, due to a strongly decreased rate of deactivation (PubMed:9333241, PubMed:16421323).2 Publications

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
Mutagenesisi374 – 376LVF → AAA: Strongly increases affinity for RHO. 1 Publication3

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei231PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20443
PRIDEiP20443

PTM databases

iPTMnetiP20443
PhosphoSitePlusiP20443

Expressioni

Tissue specificityi

Detected in retina (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000056055
CleanExiMM_SAG
ExpressionAtlasiP20443 baseline and differential
GenevisibleiP20443 MM

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer (PubMed:21288033). Interacts with RHO (via the phosphorylated C-terminus) (PubMed:26200343, PubMed:28753425).3 Publications

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 strandi13 – 17Combined sources5
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 – 76Combined sources6
Beta strandi83 – 93Combined sources11
Helixi103 – 111Combined sources9
Beta strandi116 – 121Combined sources6
Beta strandi131 – 133Combined sources3
Beta strandi144 – 157Combined sources14
Turni159 – 162Combined sources4
Turni167 – 169Combined sources3
Beta strandi171 – 178Combined sources8
Beta strandi190 – 195Combined sources6
Beta strandi204 – 211Combined sources8
Beta strandi213 – 216Combined sources4
Beta strandi221 – 229Combined sources9
Beta strandi231 – 233Combined sources3
Beta strandi235 – 265Combined sources31
Beta strandi273 – 281Combined sources9
Helixi285 – 288Combined sources4
Beta strandi295 – 297Combined sources3
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[»]
5W0PX-ray3.01A/B/C/D10-392[»]
ProteinModelPortaliP20443
SMRiP20443
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 19Interaction with RHO1 Publication9

Domaini

The C-terminus interferes with binding to non-phosphorylated RHO. Interaction with phosphorylated RHO triggers displacement of the C-terminus and leads to a conformation change that mediates high-affinity RHO binding.By similarity

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865 Eukaryota
ENOG410XR0F LUCA
GeneTreeiENSGT00390000013152
HOGENOMiHOG000231319
HOVERGENiHBG002399
InParanoidiP20443
KOiK19627
OMAiAWQFFMS
PhylomeDBiP20443
TreeFamiTF314260

Family and domain databases

Gene3Di2.60.40.640, 1 hit
2.60.40.840, 1 hit
InterProiView protein in InterPro
IPR000698 Arrestin
IPR011021 Arrestin-like_N
IPR014752 Arrestin_C
IPR011022 Arrestin_C-like
IPR017864 Arrestin_CS
IPR014753 Arrestin_N
IPR014756 Ig_E-set
PANTHERiPTHR11792 PTHR11792, 1 hit
PfamiView protein in Pfam
PF02752 Arrestin_C, 1 hit
PF00339 Arrestin_N, 1 hit
PRINTSiPR00309 ARRESTIN
SMARTiView protein in SMART
SM01017 Arrestin_C, 1 hit
SUPFAMiSSF81296 SSF81296, 2 hits
PROSITEiView protein in PROSITE
PS00295 ARRESTINS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiARRS_MOUSE
AccessioniPrimary (citable) accession number: P20443
Secondary accession number(s): Q91W62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 28, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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