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Protein

S-arrestin

Gene

SAG

Organism
Bos taurus (Bovine)
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:8003967, PubMed:25205354). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (By similarity).By similarity2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • opsin binding Source: Ensembl
  • phosphoprotein binding Source: Ensembl

GO - Biological processi

  • response to light stimulus Source: UniProtKB
  • signal transduction Source: InterPro

Enzyme and pathway databases

ReactomeiR-BTA-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-antigen1 Publication
Short name:
S-AG
Rod photoreceptor arrestin
Cleaved into the following chain:
Gene namesi
Name:SAG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 3

Organism-specific databases

VGNCiVGNC:34263 SAG

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi85F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-197. 1 Publication1
Mutagenesisi175R → E: Strongly increases affinity for RHO by breaking the interaction with D-296. Abolishes oligomerization. No effect on affinity for RHO; when associated with R-296. 2 Publications1
Mutagenesisi197F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-85. 1 Publication1
Mutagenesisi296D → R: Strongly increases affinity for RHO by breaking the interaction with R-175. No effect on affinity for RHO; when associated with E-175. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000023091 – 404S-arrestinAdd BLAST404
ChainiPRO_00000023115 – 404S-arrestin short formAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; partial1 Publication1
Modified residuei230PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08168
PRIDEiP08168

PTM databases

iPTMnetiP08168

Expressioni

Tissue specificityi

Detected in retina, in rod photoreceptor cells (at protein level) (PubMed:7515057, PubMed:8003967).2 Publications

Gene expression databases

BgeeiENSBTAG00000021480
ExpressionAtlasiP08168 baseline

Interactioni

Subunit structurei

Monomer (PubMed:21288033). Homodimer (PubMed:21288033, PubMed:10219246, PubMed:26510463). Homotetramer (PubMed:21288033, PubMed:10219246). Self-association is cooperative (PubMed:21288033). Isoform A and isoform B interact with RHO (via phosphorylated C-terminus) (PubMed:8003967, PubMed:10219246, PubMed:23604253, PubMed:25205354).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RHOP0269923EBI-15575296,EBI-8592832

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • opsin binding Source: Ensembl
  • phosphoprotein binding Source: Ensembl

Protein-protein interaction databases

BioGridi158306, 1 interactor
DIPiDIP-47525N
IntActiP08168, 3 interactors
MINTiP08168
STRINGi9913.ENSBTAP00000028633

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 11Combined sources4
Beta strandi13 – 16Combined sources4
Beta strandi20 – 27Combined sources8
Beta strandi29 – 33Combined sources5
Beta strandi41 – 47Combined sources7
Helixi49 – 52Combined sources4
Beta strandi56 – 67Combined sources12
Helixi73 – 75Combined sources3
Beta strandi79 – 92Combined sources14
Beta strandi95 – 97Combined sources3
Helixi102 – 111Combined sources10
Beta strandi115 – 120Combined sources6
Beta strandi129 – 132Combined sources4
Beta strandi143 – 155Combined sources13
Beta strandi158 – 163Combined sources6
Helixi166 – 168Combined sources3
Beta strandi169 – 179Combined sources11
Beta strandi189 – 195Combined sources7
Beta strandi202 – 210Combined sources9
Beta strandi212 – 215Combined sources4
Beta strandi220 – 228Combined sources9
Beta strandi230 – 232Combined sources3
Beta strandi234 – 247Combined sources14
Beta strandi249 – 251Combined sources3
Beta strandi254 – 263Combined sources10
Beta strandi272 – 280Combined sources9
Helixi284 – 286Combined sources3
Beta strandi291 – 293Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi301 – 303Combined sources3
Helixi318 – 321Combined sources4
Beta strandi322 – 335Combined sources14
Turni336 – 341Combined sources6
Beta strandi345 – 357Combined sources13
Beta strandi375 – 381Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYRX-ray3.30A/B/C/D1-367[»]
1CF1X-ray2.80A/B/C/D2-404[»]
1Y6Ymodel-B10-362[»]
3UGUX-ray1.85A1-370[»]
3UGXX-ray2.65A/B/C/D1-404[»]
4J2QX-ray3.00A/B1-369[»]
4PXFX-ray2.75B67-77[»]
4ZRGX-ray2.70A1-404[»]
ProteinModelPortaliP08168
SMRiP08168
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08168

Family & Domainsi

Domaini

The C-terminus of isoform A 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. Isoform B is C-terminally truncated and is therefore already in the optimal conformation for RHO binding.4 Publications

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865 Eukaryota
ENOG410XR0F LUCA
GeneTreeiENSGT00390000013152
HOGENOMiHOG000231319
HOVERGENiHBG002399
InParanoidiP08168
KOiK19627
OMAiAWQFFMS
OrthoDBiEOG091G05M2
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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P08168-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKANKPAPNH VIFKKISRDK SVTIYLGKRD YIDHVERVEP VDGVVLVDPE
60 70 80 90 100
LVKGKRVYVS LTCAFRYGQE DIDVMGLSFR RDLYFSQVQV FPPVGASGAT
110 120 130 140 150
TRLQESLIKK LGANTYPFLL TFPDYLPCSV MLQPAPQDVG KSCGVDFEIK
160 170 180 190 200
AFATHSTDVE EDKIPKKSSV RLLIRKVQHA PRDMGPQPRA EASWQFFMSD
210 220 230 240 250
KPLRLAVSLS KEIYYHGEPI PVTVAVTNST EKTVKKIKVL VEQVTNVVLY
260 270 280 290 300
SSDYYIKTVA AEEAQEKVPP NSSLTKTLTL VPLLANNRER RGIALDGKIK
310 320 330 340 350
HEDTNLASST IIKEGIDKTV MGILVSYQIK VKLTVSGLLG ELTSSEVATE
360 370 380 390 400
VPFRLMHPQP EDPDTAKESF QDENFVFEEF ARQNLKDAGE YKEEKTDQEA

AMDE
Length:404
Mass (Da):45,275
Last modified:August 1, 1988 - v1
Checksum:i26B1D80B652AF1EF
GO
Isoform B (identifier: P08168-2) [UniParc]FASTAAdd to basket
Also known as: p44

The sequence of this isoform differs from the canonical sequence as follows:
     370-370: F → A
     371-404: Missing.

Show »
Length:370
Mass (Da):41,162
Checksum:i0FFC995F47FEFBA8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35V → L in AAA30377 (PubMed:2950857).Curated1
Sequence conflicti119L → V in AAA30377 (PubMed:2950857).Curated1
Sequence conflicti177V → I in AAA30377 (PubMed:2950857).Curated1
Sequence conflicti317D → H in AAA30377 (PubMed:2950857).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000319370F → A in isoform B. 1 Publication1
Alternative sequenceiVSP_000320371 – 404Missing in isoform B. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02955 mRNA Translation: AAA30378.1
M15115 mRNA Translation: AAA30377.1
U08346 mRNA Translation: AAA20465.1
X03454 mRNA Translation: CAA27179.1
PIRiB28404 A28404
RefSeqiNP_851343.1, NM_181000.2 [P08168-2]
XP_010802144.1, XM_010803842.2 [P08168-1]
UniGeneiBt.32317

Genome annotation databases

EnsembliENSBTAT00000028633; ENSBTAP00000028633; ENSBTAG00000021480 [P08168-1]
ENSBTAT00000033205; ENSBTAP00000033126; ENSBTAG00000021480 [P08168-2]
GeneIDi280922
KEGGibta:280922

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiARRS_BOVIN
AccessioniPrimary (citable) accession number: P08168
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 28, 2018
This is version 157 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health