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Protein

S-arrestin

Gene

SAG

Organism
Bos taurus (Bovine)
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. Isoform B plays a role in the phototransduction cascade.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium

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-antigen
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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

S-antigen induces autoimmune uveitis.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-197. 1 Publication
Mutagenesisi197 – 1971F → A: Abrogates tetramerization, reduces dimerization, does not affect binding to microtubules and to phosphorylated light-activated rhodopsin; when associated with A-85. 1 Publication

Keywords - Diseasei

Autoimmune uveitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404S-arrestinPRO_0000002309Add
BLAST
Chaini5 – 404400S-arrestin short formPRO_0000002311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; partial1 Publication
Disulfide bondi128 ↔ 143Curated
Modified residuei230 – 2301PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP08168.
PRIDEiP08168.

Expressioni

Tissue specificityi

Retina and pineal gland. Isoform B is localized in the photoreceptor outer segment.

Gene expression databases

ExpressionAtlasiP08168. baseline.

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer. Self-association is cooperative.1 Publication

Protein-protein interaction databases

BioGridi158306. 1 interaction.
DIPiDIP-47525N.
IntActiP08168. 3 interactions.
STRINGi9913.ENSBTAP00000028633.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 114Combined sources
Beta strandi13 – 164Combined sources
Beta strandi20 – 278Combined sources
Beta strandi29 – 335Combined sources
Beta strandi41 – 477Combined sources
Helixi49 – 524Combined sources
Beta strandi56 – 6712Combined sources
Helixi73 – 753Combined sources
Beta strandi79 – 9214Combined sources
Beta strandi95 – 973Combined sources
Helixi102 – 11110Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi143 – 15513Combined sources
Beta strandi158 – 1636Combined sources
Helixi166 – 1683Combined sources
Beta strandi169 – 17911Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi220 – 2289Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 24714Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 26310Combined sources
Beta strandi272 – 2809Combined sources
Helixi284 – 2863Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi301 – 3033Combined sources
Helixi318 – 3214Combined sources
Beta strandi322 – 33514Combined sources
Turni336 – 3416Combined sources
Beta strandi345 – 35713Combined sources
Beta strandi375 – 3817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08168.

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP08168.
KOiK19627.
OMAiKEIYFHG.
OrthoDBiEOG79W954.
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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351V → L in AAA30377 (PubMed:2950857).Curated
Sequence conflicti119 – 1191L → V in AAA30377 (PubMed:2950857).Curated
Sequence conflicti177 – 1771V → I in AAA30377 (PubMed:2950857).Curated
Sequence conflicti317 – 3171D → H in AAA30377 (PubMed:2950857).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei370 – 3701F → A in isoform B. CuratedVSP_000319
Alternative sequencei371 – 40434Missing in isoform B. CuratedVSP_000320Add
BLAST

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158306. 1 interaction.
DIPiDIP-47525N.
IntActiP08168. 3 interactions.
STRINGi9913.ENSBTAP00000028633.

Proteomic databases

PaxDbiP08168.
PRIDEiP08168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6295.

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP08168.
KOiK19627.
OMAiKEIYFHG.
OrthoDBiEOG79W954.
TreeFamiTF314260.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP08168.
NextBioi20805044.

Gene expression databases

ExpressionAtlasiP08168. baseline.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "A splice variant of arrestin. Molecular cloning and localization in bovine retina."
    Smith W.C., Milam A.H., Dugger D., Arendt A., Hargrave P.A., Palczewski K.
    J. Biol. Chem. 269:15407-15410(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  4. "Sequence analysis of bovine retinal S-antigen. Relationships with alpha-transducin and G-proteins."
    Wistow G.J., Katial A., Craft C.M., Shinohara T.
    FEBS Lett. 196:23-28(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-404.
  5. "The amino acid sequence of S-antigen: N-terminus and uveitogenic peptides."
    Tsunasawa S., Shichi H.
    Biochim. Biophys. Acta 994:191-193(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12 AND 198-229.
  6. "Ca2+ binding capacity of cytoplasmic proteins from rod photoreceptors is mainly due to arrestin."
    Huppertz B., Weyand I., Bauer P.J.
    J. Biol. Chem. 265:9470-9475(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  7. "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-85 AND PHE-197.
  8. "X-ray crystal structure of arrestin from bovine rod outer segments."
    Granzin J., Wilden U., Choe H.W., Labahn J., Krafft B., Buldt G.
    Nature 391:918-921(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
  9. "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation."
    Hirsch J.A., Schubert C., Gurevich V.V., Sigler P.B.
    Cell 97:257-269(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiARRS_BOVIN
AccessioniPrimary (citable) accession number: P08168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 13, 2016
This is version 141 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.