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P20443 (ARRS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-arrestin
Alternative name(s):
48 kDa protein
Retinal S-antigen
Short name=S-AG
Rod photoreceptor arrestin
Gene names
Name:Sag
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Monomer. Homodimer. Homotetramer. Ref.3

Tissue specificity

Retina and pineal gland.

Involvement in disease

S-antigen induces autoimmune uveitis.

Miscellaneous

Arrestin binds calcium.

Sequence similarities

Belongs to the arrestin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403S-arrestin
PRO_0000205187

Amino acid modifications

Modified residue2311Phosphothreonine By similarity
Disulfide bond129 ↔ 144 Probable

Experimental info

Mutagenesis861F → 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. Ref.3
Mutagenesis1981F → 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. Ref.3
Mutagenesis3491A → 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. Ref.3
Sequence conflict3911T → P in AAH16498. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P20443 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 2D4CFEAF81C5FC6D

FASTA40344,930
        10         20         30         40         50         60 
MAACGKTNKS HVIFKKVSRD KSVTIYLGKR DYVDHVSQVE PVDGVVLVDP ELVKGKKVYV 

        70         80         90        100        110        120 
TLTCAFRYGQ EDIDVMGLTF RRDLYFSRVQ VYPPVGAMSV LTQLQESLLK KLGDNTYPFL 

       130        140        150        160        170        180 
LTFPDYLPCS VMLQPAPQDV GKSCGVDFEV KAFASDITDP EEDKIPKKSS VRLLIRKVQH 

       190        200        210        220        230        240 
APPEMGPQPS AEASWQFFMS DKPLNLSVSL SKEIYFHGEP IPVTVTVTNN TDKVVKKIKV 

       250        260        270        280        290        300 
SVEQIANVVL YSSDYYVKPV ASEETQEKVQ PNSTLTKTLV LVPLLANNRE RRGIALDGKI 

       310        320        330        340        350        360 
KHEDTNLASS TIIKEGIDRT VMGILVSYHI KVKLTVSGFL GELTSSEVAT EVPFRLMHPQ 

       370        380        390        400 
PEDPAKESVQ DENLVFEEFA RQNLKDTGEN TEGKKDEDAG QDE 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of mouse S-antigen."
Tsuda M., Syed M., Bugra K., Whelan J.P., McGinnis J.F., Shinohara T.
Gene 73:11-20(1988) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24086 mRNA. Translation: AAA40090.1.
BC016498 mRNA. Translation: AAH16498.1.
CCDSCCDS35656.1.
PIRJS0066.
RefSeqNP_033144.1. NM_009118.2.
UniGeneMm.1276.

3D structure databases

ProteinModelPortalP20443.
SMRP20443. Positions 11-361.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP20443.

Proteomic databases

MaxQBP20443.
PRIDEP20443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077772; ENSMUSP00000076948; ENSMUSG00000056055.
GeneID20215.
KEGGmmu:20215.
UCSCuc007bxp.1. mouse.

Organism-specific databases

CTD6295.
MGIMGI:98227. Sag.

Phylogenomic databases

eggNOGNOG330592.
HOGENOMHOG000231319.
HOVERGENHBG002399.
InParanoidP20443.
OMAKEIYFHG.
OrthoDBEOG79W954.
PhylomeDBP20443.
TreeFamTF314260.

Gene expression databases

ArrayExpressP20443.
BgeeP20443.
CleanExMM_SAG.
GenevestigatorP20443.

Family and domain databases

Gene3D2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR11792. PTHR11792. 1 hit.
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSPR00309. ARRESTIN.
SMARTSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 2 hits.
PROSITEPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297813.
PROP20443.
SOURCESearch...

Entry information

Entry nameARRS_MOUSE
AccessionPrimary (citable) accession number: P20443
Secondary accession number(s): Q91W62
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot