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Protein

Phosrestin-2

Gene

Arr1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates photoreceptor cell deactivation. Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade.1 Publication

GO - Molecular functioni

  • opsin binding Source: FlyBase

GO - Biological processi

  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • endocytosis Source: FlyBase
  • metarhodopsin inactivation Source: FlyBase
  • photoreceptor cell maintenance Source: FlyBase
  • phototransduction Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiR-DME-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-DME-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-DME-5099900. WNT5A-dependent internalization of FZD4.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosrestin-2
Alternative name(s):
Arrestin-1
Arrestin-A
Phosrestin II
Gene namesi
Name:Arr1
Synonyms:ArrA
ORF Names:CG5711
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000120. Arr1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • rhabdomere Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Phosrestin-2PRO_0000205215Add
BLAST

Post-translational modificationi

Phosphorylated, but does not undergo light-induced phosphorylation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP15372.
PRIDEiP15372.

Expressioni

Tissue specificityi

Expressed specifically and abundantly in the photoreceptors. Inner and outer segments, and the inner plexiform regions of the retina.1 Publication

Gene expression databases

BgeeiP15372.
ExpressionAtlasiP15372. differential.
GenevisibleiP15372. DM.

Interactioni

GO - Molecular functioni

  • opsin binding Source: FlyBase

Protein-protein interaction databases

BioGridi61074. 19 interactions.
DIPiDIP-19039N.
IntActiP15372. 8 interactions.
MINTiMINT-333230.
STRINGi7227.FBpp0298351.

Structurei

3D structure databases

ProteinModelPortaliP15372.
SMRiP15372. Positions 6-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
InParanoidiP15372.
KOiK13808.
OMAiMGLNFQK.
OrthoDBiEOG79W954.
PhylomeDBiP15372.

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.

P15372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVNFKVFKK CSPNNMITLY MNRRDFVDSV TQVEPIDGII VLDDEYVRQN
60 70 80 90 100
RKIFVQLVCN FRYGREDDEM IGLRFQKELT LVSQQVCPPQ KQDIQLTKMQ
110 120 130 140 150
ERLLKKLGSN AYPFVMQMPP SSPASVVLQQ KASDESQPCG VQYFVKIFTG
160 170 180 190 200
DSDCDRSHRR STINLGIRKV QYAPTKQGIQ PCTVVRKDFL LSPGELELEV
210 220 230 240 250
TLDKQLYHHG EKISVNICVR NNSNKVVKKI KAMVQQGVDV VLFQNGQFRN
260 270 280 290 300
TIAFMETSEG CPLNPGSSLQ KVMYLVPTLV ANCDRAGIAV EGDIKRKDTA
310 320 330 340 350
LASTTLIASQ DARDAFGIIV SYAVKVKLFL GALGGELCAE LPFILMHPKP
360
SRKAQLEAEG SIEA
Length:364
Mass (Da):40,771
Last modified:April 1, 1990 - v1
Checksum:i0DCC764C4F890FC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30177 Genomic DNA. No translation available.
M30140 Genomic DNA. Translation: AAA28380.1.
AE014134 Genomic DNA. Translation: AAF53644.1.
AY061824 mRNA. Translation: AAL27635.1.
PIRiA34867.
RefSeqiNP_001246073.1. NM_001259144.2.
NP_476681.1. NM_057333.4.
UniGeneiDm.450.

Genome annotation databases

EnsemblMetazoaiFBtr0081030; FBpp0080583; FBgn0000120.
FBtr0307350; FBpp0298351; FBgn0000120.
GeneIDi35078.
KEGGidme:Dmel_CG5711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30177 Genomic DNA. No translation available.
M30140 Genomic DNA. Translation: AAA28380.1.
AE014134 Genomic DNA. Translation: AAF53644.1.
AY061824 mRNA. Translation: AAL27635.1.
PIRiA34867.
RefSeqiNP_001246073.1. NM_001259144.2.
NP_476681.1. NM_057333.4.
UniGeneiDm.450.

3D structure databases

ProteinModelPortaliP15372.
SMRiP15372. Positions 6-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61074. 19 interactions.
DIPiDIP-19039N.
IntActiP15372. 8 interactions.
MINTiMINT-333230.
STRINGi7227.FBpp0298351.

Proteomic databases

PaxDbiP15372.
PRIDEiP15372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081030; FBpp0080583; FBgn0000120.
FBtr0307350; FBpp0298351; FBgn0000120.
GeneIDi35078.
KEGGidme:Dmel_CG5711.

Organism-specific databases

CTDi35078.
FlyBaseiFBgn0000120. Arr1.

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
InParanoidiP15372.
KOiK13808.
OMAiMGLNFQK.
OrthoDBiEOG79W954.
PhylomeDBiP15372.

Enzyme and pathway databases

ReactomeiR-DME-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-DME-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-DME-5099900. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

ChiTaRSiArr1. fly.
GenomeRNAii35078.
PROiP15372.

Gene expression databases

BgeeiP15372.
ExpressionAtlasiP15372. differential.
GenevisibleiP15372. DM.

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

« Hide 'large scale' publications
  1. "Isolation and structure of an arrestin gene from Drosophila."
    Smith D.P., Sheih B.-H., Zuker C.S.
    Proc. Natl. Acad. Sci. U.S.A. 87:1003-1007(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  2. "Twenty Drosophila visual system cDNA clones: one is a homolog of human arrestin."
    Hyde D.R., Mecklenburg K.L., Pollock J.A., Vihtelic T.S., Benzer S.
    Proc. Natl. Acad. Sci. U.S.A. 87:1008-1012(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Phosrestins I and II: arrestin homologs which undergo differential light-induced phosphorylation in the Drosophila photoreceptor in vivo."
    Matsumoto H., Yamada T.
    Biochem. Biophys. Res. Commun. 177:1306-1312(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  7. "Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo."
    Dolph P.J., Ranganathan R., Colley N.J., Hardy R.W., Socolich M., Zuker C.S.
    Science 260:1910-1916(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiARRA_DROME
AccessioniPrimary (citable) accession number: P15372
Secondary accession number(s): Q9VJA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.