ARRA_DROME
ID ARRA_DROME Reviewed; 364 AA.
AC P15372; Q9VJA8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phosrestin-2;
DE AltName: Full=Arrestin-1;
DE AltName: Full=Arrestin-A;
DE AltName: Full=Phosrestin II;
GN Name=Arr1; Synonyms=ArrA; ORFNames=CG5711;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1689056; DOI=10.1073/pnas.87.3.1003;
RA Smith D.P., Sheih B.-H., Zuker C.S.;
RT "Isolation and structure of an arrestin gene from Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1003-1007(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2105491; DOI=10.1073/pnas.87.3.1008;
RA Hyde D.R., Mecklenburg K.L., Pollock J.A., Vihtelic T.S., Benzer S.;
RT "Twenty Drosophila visual system cDNA clones: one is a homolog of human
RT arrestin.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1008-1012(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=1905538; DOI=10.1016/0006-291x(91)90683-x;
RA Matsumoto H., Yamada T.;
RT "Phosrestins I and II: arrestin homologs which undergo differential light-
RT induced phosphorylation in the Drosophila photoreceptor in vivo.";
RL Biochem. Biophys. Res. Commun. 177:1306-1312(1991).
RN [7]
RP FUNCTION.
RX PubMed=8316831; DOI=10.1126/science.8316831;
RA Dolph P.J., Ranganathan R., Colley N.J., Hardy R.W., Socolich M.,
RA Zuker C.S.;
RT "Arrestin function in inactivation of G protein-coupled receptor rhodopsin
RT in vivo.";
RL Science 260:1910-1916(1993).
CC -!- FUNCTION: Regulates photoreceptor cell deactivation. Arr1 and Arr2
CC proteins are mediators of rhodopsin inactivation and are essential for
CC the termination of the phototransduction cascade.
CC {ECO:0000269|PubMed:8316831}.
CC -!- TISSUE SPECIFICITY: Expressed specifically and abundantly in the
CC photoreceptors. Inner and outer segments, and the inner plexiform
CC regions of the retina. {ECO:0000269|PubMed:1689056}.
CC -!- PTM: Phosphorylated, but does not undergo light-induced
CC phosphorylation. {ECO:0000269|PubMed:1905538}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; M30177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M30140; AAA28380.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53644.1; -; Genomic_DNA.
DR EMBL; AY061824; AAL27635.1; -; mRNA.
DR PIR; A34867; A34867.
DR RefSeq; NP_001246073.1; NM_001259144.2.
DR RefSeq; NP_476681.1; NM_057333.4.
DR AlphaFoldDB; P15372; -.
DR SMR; P15372; -.
DR BioGRID; 61074; 21.
DR DIP; DIP-19039N; -.
DR IntAct; P15372; 11.
DR STRING; 7227.FBpp0298351; -.
DR PaxDb; P15372; -.
DR DNASU; 35078; -.
DR EnsemblMetazoa; FBtr0081030; FBpp0080583; FBgn0000120.
DR EnsemblMetazoa; FBtr0307350; FBpp0298351; FBgn0000120.
DR GeneID; 35078; -.
DR KEGG; dme:Dmel_CG5711; -.
DR CTD; 35078; -.
DR FlyBase; FBgn0000120; Arr1.
DR VEuPathDB; VectorBase:FBgn0000120; -.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_1_1_1; -.
DR InParanoid; P15372; -.
DR OMA; MGLNFQK; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; P15372; -.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P15372; -.
DR BioGRID-ORCS; 35078; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Arr1; fly.
DR GenomeRNAi; 35078; -.
DR PRO; PR:P15372; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000120; Expressed in head capsule and 15 other tissues.
DR ExpressionAtlas; P15372; baseline and differential.
DR Genevisible; P15372; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0002046; F:opsin binding; ISS:FlyBase.
DR GO; GO:0016059; P:deactivation of rhodopsin mediated signaling; IGI:FlyBase.
DR GO; GO:0002032; P:desensitization of G protein-coupled receptor signaling pathway by arrestin; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR GO; GO:0016060; P:metarhodopsin inactivation; IGI:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.640; -; 1.
DR Gene3D; 2.60.40.840; -; 1.
DR InterPro; IPR000698; Arrestin.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR InterPro; IPR017864; Arrestin_CS.
DR InterPro; IPR014753; Arrestin_N.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11792; PTHR11792; 1.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR PRINTS; PR00309; ARRESTIN.
DR SMART; SM01017; Arrestin_C; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS00295; ARRESTINS; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..364
FT /note="Phosrestin-2"
FT /id="PRO_0000205215"
SQ SEQUENCE 364 AA; 40771 MW; 0DCC764C4F890FC2 CRC64;
MVVNFKVFKK CSPNNMITLY MNRRDFVDSV TQVEPIDGII VLDDEYVRQN RKIFVQLVCN
FRYGREDDEM IGLRFQKELT LVSQQVCPPQ KQDIQLTKMQ ERLLKKLGSN AYPFVMQMPP
SSPASVVLQQ KASDESQPCG VQYFVKIFTG DSDCDRSHRR STINLGIRKV QYAPTKQGIQ
PCTVVRKDFL LSPGELELEV TLDKQLYHHG EKISVNICVR NNSNKVVKKI KAMVQQGVDV
VLFQNGQFRN TIAFMETSEG CPLNPGSSLQ KVMYLVPTLV ANCDRAGIAV EGDIKRKDTA
LASTTLIASQ DARDAFGIIV SYAVKVKLFL GALGGELCAE LPFILMHPKP SRKAQLEAEG
SIEA
