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Database: UniProt
Entry: P06002
LinkDB: P06002
Original site: P06002 
ID   OPS1_DROME              Reviewed;         373 AA.
AC   P06002; A0AVV9; Q4QPQ2; Q9TX56; Q9VDS8;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   19-MAR-2014, entry version 139.
DE   RecName: Full=Opsin Rh1;
DE   AltName: Full=Neither inactivation nor afterpotential E protein;
DE   AltName: Full=Outer R1-R6 photoreceptor cells opsin;
GN   Name=ninaE; Synonyms=Rh1; ORFNames=CG4550;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2985266; DOI=10.1016/0092-8674(85)90343-5;
RA   O'Tousa J.E., Baehr W., Martin R.L., Hirsh J., Pak W.L.,
RA   Applebury M.L.;
RT   "The Drosophila ninaE gene encodes an opsin.";
RL   Cell 40:839-850(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2580638; DOI=10.1016/0092-8674(85)90344-7;
RA   Zuker C.S., Cowman A.F., Rubin G.M.;
RT   "Isolation and structure of a rhodopsin gene from D. melanogaster.";
RL   Cell 40:851-858(1985).
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kapadia B., Kronmiller B.,
RA   Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M.,
RA   Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C.,
RA   Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 26-346.
RX   PubMed=8006992; DOI=10.1007/BF00176087;
RA   Carulli J.P., Chen D.M., Stark W.S., Hartl D.L.;
RT   "Phylogeny and physiology of Drosophila opsins.";
RL   J. Mol. Evol. 38:250-262(1994).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Oregon-R; TISSUE=Head;
RX   PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA   Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA   Panin V.;
RT   "Identification of N-glycosylated proteins from the central nervous
RT   system of Drosophila melanogaster.";
RL   Glycobiology 17:1388-1403(2007).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=480 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- MISCELLANEOUS: Each Drosophila eye is composed of 800 facets or
CC       ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8),
CC       the R1 to R6 cells are outer cells, while R7 and R8 are inner
CC       cells.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
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DR   EMBL; K02315; AAA28733.1; -; Genomic_DNA.
DR   EMBL; K02320; AAA28735.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; K02316; AAA28735.1; JOINED; Genomic_DNA.
DR   EMBL; K02317; AAA28735.1; JOINED; Genomic_DNA.
DR   EMBL; K02318; AAA28735.1; JOINED; Genomic_DNA.
DR   EMBL; K02319; AAA28735.1; JOINED; Genomic_DNA.
DR   EMBL; AE014297; AAF55712.1; -; Genomic_DNA.
DR   EMBL; BT010221; AAQ23539.1; -; mRNA.
DR   EMBL; BT023714; AAY85114.1; -; mRNA.
DR   EMBL; BT029277; ABK30914.1; -; mRNA.
DR   PIR; A90864; OOFF.
DR   RefSeq; NP_524407.1; NM_079683.2.
DR   UniGene; Dm.6744; -.
DR   ProteinModelPortal; P06002; -.
DR   SMR; P06002; 12-354.
DR   BioGrid; 67356; 27.
DR   DIP; DIP-17500N; -.
DR   IntAct; P06002; 2.
DR   MINT; MINT-326982; -.
DR   PaxDb; P06002; -.
DR   PRIDE; P06002; -.
DR   EnsemblMetazoa; FBtr0083857; FBpp0083266; FBgn0002940.
DR   GeneID; 42367; -.
DR   KEGG; dme:Dmel_CG4550; -.
DR   CTD; 42367; -.
DR   FlyBase; FBgn0002940; ninaE.
DR   eggNOG; NOG255465; -.
DR   GeneTree; ENSGT00730000110587; -.
DR   InParanoid; P06002; -.
DR   KO; K13802; -.
DR   OMA; NTIWGAC; -.
DR   OrthoDB; EOG790G0Q; -.
DR   PhylomeDB; P06002; -.
DR   ChiTaRS; ninaE; drosophila.
DR   GenomeRNAi; 42367; -.
DR   NextBio; 828455; -.
DR   Bgee; P06002; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:FlyBase.
DR   GO; GO:0016027; C:inaD signaling complex; IPI:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005771; C:multivesicular body; IDA:FlyBase.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:0005767; C:secondary lysosome; IDA:FlyBase.
DR   GO; GO:0016029; C:subrhabdomeral cisterna; IDA:FlyBase.
DR   GO; GO:0008020; F:G-protein coupled photoreceptor activity; IMP:FlyBase.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR   GO; GO:0009589; P:detection of UV; IMP:FlyBase.
DR   GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR   GO; GO:0071632; P:optomotor response; IMP:FlyBase.
DR   GO; GO:0030265; P:phospholipase C-activating rhodopsin mediated signaling pathway; IMP:FlyBase.
DR   GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
DR   GO; GO:0042331; P:phototaxis; IMP:FlyBase.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0009642; P:response to light intensity; IMP:FlyBase.
DR   GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR   GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001735; Opsin_RH1/RH2.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    373       Opsin Rh1.
FT                                /FTId=PRO_0000197622.
FT   TOPO_DOM      1     49       Extracellular.
FT   TRANSMEM     50     74       Helical; Name=1; (Potential).
FT   TOPO_DOM     75     86       Cytoplasmic.
FT   TRANSMEM     87    112       Helical; Name=2; (Potential).
FT   TOPO_DOM    113    126       Extracellular.
FT   TRANSMEM    127    146       Helical; Name=3; (Potential).
FT   TOPO_DOM    147    165       Cytoplasmic.
FT   TRANSMEM    166    189       Helical; Name=4; (Potential).
FT   TOPO_DOM    190    213       Extracellular.
FT   TRANSMEM    214    241       Helical; Name=5; (Potential).
FT   TOPO_DOM    242    276       Cytoplasmic.
FT   TRANSMEM    277    300       Helical; Name=6; (Potential).
FT   TOPO_DOM    301    307       Extracellular.
FT   TRANSMEM    308    332       Helical; Name=7; (Potential).
FT   TOPO_DOM    333    373       Cytoplasmic.
FT   MOD_RES     319    319       N6-(retinylidene)lysine.
FT   CARBOHYD     20     20       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD    196    196       N-linked (GlcNAc...).
FT   DISULFID    123    200       Potential.
SQ   SEQUENCE   373 AA;  41495 MW;  FFF36C90DDD68294 CRC64;
     MESFAVAAAQ LGPHFAPLSN GSVVDKVTPD MAHLISPYWN QFPAMDPIWA KILTAYMIMI
     GMISWCGNGV VIYIFATTKS LRTPANLLVI NLAISDFGIM ITNTPMMGIN LYFETWVLGP
     MMCDIYAGLG SAFGCSSIWS MCMISLDRYQ VIVKGMAGRP MTIPLALGKI AYIWFMSSIW
     CLAPAFGWSR YVPEGNLTSC GIDYLERDWN PRSYLIFYSI FVYYIPLFLI CYSYWFIIAA
     VSAHEKAMRE QAKKMNVKSL RSSEDAEKSA EGKLAKVALV TITLWFMAWT PYLVINCMGL
     FKFEGLTPLN TIWGACFAKS AACYNPIVYG ISHPKYRLAL KEKCPCCVFG KVDDGKSSDA
     QSQATASEAE SKA
//
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