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OPS6_DROME
ID   OPS6_DROME              Reviewed;         369 AA.
AC   O01668; Q8SXF4; Q9VF58;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Opsin Rh6;
DE   AltName: Full=Rhodopsin Rh6, long-wavelength;
GN   Name=Rh6; ORFNames=CG5192;
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 [MRNA] (ISOFORM B).
RC   STRAIN=Oregon-R; TISSUE=Retina;
RX   PubMed=9109375; DOI=10.1016/s0014-5793(97)00210-x;
RA   Huber A., Schulz S., Bentrop J., Groell C., Wolfrum U., Paulsen R.;
RT   "Molecular cloning of Drosophila Rh6 rhodopsin: the visual pigment of a
RT   subset of R8 photoreceptor cells.";
RL   FEBS Lett. 406:6-10(1997).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=O01668-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=O01668-2; Sequence=VSP_009271;
CC   -!- TISSUE SPECIFICITY: Each Drosophila eye is composed of 800 facets or
CC       ommatidia. Each ommatidium contains 8 photoreceptor cells (R1-R8), the
CC       R1 to R6 cells are outer cells, while R7 and R8 are inner cells. Rh6 is
CC       expressed in a subset of R8 cells, most likely expressed in the subset
CC       of R8 cells paired with Rh4-expressing R7 cells (R7y).
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC       present in the C-terminal region. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Z86118; CAB06821.1; -; mRNA.
DR   EMBL; AE014297; AAN13666.2; -; Genomic_DNA.
DR   EMBL; AY089666; AAL90404.1; -; mRNA.
DR   RefSeq; NP_524368.4; NM_079644.3. [O01668-1]
DR   AlphaFoldDB; O01668; -.
DR   SMR; O01668; -.
DR   BioGRID; 66950; 1.
DR   STRING; 7227.FBpp0082600; -.
DR   GlyGen; O01668; 3 sites.
DR   PaxDb; O01668; -.
DR   PRIDE; O01668; -.
DR   EnsemblMetazoa; FBtr0347603; FBpp0312616; FBgn0019940.
DR   GeneID; 41889; -.
DR   KEGG; dme:Dmel_CG5192; -.
DR   CTD; 41889; -.
DR   FlyBase; FBgn0019940; Rh6.
DR   VEuPathDB; VectorBase:FBgn0019940; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234631; -.
DR   HOGENOM; CLU_718813_0_0_1; -.
DR   InParanoid; O01668; -.
DR   OMA; YFAKDWF; -.
DR   PhylomeDB; O01668; -.
DR   BioGRID-ORCS; 41889; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41889; -.
DR   PRO; PR:O01668; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0019940; Expressed in head capsule and 8 other tissues.
DR   Genevisible; O01668; DM.
DR   GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IGI:FlyBase.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IGI:FlyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0007602; P:phototransduction; IGI:FlyBase.
DR   GO; GO:0007605; P:sensory perception of sound; 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   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chromophore; 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..369
FT                   /note="Opsin Rh6"
FT                   /id="PRO_0000197634"
FT   TOPO_DOM        1..46
FT                   /note="Extracellular"
FT   TRANSMEM        47..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..83
FT                   /note="Cytoplasmic"
FT   TRANSMEM        84..109
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..123
FT                   /note="Extracellular"
FT   TRANSMEM        124..143
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..162
FT                   /note="Cytoplasmic"
FT   TRANSMEM        163..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..210
FT                   /note="Extracellular"
FT   TRANSMEM        211..238
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..274
FT                   /note="Cytoplasmic"
FT   TRANSMEM        275..298
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        299..305
FT                   /note="Extracellular"
FT   TRANSMEM        306..330
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..369
FT                   /note="Cytoplasmic"
FT   MOD_RES         317
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         230..369
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_009271"
SQ   SEQUENCE   369 AA;  41691 MW;  5670A7435AD5F244 CRC64;
     MASLHPPSFA YMRDGRNLSL AESVPAEIMH MVDPYWYQWP PLEPMWFGII GFVIAILGTM
     SLAGNFIVMY IFTSSKGLRT PSNMFVVNLA FSDFMMMFTM FPPVVLNGFY GTWIMGPFLC
     ELYGMFGSLF GCVSIWSMTL IAYDRYCVIV KGMARKPLTA TAAVLRLMVV WTICGAWALM
     PLFGWNRYVP EGNMTACGTD YFAKDWWNRS YIIVYSLWVY LTPLLTIIFS YWHIMKAVAA
     HEKAMREQAK KMNVASLRNS EADKSKAIEI KLAKVALTTI SLWFFAWTPY TIINYAGIFE
     SMHLSPLSTI CGSVFAKANA VCNPIVYGLS HPKYKQVLRE KMPCLACGKD DLTSDSRTQA
     TAEISESQA
 
 
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