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Database: UniProt
Entry: Q9YGZ8
LinkDB: Q9YGZ8
Original site: Q9YGZ8 
ID   OPSD_CHELB              Reviewed;         353 AA.
AC   Q9YGZ8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   28-FEB-2018, entry version 75.
DE   RecName: Full=Rhodopsin;
GN   Name=rho;
OS   Chelon labrosus (Thicklip grey mullet) (Mugil chelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Mugilomorphae; Mugilidae; Chelon.
OX   NCBI_TaxID=48171;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Archer S.N., Hirano J.;
RT   "Comparative analysis of opsins in Mediterranian coastal fish.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Photoreceptor required for image-forming vision at low
CC       light intensity. While most salt water fish species use retinal as
CC       chromophore, most freshwater fish use 3-dehydroretinal, or a
CC       mixture of retinal and 3-dehydroretinal (By similarity). Light-
CC       induced isomerization of 11-cis to all-trans retinal triggers a
CC       conformational change that activates signaling via G-proteins.
CC       Subsequent receptor phosphorylation mediates displacement of the
CC       bound G-protein alpha subunit by arrestin and terminates signaling
CC       (By similarity). {ECO:0000250|UniProtKB:P02699,
CC       ECO:0000250|UniProtKB:P08100, ECO:0000250|UniProtKB:P32309}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P08100};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P08100}. Cell
CC       projection, cilium, photoreceptor outer segment
CC       {ECO:0000250|UniProtKB:P35359}. Note=Synthesized in the inner
CC       segment (IS) of rod photoreceptor cells before vectorial transport
CC       to disk membranes in the rod outer segment (OS) photosensory
CC       cilia. {ECO:0000250|UniProtKB:P08100}.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC       {ECO:0000250|UniProtKB:P02699}.
CC   -!- PTM: Contains one covalently linked retinal chromophore.
CC       {ECO:0000250|UniProtKB:P02699}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
DR   EMBL; Y18669; CAA77251.1; -; mRNA.
DR   ProteinModelPortal; Q9YGZ8; -.
DR   SMR; Q9YGZ8; -.
DR   HOVERGEN; HBG107442; -.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR   GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR   GO; GO:0008020; F:G-protein coupled photoreceptor activity; ISS:UniProtKB.
DR   GO; GO:0016038; P:absorption of visible light; ISS:UniProtKB.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
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; IPR027430; Retinal_BS.
DR   InterPro; IPR000732; Rhodopsin.
DR   InterPro; IPR019477; Rhodopsin_N.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF10413; Rhodopsin_N; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
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   Cell projection; Chromophore; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN         1    353       Rhodopsin.
FT                                /FTId=PRO_0000197659.
FT   TOPO_DOM      1     36       Extracellular. {ECO:0000305}.
FT   TRANSMEM     37     61       Helical; Name=1.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM     62     73       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM     74     96       Helical; Name=2.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM     97    110       Extracellular. {ECO:0000305}.
FT   TRANSMEM    111    133       Helical; Name=3.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM    134    152       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    153    173       Helical; Name=4.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM    174    202       Extracellular. {ECO:0000305}.
FT   TRANSMEM    203    224       Helical; Name=5.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM    225    252       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    253    274       Helical; Name=6.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM    275    286       Extracellular. {ECO:0000305}.
FT   TRANSMEM    287    308       Helical; Name=7.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   TOPO_DOM    309    353       Cytoplasmic. {ECO:0000305}.
FT   MOTIF       134    136       'Ionic lock' involved in activated form
FT                                stabilization.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   SITE        113    113       Plays an important role in the
FT                                conformation switch to the active
FT                                conformation.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   MOD_RES     296    296       N6-(retinylidene)lysine.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   LIPID       322    322       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   LIPID       323    323       S-palmitoyl cysteine.
FT                                {ECO:0000250|UniProtKB:P02699}.
FT   CARBOHYD      2      2       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     15     15       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    110    187       {ECO:0000255|PROSITE-ProRule:PRU00521}.
SQ   SEQUENCE   353 AA;  39505 MW;  8C4B6F4847B3C632 CRC64;
     MNGTEGPYFY IPMVNTTGIV RSPYEYPQYY LVNPAAYAAL GAYMFLLILV GFPVNFLTLY
     VTLEHKKLRT PLNYILLNLA VADLFMVLGG FTTTMYTSMH GYFVLGRLGC NVEGFFATLG
     GEIALWSLVV LAIERWVVVC KPISNFRFSE DHAIMGLAFT WVMASACAVP PLVGWSRYIP
     EGMQCSCGID YYTRAEGFNN ESFVIYMFVC HFLIPLVVVF FCYGRLLCAV KEAAAAQQES
     ETTQRAEREV SRMVVIMVVA FLVCWCPYAG VAWYIFTHQG SEFGPLFMTF PAFFAKSSSI
     YNPMIYICMN KQFRHCMITT LCCGKNPFEE EEGASTTSKT EASSVSSSSV SPA
//
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