Entry sw:OPSD_SCYCA

ID   OPSD_SCYCA              Reviewed;         354 AA.
AC   O93459;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   05-OCT-2016, entry version 70.
DE   RecName: Full=Rhodopsin;
GN   Name=rho;
OS   Scyliorhinus canicula (Small-spotted catshark) (Squalus canicula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes;
OC   Scyliorhinidae; Scyliorhinus.
OX   NCBI_TaxID=7830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Bozzano A., Murgia R., Vallerga S., Hirano J., Archer S.N.;
RT   "Adaptational features of the photoreceptor system in the retinae of
RT   two species of dogfish: relationships with feeding habits and depth
RT   distribution.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Visual pigments such as rhodopsin and porphyropsin are
CC       light-absorbing molecules that mediate vision. Rhodopsin consists
CC       of an apoprotein, opsin, covalently linked to 11-cis-retinal. This
CC       receptor is coupled to the activation of phospholipase C.
CC       Porphyropsin consists of opsin covalently linked to 11-cis 3,4-
CC       didehydroretinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC       vision in dim light.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
DR   EMBL; Y17585; CAA76797.1; -; mRNA.
DR   ProteinModelPortal; O93459; -.
DR   HOVERGEN; HBG107442; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.840.10; -; 1.
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   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    354       Rhodopsin.
FT                                /FTId=PRO_0000197718.
FT   TOPO_DOM      1     36       Extracellular.
FT   TRANSMEM     37     61       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     62     73       Cytoplasmic.
FT   TRANSMEM     74     98       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM     99    113       Extracellular.
FT   TRANSMEM    114    133       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    134    152       Cytoplasmic.
FT   TRANSMEM    153    176       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    177    202       Extracellular.
FT   TRANSMEM    203    230       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    231    252       Cytoplasmic.
FT   TRANSMEM    253    276       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    277    284       Extracellular.
FT   TRANSMEM    285    309       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    310    354       Cytoplasmic.
FT   MOD_RES     296    296       N6-(retinylidene)lysine. {ECO:0000250}.
FT   LIPID       322    322       S-palmitoyl cysteine. {ECO:0000250}.
FT   CARBOHYD      2      2       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     15     15       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    110    187       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       290    306       ipat:OPSIN [T]
FT   MYHIT        55    306       ipfam:7tm_1 [T]
FT   MYHIT        54    306       iprf:G_PROTEIN_RECEP_F1_2 [T]
FT   MYHIT       123    139       ipat:G_PROTEIN_RECEP_F1_1 [T]
FT   MYHIT         2     37       ipfam:Rhodopsin_N [T]
SQ   SEQUENCE   354 AA;  39761 MW;  C2AE5F63CED4AC70 CRC64;
     MNGTEGENFY IPMSNKTGVV RSPFDYPQYY LAEPWKFSVL AAYMFFLIIA GFPVNFLTLY
     VTIQHKKLRQ PLNYILLNLA VADLFMIFGG FPSTMITSMN GYFVFGPSGC NFEGFFATLG
     GEIGLWSLVV LAIERYVVVC KPMSNFRFGS QHAFMGVGLT WIMAMACAFP PLVGWSRYIP
     EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFSIPLTIIF FCYGRLVCTV KEAAAQQQES
     ETTQRAEREV TRMVIIMVIA FLICWLPYAS VAFFIFCNQG SEFGPIFMTI PAFFAKAASL
     YNPLIYILMN KQFRNCMITT ICCGKNPFEE EESTSASASK TEASSVSSSQ VAPA
//