Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-6637-01432
Entry Name
UniProt Accession
Theoretical PI
6.98
Molecular Weight
49835.96
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rhodopsin
Protein Synonyms/Alias
Gene Name
RHO
Gene Synonyms/Alias
Created Date
01-JUL-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
336
Canonical
TFPWVLTCCQFDDKE
[1]
S-Palmitoylation
337
Canonical
FPWVLTCCQFDDKET
[1]
S-Palmitoylation
Organism
Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus)
NCBI Taxa ID
6637
Reference
[1] Kiiver K, Tagen I, Zusinaite E, Tamberg N, Fazakerley JK, Merits A. Propertiesof non-structural protein 1 of Semliki Forest virus and its interference withvirus replication. J Gen Virol. 2008 Jun;89(Pt 6):1457-66. doi:10.1099/vir.0.2008/000299-0.[PMID:18474562]
Functional Description
Visual pigments such as rhodopsin and porphyropsin are light-absorbing molecules that mediate vision. Rhodopsin consists of an apoprotein, opsin, covalently linked to 11-cis-retinal. This receptor is coupled to the activation of phospholipase C. Porphyropsin consists of opsin covalently linked to 11-cis 3,4- didehydroretinal.
Sequence Annotation
Topological domain: 2 33 Extracellular.
Transmembrane: 34 58 Helical; Name=1.
Topological domain: 59 70 Cytoplasmic.
Transmembrane: 71 97 Helical; Name=2.
Topological domain: 98 111 Extracellular.
Transmembrane: 112 131 Helical; Name=3.
Topological domain: 132 151 Cytoplasmic.
Transmembrane: 152 175 Helical; Name=4.
Topological domain: 176 199 Extracellular.
Transmembrane: 200 227 Helical; Name=5.
Topological domain: 228 261 Cytoplasmic.
Transmembrane: 262 285 Helical; Name=6.
Topological domain: 286 293 Extracellular.
Transmembrane: 294 318 Helical; Name=7.
Topological domain: 319 448 Cytoplasmic.
Modified residue: 305 305 N6-(retinylidene)lysine.
Protein Length
448 AA.
Protein Sequence
(Canonical)
MGRDLRDNET WWYNPSIVVH PHWREFDQVP DAVYYSLGIF IGICGIIGCG GNGIVIYLFT  60
KTKSLQTPAN MFIINLAFSD FTFSLVNGFP LMTISCFLKK WIFGFAACKV YGFIGGIFGF  120
MSIMTMAMIS IDRYNVIGRP MAASKKMSHR RAFIMIIFVW LWSVLWAIGP IFGWGAYTLE  180
GVLCNCSFDY ISRDSTTRSN ILCMFILGFF GPILIIFFCY FNIVMSVSNH EKEMAAMAKR  240
LNAKELRKAQ AGANAEMRLA KISIVIVSQF LLSWSPYAVV ALLAQFGPLE WVTPYAAQLP  300
VMFAKASAIH NPMIYSVSHP KFREAISQTF PWVLTCCQFD DKETEDDKDA ETEIPAGESS  360
DAAPSADAAQ MKEMMAMMQK MQQQQAAYPP QGYAPPPQGY PPQGYPPQGY PPQGYPPQGY  420
PPPPQGAPPQ GAPPAAPPQG VDNQAYQA                                     448
FASTA
(Canonical)
>LipidDB-6637-01432|P31356
MGRDLRDNETWWYNPSIVVHPHWREFDQVPDAVYYSLGIFIGICGIIGCGGNGIVIYLFT
KTKSLQTPANMFIINLAFSDFTFSLVNGFPLMTISCFLKKWIFGFAACKVYGFIGGIFGF
MSIMTMAMISIDRYNVIGRPMAASKKMSHRRAFIMIIFVWLWSVLWAIGPIFGWGAYTLE
GVLCNCSFDYISRDSTTRSNILCMFILGFFGPILIIFFCYFNIVMSVSNHEKEMAAMAKR
LNAKELRKAQAGANAEMRLAKISIVIVSQFLLSWSPYAVVALLAQFGPLEWVTPYAAQLP
VMFAKASAIHNPMIYSVSHPKFREAISQTFPWVLTCCQFDDKETEDDKDAETEIPAGESS
DAAPSADAAQMKEMMAMMQKMQQQQAAYPPQGYAPPPQGYPPQGYPPQGYPPQGYPPQGY
PPPPQGAPPQGAPPAAPPQGVDNQAYQA
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW
GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW
GO:0007602; P:phototransduction; IEA:UniProtKB-KW
GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW
GO:0007601; P:visual perception; IEA:UniProtKB-KW
Interpro
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
InterPro; IPR001760; Opsin
InterPro; IPR027430; Retinal_BS
InterPro; IPR006031; XYPPX
Pfam
Pfam; PF00001; 7tm_1;
Pfam; PF02162; XYPPX;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PROSITE; PS00238; OPSIN;
PRINTS
PRINTS; PR00237; GPCRRHODOPSN;
PRINTS; PR00238; OPSIN;