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Rhodopsin

 OPSD_CALPD              Reviewed;         348 AA.
Q6W3E1;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-NOV-2018, entry version 56.
RecName: Full=Rhodopsin;
Name=RHO; Synonyms=RH1;
Caluromys philander (Bare-tailed woolly opossum).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Metatheria; Didelphimorphia; Didelphidae; Caluromys.
NCBI_TaxID=70610;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=14659889; DOI=10.1016/j.gene.2003.09.016;
Hunt D.M., Arrese C.A., von Dornum M., Rodger J., Oddy A.,
Cowing J.A., Ager E.I., Bowmaker J.K., Beazley L.D., Shand J.;
"The rod opsin pigments from two marsupial species, the South American
bare-tailed woolly opossum and the Australian fat-tailed dunnart.";
Gene 323:157-162(2003).
-!- FUNCTION: Photoreceptor required for image-forming vision at low
light intensity. Required for photoreceptor cell viability after
birth (By similarity). Light-induced isomerization of 11-cis to
all-trans retinal triggers a conformational change that activates
signaling via G-proteins. Subsequent receptor phosphorylation
mediates displacement of the bound G-protein alpha subunit by the
arrestin SAG and terminates signaling (By similarity).
{ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100}.
-!- SUBUNIT: Homodimer. Interacts (phosphorylated form) with SAG.
Interacts with GNAT1, Interacts with GNAT3. SAG and G-proteins
compete for a common binding site. Interacts with GRK1 (By
similarity). {ECO:0000250|UniProtKB:P02699,
ECO:0000250|UniProtKB:P08100}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell
projection, cilium, photoreceptor outer segment
{ECO:0000250|UniProtKB:P02699}. Note=Synthesized in the inner
segment (IS) of rod photoreceptor cells before vectorial transport
to disk membranes in the rod outer segment (OS) photosensory
cilia. {ECO:0000250|UniProtKB:P08100}.
-!- PTM: Phosphorylated on some or all of the serine and threonine
residues present in the C-terminal region.
{ECO:0000250|UniProtKB:P02699}.
-!- PTM: Contains one covalently linked retinal chromophore. Upon
light absorption, the covalently bound 11-cis-retinal is converted
to all-trans-retinal. After hydrolysis of the Schiff base and
release of the covalently bound all-trans-retinal, active
rhodopsin is regenerated by binding of a fresh molecule of 11-cis-
retinal. {ECO:0000250|UniProtKB:P02699}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Opsin subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AY313946; AAQ82903.1; -; mRNA.
ProteinModelPortal; Q6W3E1; -.
HOVERGEN; HBG107442; -.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
GO; GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR001760; Opsin.
InterPro; IPR027430; Retinal_BS.
InterPro; IPR000732; Rhodopsin.
InterPro; IPR019477; Rhodopsin_N.
Pfam; PF00001; 7tm_1; 1.
Pfam; PF10413; Rhodopsin_N; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00238; OPSIN.
PRINTS; PR00579; RHODOPSIN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE; PS00238; OPSIN; 1.
2: Evidence at transcript level;
Acetylation; Cell projection; Chromophore; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein;
Receptor; Retinal protein; Sensory transduction; Transducer;
Transmembrane; Transmembrane helix; Vision; Zinc.
CHAIN 1 348 Rhodopsin.
/FTId=PRO_0000227017.
TOPO_DOM 1 36 Extracellular. {ECO:0000305}.
TRANSMEM 37 61 Helical; Name=1.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 62 73 Cytoplasmic. {ECO:0000305}.
TRANSMEM 74 96 Helical; Name=2.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 97 110 Extracellular. {ECO:0000305}.
TRANSMEM 111 133 Helical; Name=3.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 134 152 Cytoplasmic. {ECO:0000305}.
TRANSMEM 153 173 Helical; Name=4.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 174 202 Extracellular. {ECO:0000305}.
TRANSMEM 203 224 Helical; Name=5.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 225 252 Cytoplasmic. {ECO:0000305}.
TRANSMEM 253 274 Helical; Name=6.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 275 286 Extracellular. {ECO:0000305}.
TRANSMEM 287 308 Helical; Name=7.
{ECO:0000250|UniProtKB:P02699}.
TOPO_DOM 309 348 Cytoplasmic. {ECO:0000305}.
REGION 330 348 Interaction with SAG.
{ECO:0000250|UniProtKB:P02699}.
MOTIF 134 136 'Ionic lock' involved in activated form
stabilization.
{ECO:0000250|UniProtKB:P02699}.
METAL 201 201 Zinc. {ECO:0000250|UniProtKB:P02699}.
METAL 279 279 Zinc. {ECO:0000250|UniProtKB:P02699}.
SITE 113 113 Plays an important role in the
conformation switch to the active
conformation.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 296 296 N6-(retinylidene)lysine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000250|UniProtKB:P02700}.
MOD_RES 336 336 Phosphothreonine.
{ECO:0000250|UniProtKB:P02700}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000250|UniProtKB:P02700}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 342 342 Phosphothreonine.
{ECO:0000250|UniProtKB:P02699}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:P02699}.
LIPID 322 322 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P02699}.
LIPID 323 323 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P02699}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 110 187 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 348 AA; 38921 MW; 5BD17A0FA2A29ACD CRC64;
MNGTEGPNFY VPFSNKTGVV RSPFEEPQYY LAEPWQFSCL AAYMFMLIVL GFPINFLTLY
VTIQHKKLRT PLNYILLNLA IADLFMVFGG FTTTLYTSLH GYFVFGPTGC DLEGFFATLG
GEIALWSLVV LAIERYIVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLVGWSRYIP
EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMVVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIA FLICWLPYAG VAFYIFTHQG SNFGPILMTL PAFFAKTSAV
YNPVIYIMLN KQFRTCMLTT LCCGKIPLGD DEASATASKT ETSQVAPA


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Catalog number Product name Quantity
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