OPSB_RAT
ID OPSB_RAT Reviewed; 346 AA.
AC Q63652; O70363;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Short-wave-sensitive opsin 1;
DE Short=S opsin;
DE AltName: Full=Blue cone photoreceptor pigment;
DE AltName: Full=Blue-sensitive opsin;
DE Short=BOP;
DE AltName: Full=Short wavelength-sensitive cone opsin;
GN Name=Opn1sw; Synonyms=Bcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX PubMed=9147475; DOI=10.1017/s0952523800011366;
RA Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H.,
RA Palczewski K.;
RT "Molecular cloning and localization of rhodopsin kinase in the mammalian
RT pineal.";
RL Vis. Neurosci. 14:225-232(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RA Delahaye-Brown A.-M.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Required for the maintenance of cone
CC outer segment organization in the ventral retina, but not essential for
CC the maintenance of functioning cone photoreceptors (By similarity).
CC Involved in ensuring correct abundance and localization of retinal
CC membrane proteins (By similarity). May increase spectral sensitivity in
CC dim light (By similarity). {ECO:0000250|UniProtKB:P03999,
CC ECO:0000250|UniProtKB:P51491}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P03999};
CC Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplasm, perinuclear
CC region {ECO:0000250|UniProtKB:P03999}.
CC -!- TISSUE SPECIFICITY: Expressed in cone photoreceptor cells.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region.
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; U63972; AAB05931.1; -; mRNA.
DR EMBL; AF051163; AAC05294.1; -; mRNA.
DR RefSeq; NP_112277.1; NM_031015.1.
DR AlphaFoldDB; Q63652; -.
DR SMR; Q63652; -.
DR STRING; 10116.ENSRNOP00000009278; -.
DR GlyGen; Q63652; 1 site.
DR PhosphoSitePlus; Q63652; -.
DR PaxDb; Q63652; -.
DR GeneID; 81644; -.
DR KEGG; rno:81644; -.
DR UCSC; RGD:621033; rat.
DR CTD; 611; -.
DR RGD; 621033; Opn1sw.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q63652; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; Q63652; -.
DR Reactome; R-RNO-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-419771; Opsins.
DR PRO; PR:Q63652; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
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; IPR001521; Opsin_blue.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00574; OPSINBLUE.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chromophore; Cytoplasm; 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..346
FT /note="Short-wave-sensitive opsin 1"
FT /id="PRO_0000197767"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT TRANSMEM 32..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..68
FT /note="Cytoplasmic"
FT TRANSMEM 69..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..108
FT /note="Extracellular"
FT TRANSMEM 109..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..147
FT /note="Cytoplasmic"
FT TRANSMEM 148..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..197
FT /note="Extracellular"
FT TRANSMEM 198..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..247
FT /note="Cytoplasmic"
FT TRANSMEM 248..271
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..279
FT /note="Extracellular"
FT TRANSMEM 280..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..346
FT /note="Cytoplasmic"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="N6-(retinylidene)lysine"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 105..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 70
FT /note="I -> V (in Ref. 2; AAC05294)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="F -> L (in Ref. 2; AAC05294)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="Y -> D (in Ref. 2; AAC05294)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="G -> S (in Ref. 2; AAC05294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 39062 MW; 6DE181761AD4F296 CRC64;
MSGEDEFYLF QNISSVGPWD GPQYHIAPVW AFHLQAAFMG FVFFAGTPLN ATVLVATLHY
KKLRQPLNYI LVNVSLGGFL FCIFSVFTVF IASCHGYFLF GRHVCALEAF LGSVAGLVTG
WSLAFLAFER YLVICKPFGN IRFNSKHALT VVLITWTIGI GVSIPPFFGW SRFIPEGLQC
SCGPDWYTVG TKYRSEHYTW FLFIFCFIIP LSLICFSYFQ LLRTLRAVAA QQQESATTQK
AEREVSHMVV VMVGSFCLCY VPYAALAMYM VNNRNHGLYL RLVTIPAFFS KSSCVYNPII
YCFMNKQFRA CILEMVCRKP MTDESDMSGS QKTEVSTVSS SKVGPH
