OPSR_ANOCA
ID OPSR_ANOCA Reviewed; 369 AA.
AC P41592;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Red-sensitive opsin;
DE AltName: Full=Red cone photoreceptor pigment;
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8500618; DOI=10.1016/0014-5793(93)81350-9;
RA Kawamura S., Yokoyama S.;
RT "Molecular characterization of the red visual pigment gene of the American
RT chameleon (Anolis carolinensis).";
RL FEBS Lett. 323:247-251(1993).
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. This opsin uses a vitamin A2 chromophore.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=625 nm;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000250}.
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; U08131; AAA17706.1; -; Unassigned_DNA.
DR PIR; S33250; S33250.
DR RefSeq; XP_008102123.1; XM_008103916.2.
DR AlphaFoldDB; P41592; -.
DR SMR; P41592; -.
DR STRING; 28377.ENSACAP00000012416; -.
DR Ensembl; ENSACAT00000012669; ENSACAP00000012416; ENSACAG00000012605.
DR GeneID; 100564371; -.
DR KEGG; acs:100564371; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P41592; -.
DR OMA; YNITTVW; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000012605; Expressed in dewlap.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:AgBase.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0031982; C:vesicle; ISS:AgBase.
DR GO; GO:0031404; F:chloride ion binding; ISS:AgBase.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0016037; P:light absorption; ISS:AgBase.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0070207; P:protein homotrimerization; ISS:AgBase.
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; IPR000378; Opsin_red/grn.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00575; OPSINREDGRN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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 Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..369
FT /note="Red-sensitive opsin"
FT /id="PRO_0000197791"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT TRANSMEM 56..80
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..92
FT /note="Cytoplasmic"
FT TRANSMEM 93..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..132
FT /note="Extracellular"
FT TRANSMEM 133..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..171
FT /note="Cytoplasmic"
FT TRANSMEM 172..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..221
FT /note="Extracellular"
FT TRANSMEM 222..249
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..271
FT /note="Cytoplasmic"
FT TRANSMEM 272..295
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..303
FT /note="Extracellular"
FT TRANSMEM 304..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..369
FT /note="Cytoplasmic"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 369 AA; 40844 MW; D51E194661622B5E CRC64;
MAGTVTEAWD VAVFAARRRN DEDDTTRDSL FTYTNSNNTR GPFEGPNYHI APRWVYNITS
VWMIFVVIAS IFTNGLVLVA TAKFKKLRHP LNWILVNLAI ADLGETVIAS TISVINQISG
YFILGHPMCV LEGYTVSTCG ISALWSLAVI SWERWVVVCK PFGNVKFDAK LAVAGIVFSW
VWSAVWTAPP VFGWSRYWPH GLKTSCGPDV FSGSDDPGVL SYMIVLMITC CFIPLAVILL
CYLQVWLAIR AVAAQQKESE STQKAEKEVS RMVVVMIIAY CFCWGPYTVF ACFAAANPGY
AFHPLAAALP AYFAKSATIY NPIIYVFMNR QFRNCIMQLF GKKVDDGSEL SSTSRTEVSS
VSNSSVSPA
