OPSB_ANOCA
ID OPSB_ANOCA Reviewed; 355 AA.
AC P51471;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Blue-sensitive opsin;
DE AltName: Full=Blue photoreceptor pigment;
DE AltName: Full=RH2 opsin;
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 [GENOMIC DNA].
RX PubMed=7643409; DOI=10.1007/bf00160506;
RA Kawamura S., Yokoyama S.;
RT "Paralogous origin of the rhodopsinlike opsin genes in lizards.";
RL J. Mol. Evol. 40:594-600(1995).
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)=~503 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S79167; AAB35062.1; -; Genomic_DNA.
DR EMBL; S79124; AAB35062.1; JOINED; Genomic_DNA.
DR EMBL; S79134; AAB35062.1; JOINED; Genomic_DNA.
DR EMBL; S79165; AAB35062.1; JOINED; Genomic_DNA.
DR EMBL; S79166; AAB35062.1; JOINED; Genomic_DNA.
DR PIR; I51319; I51319.
DR RefSeq; NP_001278323.1; NM_001291394.1.
DR AlphaFoldDB; P51471; -.
DR SMR; P51471; -.
DR STRING; 28377.ENSACAP00000015846; -.
DR Ensembl; ENSACAT00000016163; ENSACAP00000015846; ENSACAG00000016065.
DR GeneID; 100553640; -.
DR KEGG; acs:100553640; -.
DR CTD; 42261; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P51471; -.
DR OMA; MSVPAFF; -.
DR OrthoDB; 940057at2759; -.
DR TreeFam; TF324998; -.
DR Proteomes; UP000001646; Chromosome 4.
DR Bgee; ENSACAG00000016065; Expressed in dewlap.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
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:0007601; P:visual perception; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW Receptor; Reference proteome; Retinal protein; Sensory transduction;
KW Transducer; Transmembrane; Transmembrane helix; Vision.
FT CHAIN 1..355
FT /note="Blue-sensitive opsin"
FT /id="PRO_0000197753"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT TRANSMEM 74..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Extracellular"
FT TRANSMEM 114..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT TRANSMEM 153..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..202
FT /note="Extracellular"
FT TRANSMEM 203..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..252
FT /note="Cytoplasmic"
FT TRANSMEM 253..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..284
FT /note="Extracellular"
FT TRANSMEM 285..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..355
FT /note="Cytoplasmic"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 355 AA; 39983 MW; 555B671A4DE96EA6 CRC64;
MNGTEGINFY VPLSNKTGLV RSPFEYPQYY LAEPWKYKVV CCYIFFLIFT GLPINILTLL
VTFKHKKLRQ PLNYILVNLA VADLFMACFG FTVTFYTAWN GYFIFGPIGC AIEGFFATLG
GQVALWSLVV LAIERYIVVC KPMGNFRFSA THALMGISFT WFMSFSCAAP PLLGWSRYIP
EGMQCSCGPD YYTLNPDYHN ESYVLYMFGV HFVIPVVVIF FSYGRLICKV REAAAQQQES
ASTQKAEREV TRMVILMVLG FLLAWTPYAM VAFWIFTNKG VDFSATLMSV PAFFSKSSSL
YNPIIYVLMN KQFRNCMITT ICCGKNPFGD EDVSSSVSQS KTEVSSVSSS QVSPA
