OPSO_RUTRU
ID OPSO_RUTRU Reviewed; 382 AA.
AC Q7T3Q7; Q7T3Q6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Opsin-VA;
DE AltName: Full=Vertebrate ancient opsin;
OS Rutilus rutilus (Roach).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Leuciscidae; Leuciscinae; Rutilus.
OX NCBI_TaxID=48668;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM77793.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Retina {ECO:0000312|EMBL:AAM77793.1};
RX PubMed=12906786; DOI=10.1016/s0960-9822(03)00509-8;
RA Jenkins A., Munoz M., Tarttelin E.E., Bellingham J., Foster R.G.,
RA Hankins M.W.;
RT "VA opsin, melanopsin, and an inherent light response within retinal
RT interneurons.";
RL Curr. Biol. 13:1269-1278(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12906786};
CC IsoId=Q7T3Q7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12906786};
CC IsoId=Q7T3Q7-2; Sequence=VSP_052261, VSP_052262;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of retinal horizontal cells
CC as well as in retinal ganglion cells. {ECO:0000269|PubMed:12906786}.
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; AY116411; AAM77793.1; -; mRNA.
DR EMBL; AY116412; AAM77794.1; -; mRNA.
DR AlphaFoldDB; Q7T3Q7; -.
DR SMR; Q7T3Q7; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002206; Opsin_pineal.
DR InterPro; IPR027430; Retinal_BS.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00666; PINOPSIN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromophore; Disulfide bond;
KW G-protein coupled receptor; Membrane; Photoreceptor protein; Receptor;
KW Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..382
FT /note="Opsin-VA"
FT /id="PRO_0000271191"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 330..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT DISULFID 103..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 304..310
FT /note="FRKCLVQ -> VTLHSCT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12906786"
FT /id="VSP_052261"
FT VAR_SEQ 311..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12906786"
FT /id="VSP_052262"
SQ SEQUENCE 382 AA; 42903 MW; 2B5CB4C056482C1B CRC64;
MELFPVAVNG VSHAEDPFSG PLTFIAPWNY KVLATLMFVV TAASLSENFA VMLVTFRFTQ
LRKPLNYIIV NLSLADFLVS LTGGTISFLT NYHGYFFLGK WACVLEGFAV TYFGIVALWS
LAVLAFERFF VICRPLGNIR LRGKHAALGL LFVWTFSFIW TIPPVLGWSS YTVSKIGTTC
EPNWYSGNFH DHTFIIAFFI TCFILPLGVI VVCYCKLIKK LRKVSNTHGR LGNARKPERQ
VTRMVVVMIV AFMVAWTPYA AFSIVVTAHP SIHLDPRLAA APAFFSKTAA VYNPVIYVFM
NKQFRKCLVQ LLRCRDVTII EGNINQTSER QGMTNESHTG EMSTIASRIP KDGSIPEKTQ
EHPGERRSLA HIPIPENKVC PM
