OPS2_MANSE
ID OPS2_MANSE Reviewed; 377 AA.
AC O02465;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Opsin-2;
DE Short=MANOP2 {ECO:0000303|PubMed:9343857};
DE AltName: Full=Rhodopsin 2, short-wavelength {ECO:0000303|PubMed:9343857};
DE AltName: Full=Rhodopsin P357 {ECO:0000303|PubMed:12939366};
GN Name=OP2;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1] {ECO:0000312|EMBL:AAD11965.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina {ECO:0000312|EMBL:AAD11965.1};
RX PubMed=9343857; DOI=10.1242/jeb.200.18.2469;
RA Chase M.R., Bennett R.R., White R.H.;
RT "Three opsin-encoding cDNAS from the compound eye of Manduca sexta.";
RL J. Exp. Biol. 200:2469-2478(1997).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RC TISSUE=Retina {ECO:0000269|PubMed:12939366};
RX PubMed=12939366; DOI=10.1242/jeb.00571;
RA White R.H., Xu H., Munch T.A., Bennett R.R., Grable E.A.;
RT "The retina of Manduca sexta: rhodopsin expression, the mosaic of green-,
RT blue- and UV-sensitive photoreceptors, and regional specialization.";
RL J. Exp. Biol. 206:3337-3348(2003).
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. May play a role in photoperiodic photoreception.
CC {ECO:0000250|UniProtKB:Q95YI3, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the retina, expression is essentially uniformly
CC distributed, but a higher level is seen in the dorsal region of the
CC retina and in the dorsal rim retinulae. {ECO:0000269|PubMed:12939366}.
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; L78081; AAD11965.1; -; mRNA.
DR AlphaFoldDB; O02465; -.
DR SMR; O02465; -.
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 GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000856; Opsin_RH3/RH4.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00577; OPSINRH3RH4.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW Vision.
FT CHAIN 1..377
FT /note="Opsin-2"
FT /id="PRO_0000389623"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..146
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 355..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 377 AA; 41201 MW; 9B7708E2CA61BC36 CRC64;
MNNQSENYYH GAQFEALKSA GAIEMLGDGL TGDDLAAIPE HWLSYPAPPA SAHTALALLY
IFFTFAALVG NGMVIFIFST TKSLRTSSNF LVLNLAILDF IMMAKAPIFI YNSAMRGFAV
GTVGCQIFAL MGAYSGIGAG MTNACIAYDR HSTITRPLDG RLSEGKVLLM VAFVWIYSTP
WALLPLLKIW GRYVPEGYLT SCSFDYLTNT FDTKLFVACI FTCSYVFPMS LIIYFYSGIV
KQVFAHEAAL REQAKKMNVE SLRANQGGSS ESAEIRIAKA ALTVCFLFVA SWTPYGVMAL
IGAFGNQQLL TPGVTMIPAV ACKAVACISP WVYAIRHPMY RQELQRRMPW LQIDEPDDTV
STATSNTTNS APPAATA
