ID   OPSP_PETMA              Reviewed;         444 AA.
AC   O42490;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Pineal opsin;
DE   AltName: Full=Pineal gland-specific opsin;
DE            Short=P-opsin;
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9427550; DOI=10.1016/s0378-1119(97)00458-7;
RA   Yokoyama S., Zhang H.;
RT   "Cloning and characterization of the pineal gland-specific opsin gene of
RT   marine lamprey (Petromyzon marinus).";
RL   Gene 202:89-93(1997).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Pineal gland.
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; U90671; AAC41240.1; -; Genomic_DNA.
DR   EMBL; U90667; AAC41240.1; JOINED; Genomic_DNA.
DR   EMBL; U90668; AAC41240.1; JOINED; Genomic_DNA.
DR   EMBL; U90669; AAC41240.1; JOINED; Genomic_DNA.
DR   EMBL; U90670; AAC41240.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; O42490; -.
DR   SMR; O42490; -.
DR   STRING; 7757.ENSPMAP00000008192; -.
DR   TreeFam; TF324998; -.
DR   Proteomes; UP000245300; Unplaced.
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:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
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.
FT   CHAIN           1..444
FT                   /note="Pineal opsin"
FT                   /id="PRO_0000197810"
FT   TOPO_DOM        1..46
FT                   /note="Extracellular"
FT   TRANSMEM        47..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..83
FT                   /note="Cytoplasmic"
FT   TRANSMEM        84..108
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..123
FT                   /note="Extracellular"
FT   TRANSMEM        124..143
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..162
FT                   /note="Cytoplasmic"
FT   TRANSMEM        163..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..210
FT                   /note="Extracellular"
FT   TRANSMEM        211..238
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..260
FT                   /note="Cytoplasmic"
FT   TRANSMEM        261..284
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..292
FT                   /note="Extracellular"
FT   TRANSMEM        293..317
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..444
FT                   /note="Cytoplasmic"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         304
FT                   /note="N6-(retinylidene)lysine"
FT   LIPID           331
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        120..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   444 AA;  48080 MW;  4F62BDA3BA925600 CRC64;
     MDALQESPPS HHSLPSALPS ATGGNGTVAT MHNPFERPLE GIAPWNFTML AALMGTITAL
     SLGENFAVIV VTARFRQLRQ PLNYVLVNLA AADLLVSAIG GSVSFFTNIK GYFFLGVHAC
     VLEGFAVTYF GVVALWSLAL LAFERYFVIC RPLGNFRLQS KHAVLGLAVV WVFSLACTLP
     PVLGWSSYRP SMIGTTCEPN WYSGELHDHT FILMFFSTCF IFPLAVIFFS YGKLIQKLKK
     ASETQRGLES TRRAEQQVTR MVVVMILAFL VCWMPYATFS IVVTACPTIH LDPLLAAVPA
     FFSKTATVYN PVIYIFMNKQ FRDCFVQVLP CKGLKKVSAT QTAGAQDTEH TASVNTQSPG
     NRHNIALAAG SLRFTGAVAP SPATGVVEPT MSAAGSMGAP PNKSTAPCQQ QGQQQQQQGT
     PIPAITHVQP LLTHSESVSK ICPV