ID   OPSP_COLLI              Reviewed;         349 AA.
AC   P51476;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pinopsin;
DE   AltName: Full=Pineal gland-specific opsin;
DE            Short=P-opsin;
DE            Short=Pineal opsin;
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Pineal gland;
RX   PubMed=8982090; DOI=10.1016/s0378-1119(96)00476-3;
RA   Kawamura S., Yokoyama S.;
RT   "Molecular characterization of the pigeon P-opsin gene.";
RL   Gene 182:213-214(1996).
CC   -!- FUNCTION: Produces a slow and prolonged phototransduction response
CC       consistent with the non-visual function of pineal photoreception.
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; U50598; AAB40945.1; -; Genomic_DNA.
DR   PIR; JC5490; JC5490.
DR   AlphaFoldDB; P51476; -.
DR   SMR; P51476; -.
DR   eggNOG; KOG3656; Eukaryota.
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:0016037; P:light absorption; IEA:UniProt.
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; IPR002206; Opsin_pineal.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
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   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..349
FT                   /note="Pinopsin"
FT                   /id="PRO_0000197808"
FT   TOPO_DOM        1..32
FT                   /note="Extracellular"
FT   TRANSMEM        33..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..69
FT                   /note="Cytoplasmic"
FT   TRANSMEM        70..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..109
FT                   /note="Extracellular"
FT   TRANSMEM        110..129
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..148
FT                   /note="Cytoplasmic"
FT   TRANSMEM        149..172
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..196
FT                   /note="Extracellular"
FT   TRANSMEM        197..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..246
FT                   /note="Cytoplasmic"
FT   TRANSMEM        247..270
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..278
FT                   /note="Extracellular"
FT   TRANSMEM        279..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..349
FT                   /note="Cytoplasmic"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         290
FT                   /note="N6-(retinylidene)lysine"
FT   LIPID           316
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           317
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        106..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   349 AA;  38364 MW;  A5DF307B428D5E1D CRC64;
     MDPTNSPQEP PHTSTPGPFD GPQWPHQAPR GMYLSVAVLM GIVVISASVV NGLVIVVSIR
     YKKLRSPLNY ILVNLAMADL LVTLCGSSVS FSNNINGFFV FGKRLCELEG FMVSLTGIVG
     LWSLAILALE RYVVVCRPLG DFRFQHRHAV TGCAFTWVWS LLWTTPPLLG WSSYVPEGLR
     TSCGPNWYTG GSNNNSYILT LFVTCFVMPL SLILFSYANL LMTLRAAAAQ QQESDTTQQA
     ERQVTRMVVA MVMAFLICWL PYTTFALVVA TNKDIAIQPA LASLPSYFSK TATVYNPIIY
     VFMNKQFQSC LLKMLCCGHH PRGTGRTAPA APASPTDGLR NKVTPSHPV