ID   OPSP_CHICK              Reviewed;         351 AA.
AC   P51475; P79794;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Pinopsin;
DE   AltName: Full=Pineal gland-specific opsin;
DE            Short=P-opsin;
DE            Short=Pineal opsin;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pineal gland;
RX   PubMed=7878470; DOI=10.1126/science.7878470;
RA   Max M., McKinnon P.J., Seidenman K.J., Barrett R.K., Applebury M.L.,
RA   Takahashi J.S., Margolskee R.F.;
RT   "Pineal opsin: a nonvisual opsin expressed in chick pineal.";
RL   Science 267:1502-1506(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pineal gland;
RX   PubMed=7969427; DOI=10.1038/372094a0;
RA   Okano T., Yoshizawa T., Fukada Y.;
RT   "Pinopsin is a chicken pineal photoreceptive molecule.";
RL   Nature 372:94-97(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=White leghorn; TISSUE=Pineal gland;
RX   PubMed=9756926; DOI=10.1074/jbc.273.41.26820;
RA   Max M., Surya A., Takahashi J.S., Margolskee R.F., Knox B.E.;
RT   "Light-dependent activation of rod transducin by pineal opsin.";
RL   J. Biol. Chem. 273:26820-26826(1998).
CC   -!- FUNCTION: Produces a slow and prolonged phototransduction response
CC       consistent with the non-visual function of pineal photoreception.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=~470 nm;
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; U15762; AAA64223.1; -; mRNA.
DR   EMBL; U87449; AAB47565.1; -; Genomic_DNA.
DR   PIR; A55962; A55962.
DR   RefSeq; NP_990740.1; NM_205409.2.
DR   AlphaFoldDB; P51475; -.
DR   SMR; P51475; -.
DR   STRING; 9031.ENSGALP00000007864; -.
DR   PaxDb; P51475; -.
DR   GeneID; 396377; -.
DR   KEGG; gga:396377; -.
DR   CTD; 102096571; -.
DR   VEuPathDB; HostDB:geneid_396377; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_009579_3_0_1; -.
DR   InParanoid; P51475; -.
DR   OrthoDB; 940057at2759; -.
DR   PhylomeDB; P51475; -.
DR   TreeFam; TF324998; -.
DR   PRO; PR:P51475; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0036064; C:ciliary basal body; IDA:AgBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042599; C:lamellar body; IDA:AgBase.
DR   GO; GO:0097232; C:lamellar body membrane; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
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; IDA: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:0007602; P:phototransduction; IBA:GO_Central.
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; Reference proteome; Retinal protein; Sensory transduction;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..351
FT                   /note="Pinopsin"
FT                   /id="PRO_0000197807"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT   TRANSMEM        31..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..67
FT                   /note="Cytoplasmic"
FT   TRANSMEM        68..92
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..107
FT                   /note="Extracellular"
FT   TRANSMEM        108..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..146
FT                   /note="Cytoplasmic"
FT   TRANSMEM        147..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..194
FT                   /note="Extracellular"
FT   TRANSMEM        195..222
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..244
FT                   /note="Cytoplasmic"
FT   TRANSMEM        245..268
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..276
FT                   /note="Extracellular"
FT   TRANSMEM        277..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..351
FT                   /note="Cytoplasmic"
FT   MOD_RES         288
FT                   /note="N6-(retinylidene)lysine"
FT   LIPID           314
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           315
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        28
FT                   /note="Q -> W (in Ref. 3; AAB47565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="K -> R (in Ref. 2; AAA64223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="A -> T (in Ref. 2; AAA64223)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  38174 MW;  56BDFAD187008338 CRC64;
     MSSNSSQAPP NGTPGPFDGP QWPYQAPQST YVGVAVLMGT VVACASVVNG LVIVVSICYK
     KLRSPLNYIL VNLAVADLLV TLCGSSVSLS NNINGFFVFG RRMCELEGFM VSLTGIVGLW
     SLAILALERY VVVCKPLGDF QFQRRHAVSG CAFTWGWALL WSAPPLLGWS SYVPEGLRTS
     CGPNWYTGGS NNNSYILSLF VTCFVLPLSL ILFSYTNLLL TLRAAAAQQK EADTTQRAER
     EVTRMVIVMV MAFLLCWLPY STFALVVATH KGIIIQPVLA SLPSYFSKTA TVYNPIIYVF
     MNKQFQSCLL EMLCCGYQPQ RTGKASPGTP GPHADVTAAG LRNKVMPAHP V