ID   OPSP_ICTPU              Reviewed;         346 AA.
AC   O42266;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Parapinopsin;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9334384; DOI=10.1523/jneurosci.17-21-08083.1997;
RA   Blackshaw S., Snyder S.H.;
RT   "Parapinopsin, a novel catfish opsin localized to the parapineal organ,
RT   defines a new gene family.";
RL   J. Neurosci. 17:8083-8092(1997).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Parapineal organ.
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}.
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; AF028014; AAB84050.1; -; mRNA.
DR   RefSeq; NP_001187002.1; NM_001200073.1.
DR   AlphaFoldDB; O42266; -.
DR   SMR; O42266; -.
DR   GeneID; 100304471; -.
DR   KEGG; ipu:100304471; -.
DR   CTD; 100331083; -.
DR   OrthoDB; 704940at2759; -.
DR   Proteomes; UP000221080; Chromosome 5.
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   2: Evidence at transcript 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..346
FT                   /note="Parapinopsin"
FT                   /id="PRO_0000197809"
FT   TOPO_DOM        1..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..169
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..221
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..268
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          325..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         288
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   LIPID           315
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   346 AA;  38203 MW;  A70871684F8FC7FD CRC64;
     MASIILINFS ETDTLHLGSV NDHIMPRIGY TILSIIMALS STFGIILNMV VIIVTVRYKQ
     LRQPLNYALV NLAVADLGCP VFGGLLTAVT NAMGYFSLGR VGCVLEGFAV AFFGIAGLCS
     VAVIAVDRYM VVCRPLGAVM FQTKHALAGV VFSWVWSFIW NTPPLFGWGS YQLEGVMTSC
     APNWYRRDPV NVSYILCYFM LCFALPFATI IFSYMHLLHT LWQVAKLQVA DSGSTAKVEV
     QVARMVVIMV MAFLLTWLPY AAFALTVIID SNIYINPVIG TIPAYLAKSS TVFNPIIYIF
     MNRQFRDYAL PCLLCGKNPW AAKEGRDSDT NTLTTTVSKN TSVSPL