ID   REIS_TODPA              Reviewed;         301 AA.
AC   P23820;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Retinochrome;
DE   AltName: Full=Retinal photoisomerase;
OS   Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae; Todarodes.
OX   NCBI_TaxID=6637;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2226795; DOI=10.1016/0014-5793(90)80383-t;
RA   Hara-Nishimura I., Matsumoto T., Mori H., Nishimura M., Hara R., Hara T.;
RT   "Cloning and nucleotide sequence of cDNA for retinochrome, retinal
RT   photoisomerase from the squid retina.";
RL   FEBS Lett. 271:106-110(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15 AND 114-128.
RC   TISSUE=Retina;
RA   Uematsu J., Hara-Nishimura I., Wada K., Matsubara H., Hara T.;
RT   "Amino-terminal sequence of squid retinochrome.";
RL   Photobiochem. Photobiophys. 13:197-201(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 274-281, AND RETINAL-BINDING SITE.
RC   TISSUE=Retina;
RX   PubMed=8243675; DOI=10.1016/0014-5793(93)80447-3;
RA   Hara-Nishimura I., Kondo M., Nishimura M., Hara R., Hara T.;
RT   "Amino acid sequence surrounding the retinal-binding site in retinochrome
RT   of the squid, Todarodes pacificus.";
RL   FEBS Lett. 335:94-98(1993).
CC   -!- FUNCTION: Retinochrome is capable of acting as an effective catalyst in
CC       the light to convert various isomers of retinal into 11-cis, the form
CC       that is required by opsin to resynthesize rhodopsin.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Mainly stored in myeloid bodies of the inner
CC       segments.
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; X57143; CAA40422.1; -; mRNA.
DR   PIR; S12864; S12864.
DR   AlphaFoldDB; P23820; -.
DR   SMR; P23820; -.
DR   BioCyc; MetaCyc:MON-17359; -.
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; IPR027430; Retinal_BS.
DR   InterPro; IPR032972; RRH.
DR   PANTHER; PTHR24240:SF77; PTHR24240:SF77; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Direct protein sequencing; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..301
FT                   /note="Retinochrome"
FT                   /id="PRO_0000197812"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..94
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..120
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..255
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..289
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..301
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         275
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000269|PubMed:8243675"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   301 AA;  33490 MW;  CBB37317486B27FC CRC64;
     MFGNPAMTGL HQFTMWEHYF TGSIYLVLGC VVFSLCGMCI IFLARQSPKP RRKYAILIHV
     LITAMAVNGG DPAHASSSIV GRWLYGSVGC QLMGFWGFFG GMSHIWMLFA FAMERYMAVC
     HREFYQQMPS VYYSIIVGLM YTFGTFWATM PLLGWASYGL EVHGTSCTIN YSVSDESYQS
     YVFFLAIFSF IFPMVSGWYA ISKAWSGLSA IPDAEKEKDK DILSEEQLTA LAGAFILISL
     ISWSGFGYVA IYSALTHGGA QLSHLRGHVP PIMSKTGCAL FPLLIFLLTA RSLPKSDTKK
     P