ID   A0A897TIV4_NANAN        Unreviewed;       352 AA.
AC   A0A897TIV4;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   27-NOV-2024, entry version 14.
DE   RecName: Full=Rhodopsin {ECO:0000256|RuleBase:RU004951};
GN   Name=rh2a-beta {ECO:0000313|EMBL:QSG73667.1};
OS   Nannacara anomala (Goldeneye cichlid).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Cichlasomatini; Nannacara.
OX   NCBI_TaxID=168802 {ECO:0000313|EMBL:QSG73667.1};
RN   [1] {ECO:0000313|EMBL:QSG73667.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=33619757;
RA   Torres-Dowdall J., Karagic N., Harer A., Meyer A.;
RT   "Diversity in visual sensitivity across Neotropical cichlid fishes via
RT   differential expression and intraretinal variation of opsin genes.";
RL   Mol. Ecol. 0:0-0(2021).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently linked
CC       to cis-retinal. {ECO:0000256|ARBA:ARBA00002881}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
CC   -!- PTM: Contains one covalently linked retinal chromophore.
CC       {ECO:0000256|PIRSR:PIRSR600732-50}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC       subfamily. {ECO:0000256|RuleBase:RU004951}.
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DR   EMBL; MW588232; QSG73667.1; -; mRNA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:TreeGrafter.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071482; P:cellular response to light stimulus; IEA:TreeGrafter.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   FunFam; 1.20.1070.10:FF:000018; Rhodopsin; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR050125; GPCR_opsins.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR027430; Retinal_BS.
DR   InterPro; IPR000732; Rhodopsin.
DR   InterPro; IPR019477; Rhodopsin_N.
DR   PANTHER; PTHR24240:SF153; GREEN-SENSITIVE OPSIN; 1.
DR   PANTHER; PTHR24240; OPSIN; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF10413; Rhodopsin_N; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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 {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|PIRSR:PIRSR600732-
KW   50};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR600732-3};
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW   ECO:0000256|RuleBase:RU004951};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR600732-
KW   4};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004951};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600732-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543,
KW   ECO:0000256|RuleBase:RU004951};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004951};
KW   Retinal protein {ECO:0000256|ARBA:ARBA00022925,
KW   ECO:0000256|PIRSR:PIRSR600732-50};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606,
KW   ECO:0000256|RuleBase:RU004951};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004951};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004951};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004951}; Vision {ECO:0000256|ARBA:ARBA00023305};
KW   Zinc {ECO:0000256|PIRSR:PIRSR600732-1}.
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        262..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   TRANSMEM        291..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004951"
FT   DOMAIN          62..314
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-1"
FT   SITE            121
FT                   /note="Plays an important role in the conformation switch
FT                   to the active conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-2"
FT   MOD_RES         304
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-50"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-4"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-4"
FT   DISULFID        118..195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600732-3"
SQ   SEQUENCE   352 AA;  38459 MW;  5554DFD35D2A6627 CRC64;
     MGWDGGIEPN GTEGKNFYIP MSNRTGIVRS PFEYPXXXXX XXXXXXXXAF YMFFLICTGT
     PINGLTLFVT AQNKKLRQPL NYILVNLAVA GLIMCCFGFT ITLTSALNGY FILGPTFCAI
     EGFMATLGGE VALWSLVVLA IERYVVVCKP MGSFKFSGTH AGAGVLFTWI MAMACAGPPL
     FGWSRYIPEG MQCSCGPDYY TLAPGFNNES YVIYMFVVHF FIPVFVIFFT YGSLVMTVKA
     AAAQQQDSAS TQKAEKEVTR MCILMVLGFL VAWTPYASFA GWIFLNKGAS FSALTAALPA
     FFAKSSALYN PIIYVLMNKQ FRNCMLSTIG MGGMVEDETS VSASKTEVSS VS
//