OPN4A_GADMO
ID OPN4A_GADMO Reviewed; 561 AA.
AC Q804X9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Melanopsin-A;
DE AltName: Full=Opsin-4A;
GN Name=opn4a;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO20043.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12508316; DOI=10.1002/cne.10523;
RA Drivenes O., Soviknes A.M., Ebbesson L.O., Fjose A., Seo H.C., Helvik J.V.;
RT "Isolation and characterization of two teleost melanopsin genes and their
RT differential expression within the inner retina and brain.";
RL J. Comp. Neurol. 456:84-93(2003).
CC -!- FUNCTION: Photoreceptor implicated in non-image-forming responses to
CC light. {ECO:0000250|UniProtKB:Q9QXZ9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9QXZ9};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in retina and brain. Expressed in a
CC subset of retinal horizontal cells as well as a small number of
CC amacrine and retinal ganglion cells. Also expressed in a small
CC population of neurons in the suprachiasmatic nucleus (SNC).
CC {ECO:0000269|PubMed:12508316}.
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; AF385823; AAO20043.1; -; mRNA.
DR AlphaFoldDB; Q804X9; -.
DR SMR; Q804X9; -.
DR PRIDE; Q804X9; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 2.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chromophore; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Melanopsin-A"
FT /id="PRO_0000270990"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 359..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 299
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 561 AA; 62650 MW; 0A4BF62570AFF648 CRC64;
MRPSTDTMEA DTAATHRNFI TKVDVPDHAH YTVAFFVSVI GTLGVTGNAL VQFAFYSNKK
LRNLPNYFIM NQAASDFLMA FTQSPFFFIN CLNREWIFGE LGCKLYAFLG ALFGITSMIN
LLAISLDRYM VITRPLEAMK WNSKRRTTIA ILLVWLYSLA WSLAPLVGWS SYIPEGLRTS
CTWDYVTYTA SNRSYTMMLC CFVFFIPLAI ISYCYLFMFL AIRKTSRDVE RLGIQVRKST
IIRQKSIRTE WKLAKIAFVV IVVYVLSWSP YACVTMISWS GHANILSPYS KTVPAVIAKA
STIYNPFIYA IIHQKYRKTL ADKVPCLRFL APNKRKDCTS SSFSGSSYRD SVISRTSTAI
RRQSTAASRH ASASKTAAGA SSYSSSDRVF GDVEMDPIDW RSGASFRRHS SRGSTRRDRL
LKKQQMERTN KSAAHKQPSP STKMSATHCK NKTVSSSVNM AAAPPQLVLI RKRSQSLTNG
LSDAGKKTTV ANGTPGNHKS KSADLHFRNL PALDQALNVP RIIVISPTSE DCLVKHESSF
TDDGSVGTVV DEDSLEDNDV V
