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OPN4L_DANRE
ID   OPN4L_DANRE             Reviewed;         500 AA.
AC   Q1JPS6; Q8AV31;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Melanopsin-like;
DE   AltName: Full=Melanopsin;
DE   AltName: Full=Opsin-4-like;
GN   Name=opn4l; Synonyms=opn4c, opn4m2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAL82577.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Retina {ECO:0000312|EMBL:AAL82577.1};
RX   PubMed=12487121; DOI=10.1016/s0169-328x(02)00454-0;
RA   Bellingham J., Whitmore D., Philp A.R., Wells D.J., Foster R.G.;
RT   "Zebrafish melanopsin: isolation, tissue localisation and phylogenetic
RT   position.";
RL   Brain Res. Mol. Brain Res. 107:128-136(2002).
RN   [2] {ECO:0000312|EMBL:AAI16615.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 a subset of retinal horizontal cells.
CC       {ECO:0000269|PubMed:12487121}.
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; AY078161; AAL82577.1; -; mRNA.
DR   EMBL; BC116614; AAI16615.1; -; mRNA.
DR   RefSeq; NP_840074.2; NM_178289.3.
DR   AlphaFoldDB; Q1JPS6; -.
DR   SMR; Q1JPS6; -.
DR   STRING; 7955.ENSDARP00000002787; -.
DR   PaxDb; Q1JPS6; -.
DR   Ensembl; ENSDART00000018501; ENSDARP00000002787; ENSDARG00000007553.
DR   GeneID; 352918; -.
DR   KEGG; dre:352918; -.
DR   CTD; 352918; -.
DR   ZFIN; ZDB-GENE-030314-2; opn4.1.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234631; -.
DR   HOGENOM; CLU_009579_3_12_1; -.
DR   InParanoid; Q1JPS6; -.
DR   OMA; VRTHEQM; -.
DR   OrthoDB; 911005at2759; -.
DR   PhylomeDB; Q1JPS6; -.
DR   TreeFam; TF324998; -.
DR   PRO; PR:Q1JPS6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000007553; Expressed in head and 13 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0009881; F:photoreceptor activity; IDA:ZFIN.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:ZFIN.
DR   GO; GO:0008377; P:light-induced release of internally sequestered calcium ion; IDA:ZFIN.
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; 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; 1.
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..500
FT                   /note="Melanopsin-like"
FT                   /id="PRO_0000270989"
FT   TOPO_DOM        1..65
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..500
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          404..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         330
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        137..215
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        185
FT                   /note="L -> F (in Ref. 1; AAL82577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="V -> L (in Ref. 1; AAL82577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="S -> SH (in Ref. 1; AAL82577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="S -> P (in Ref. 1; AAL82577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="I -> V (in Ref. 1; AAL82577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  54490 MW;  4D0895F1CAAA12B2 CRC64;
     MSHHSSWRGH HCAPGDINCT AGFKESLGSR NYKLLHVPVH GPTHSHHHDP PHPFPTVDVP
     DHAHYIIGSV ILIVGITGVI GNALVVYVFC RSRTLRTAGN MFIVNLAVAD FLMSVTQSPV
     FFAASLHRRW VFGERPCELY AFCGALFGIC SMMTLTAIAA DRCLAITQPL ALVSRVSRRK
     AGAVLVVVWL YSLGWSLPPF FGWSAYVPEG LQTSCSWDYM TFTPSVRAYT ILLFVFVFFI
     PLGIIGSCYF AIFQTIRAAG KEIRELDCGE THKVYERMQN EWKMAKVALV VIVLFIISWS
     PYSVVALTAT AGYSHFLTPY MNSVPAVIAK ASAIHNPIIY AITHPKYRVA IARYIPVLRP
     ILRVKEKDLR SSFSSGSVSS RRPTLTSQCS LGVSMGNAAR ANGRWGKTRL SSASDSDSCW
     TESEADGSSV SSLTFGRRVS TEISTDTVIL SSGSSVSNAS GQKSERAHKV ISVPVPSITF
     ETDAADGESL SDGKALLGGN
 
 
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