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OPSB_ASTFA
ID   OPSB_ASTFA              Reviewed;         355 AA.
AC   P51472;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Blue-sensitive opsin;
DE   AltName: Full=Blue cone photoreceptor pigment;
GN   Name=B23;
OS   Astyanax fasciatus (Blind cave fish) (Astyanax mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Psalidodon.
OX   NCBI_TaxID=223369;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Eye;
RX   PubMed=8224220; DOI=10.1016/0014-5793(93)81673-n;
RA   Yokoyama R., Yokoyama S.;
RT   "Molecular characterization of a blue visual pigment gene in the fish
RT   Astyanax fasciatus.";
RL   FEBS Lett. 334:27-31(1993).
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.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: The color pigments are found in the cone
CC       photoreceptor cells.
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}.
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DR   EMBL; AF134766; AAB28911.1; -; Genomic_DNA.
DR   EMBL; AF134762; AAB28911.1; JOINED; Genomic_DNA.
DR   EMBL; AF134763; AAB28911.1; JOINED; Genomic_DNA.
DR   EMBL; AF134764; AAB28911.1; JOINED; Genomic_DNA.
DR   EMBL; AF134765; AAB28911.1; JOINED; Genomic_DNA.
DR   PIR; S39028; S39028.
DR   AlphaFoldDB; P51472; -.
DR   SMR; P51472; -.
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; IPR001760; Opsin.
DR   InterPro; IPR001521; Opsin_blue.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00574; OPSINBLUE.
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   Membrane; Phosphoprotein; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..355
FT                   /note="Blue-sensitive opsin"
FT                   /id="PRO_0000197754"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..66
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..78
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..104
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..138
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..314
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          334..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         301
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        115..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   355 AA;  39690 MW;  4179B41F7FEA1843 CRC64;
     MKSRPQEFQE DFYIPIPLDT NNITALSPFL VPQDHLGGSG IFMIMTVFML FLFIGGTSIN
     VLTIVCTVQY KKLRSHLNYI LVNLAISNLL VSTVGSFTAF VSFLNRYFIF GPTACKIEGF
     VATLGGMVSL WSLSVVAFER WLVICKPVGN FSFKGTHAII GCALTWFFAL LASTPPLFGW
     SRYIPEGLQC SCGPDWYTTE NKYNNESYVM FLFCFCFGFP FTVILFCYGQ LLFTLKSAAK
     AQADSASTQK AEREVTKMVV VMVMGFLVCW LPYASFALWV VFNRGQSFDL RLGTIPSCFS
     KASTVYNPVI YVFMNKQFRS CMMKLIFCGK SPFGDDEEAS SSSQVTQVSS VGPEK
 
 
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