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OPSR_CHICK
ID   OPSR_CHICK              Reviewed;         362 AA.
AC   P22329;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Red-sensitive opsin;
DE   AltName: Full=Iodopsin;
DE   AltName: Full=Red cone photoreceptor pigment;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2268324; DOI=10.1016/s0006-291x(05)80915-5;
RA   Tokunaga F., Iwasa T., Miyagishi M., Kayada S.;
RT   "Cloning of cDNA and amino acid sequence of one of chicken cone visual
RT   pigments.";
RL   Biochem. Biophys. Res. Commun. 173:1212-1217(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2226824; DOI=10.1016/0014-5793(90)80465-u;
RA   Kuwata O., Imamoto Y., Okano T., Kokame K., Kojima D., Matsumoto H.,
RA   Morodome A., Fukada Y., Shichida Y., Yasuda K., Shimura Y., Yoshizawa T.;
RT   "The primary structure of iodopsin, a chicken red-sensitive cone pigment.";
RL   FEBS Lett. 272:128-132(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 322-362, AND PHOSPHORYLATION.
RX   PubMed=2271641; DOI=10.1021/bi00495a013;
RA   Fukada Y., Kokame K., Okano T., Shichida Y., Yoshizawa T., McDowell J.H.,
RA   Hargrave P.A., Palczewski K.;
RT   "Phosphorylation of iodopsin, chicken red-sensitive cone visual pigment.";
RL   Biochemistry 29:10102-10106(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
RX   PubMed=7629014; DOI=10.1093/oxfordjournals.jbchem.a124736;
RA   Ishihara H., Engel J.D., Yamamoto M.;
RT   "Structure and regulation of the chicken GATA-3 gene.";
RL   J. Biochem. 117:499-508(1995).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=571 nm;
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:0000269|PubMed:2271641}.
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; M62903; AAA49137.1; -; mRNA.
DR   EMBL; X57490; CAA40727.1; -; mRNA.
DR   PIR; A37783; A37783.
DR   RefSeq; NP_990771.1; NM_205440.1.
DR   AlphaFoldDB; P22329; -.
DR   SMR; P22329; -.
DR   PRIDE; P22329; -.
DR   GeneID; 396421; -.
DR   KEGG; gga:396421; -.
DR   CTD; 5956; -.
DR   VEuPathDB; HostDB:geneid_396421; -.
DR   OrthoDB; 940057at2759; -.
DR   PhylomeDB; P22329; -.
DR   PRO; PR:P22329; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0044297; C:cell body; IDA:AgBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:AgBase.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:AgBase.
DR   GO; GO:0031982; C:vesicle; IDA:AgBase.
DR   GO; GO:0031404; F:chloride ion binding; IDA:AgBase.
DR   GO; GO:0008020; F:G protein-coupled photoreceptor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR   GO; GO:0016039; P:absorption of UV light; IDA:AgBase.
DR   GO; GO:0016038; P:absorption of visible light; IDA:AgBase.
DR   GO; GO:0071482; P:cellular response to light stimulus; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0016037; P:light absorption; IDA:AgBase.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR   GO; GO:0070207; P:protein homotrimerization; IDA:AgBase.
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; IPR000378; Opsin_red/grn.
DR   InterPro; IPR027430; Retinal_BS.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00575; OPSINREDGRN.
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   1: Evidence at protein level;
KW   Chromophore; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN           1..362
FT                   /note="Red-sensitive opsin"
FT                   /id="PRO_0000197797"
FT   TOPO_DOM        1..49
FT                   /note="Extracellular"
FT   TRANSMEM        50..74
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..86
FT                   /note="Cytoplasmic"
FT   TRANSMEM        87..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..126
FT                   /note="Extracellular"
FT   TRANSMEM        127..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..165
FT                   /note="Cytoplasmic"
FT   TRANSMEM        166..189
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..215
FT                   /note="Extracellular"
FT   TRANSMEM        216..243
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..265
FT                   /note="Cytoplasmic"
FT   TRANSMEM        266..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..297
FT                   /note="Extracellular"
FT   TRANSMEM        298..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..362
FT                   /note="Cytoplasmic"
FT   MOD_RES         309
FT                   /note="N6-(retinylidene)lysine"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        123..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        55
FT                   /note="V -> L (in Ref. 2; CAA40727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="W -> S (in Ref. 2; CAA40727)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  40326 MW;  C54426EF63E64B66 CRC64;
     MAAWEAAFAA RRRHEEEDTT RDSVFTYTNS NNTRGPFEGP NYHIAPRWVY NLTSVWMIFV
     VAASVFTNGL VLVATWKFKK LRHPLNWILV NLAVADLGET VIASTISVIN QISGYFILGH
     PMCVVEGYTV SACGITALWS LAIISWERWF VVCKPFGNIK FDGKLAVAGI LFSWLWSCAW
     TAPPIFGWSR YWPHGLKTSC GPDVFSGSSD PGVQSYMVVL MVTCCFFPLA IIILCYLQVW
     LAIRAVAAQQ KESESTQKAE KEVSRMVVVM IVAYCFCWGP YTFFACFAAA NPGYAFHPLA
     AALPAYFAKS ATIYNPIIYV FMNRQFRNCI LQLFGKKVDD GSEVSTSRTE VSSVSNSSVS
     PA
 
 
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