PDE6C_CHICK
ID PDE6C_CHICK Reviewed; 862 AA.
AC P52731;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha';
DE EC=3.1.4.35 {ECO:0000250|UniProtKB:P51160};
DE AltName: Full=cGMP phosphodiesterase 6C;
DE Flags: Precursor;
GN Name=PDE6C;
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 STRAIN=Rhode Island red; TISSUE=Retina;
RX PubMed=7821382; DOI=10.1006/exer.1994.1119;
RA Semple-Rowland S.L., Green D.A.;
RT "Molecular characterization of the alpha'-subunit of cone photoreceptor
RT cGMP phosphodiesterase in normal and rd chicken.";
RL Exp. Eye Res. 59:365-372(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 55-225 IN COMPLEX WITH CGMP.
RX PubMed=18614542; DOI=10.1074/jbc.m802891200;
RA Martinez S.E., Heikaus C.C., Klevit R.E., Beavo J.A.;
RT "The structure of the GAF A domain from phosphodiesterase 6C reveals
RT determinants of cGMP binding, a conserved binding surface, and a large
RT cGMP-dependent conformational change.";
RL J. Biol. Chem. 283:25913-25919(2008).
CC -!- FUNCTION: As cone-specific cGMP phosphodiesterase, it plays an
CC essential role in light detection and cone phototransduction by rapidly
CC decreasing intracellular levels of cGMP.
CC {ECO:0000250|UniProtKB:P51160}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; EC=3.1.4.35;
CC Evidence={ECO:0000250|UniProtKB:P51160};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000250};
CC -!- SUBUNIT: Composed of two alpha' subunits that are associated with 3
CC smaller proteins of 11, 13, and 15 kDa. {ECO:0000269|PubMed:18614542}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; L29233; AAC42223.1; -; mRNA.
DR PIR; I50186; I50186.
DR RefSeq; NP_990317.1; NM_204986.1.
DR PDB; 3DBA; X-ray; 2.57 A; A/B=55-225.
DR PDB; 3JBQ; EM; 11.00 A; 1/2=55-228.
DR PDB; 6X88; X-ray; 3.20 A; A/B=1-862.
DR PDBsum; 3DBA; -.
DR PDBsum; 3JBQ; -.
DR PDBsum; 6X88; -.
DR AlphaFoldDB; P52731; -.
DR SMR; P52731; -.
DR STRING; 9031.ENSGALP00000010688; -.
DR PaxDb; P52731; -.
DR GeneID; 395834; -.
DR KEGG; gga:395834; -.
DR CTD; 5146; -.
DR VEuPathDB; HostDB:geneid_395834; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P52731; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; P52731; -.
DR BRENDA; 3.1.4.35; 1306.
DR EvolutionaryTrace; P52731; -.
DR PRO; PR:P52731; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; cGMP; cGMP-binding; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome; Repeat; Sensory transduction; Vision.
FT CHAIN 1..859
FT /note="Cone cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit alpha'"
FT /id="PRO_0000198832"
FT PROPEP 860..862
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370790"
FT DOMAIN 75..224
FT /note="GAF 1"
FT DOMAIN 256..433
FT /note="GAF 2"
FT DOMAIN 486..819
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 830..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 562
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:18614542"
FT BINDING 116
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:18614542"
FT BINDING 169..172
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:18614542"
FT BINDING 176
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:18614542"
FT BINDING 566
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 859
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 859
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6X88"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:3DBA"
FT STRAND 189..204
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 207..223
FT /evidence="ECO:0007829|PDB:3DBA"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:6X88"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6X88"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:6X88"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6X88"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6X88"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6X88"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:6X88"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:6X88"
FT STRAND 399..411
FT /evidence="ECO:0007829|PDB:6X88"
FT HELIX 416..446
FT /evidence="ECO:0007829|PDB:6X88"
FT TURN 447..452
FT /evidence="ECO:0007829|PDB:6X88"
SQ SEQUENCE 862 AA; 100009 MW; BD3145BB5FF826A8 CRC64;
MGEVNKDAVE KYLENNPQFA KEYFDRKMRA EVLGSIFQVS PGDVKEGVSF KDMSRLEECN
ILFELLTEIQ DEAGSMEKIV HKTLQRLSQL LARDRCSMFI CRSRNGIPEV ATRLLNVTPT
SKFEDNLVNP DKETVFPLDI GIAGWVAHTK KFFNIPDVKK NNHFSDYLDK KTGYTTVNMM
AIPITQGKEV LAVVMALNKL NASEFSKEDE EVFKKYLNFI SLVLRNHHTS YLYNIESRRS
QMLLWSANKV FEELTDIERQ FHKALYTIRM YLNCERYSVG LLDMTKEKEF YDEWPIRLGE
AEPYKGPKTP DGREVNFYKI IDYILHGKEE IKVIPTPPAD HWCLISGLPT YVAENGFICN
MMNAPADEYF TFQKGPVDET GWVIKNVLSL PIVNKKEEIV GVATFYNRKD GKPFDEYDEQ
IIETLTQFLG WSVLNTDTYD KMNKLENRKD IAQEMLMYQT KATPTEVESI LKYKEKLNVK
SIEECDEKDL IRILKEELPD PKDLELYEFR FSDFPVTEHG LITCGIRLFF EINVVEKFKV
PAEVLTRWMY TVRKGYRDIT YHNWRHGFNV GQTMFTLLMT GRIKKYYTDL EAFAMVAAAF
CHDIDHRGTN NLYQMKSAAP LAKLHGSSIL ERHHLEYSKT LLQDESLNIF QNLNKRQFET
VLHLFEVAII ATDLALYFKK RTMFQKIVDA IEKMETEEEA IKYISIDPTK KEVIMAMMMT
GCDLSAITKP WEVQSKVALM VANEFWEQGD LERTVLQQQP IPMMDRNKGD ELPKLQVGFI
DFVCTFVYKE FSRFHKEITP MFDGLQNNRV EWKTRADEYE EKMKVIEEQK KKEEEAAAKK
AENAAGGGGG GEDGKSKTCI VL
