PDE6B_BOVIN
ID PDE6B_BOVIN Reviewed; 853 AA.
AC P23439;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta;
DE Short=GMP-PDE beta;
DE EC=3.1.4.35;
DE Flags: Precursor;
GN Name=PDE6B; Synonyms=PDEB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT SER-2.
RX PubMed=2165490; DOI=10.1016/s0021-9258(19)38252-3;
RA Lipkin V.M., Khramtsov N.V., Vasilevskaya I.A., Atabekova N.V.,
RA Muradov K.G., Gubanov V.V., Li T., Johnston J.P., Volpp K.J.,
RA Applebury M.L.;
RT "Beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase.
RT Comparison with the phosphodiesterase family.";
RL J. Biol. Chem. 265:12955-12959(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2161230;
RA Lipkin V.M., Gubanov V.V., Khramtsov N.V., Vasilevskaya I.A.,
RA Atabekova N.V., Muradov K.G., Shuvaeva T.M., Surina E.A., Zagranichny V.E.,
RA Li T.;
RT "Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of
RT beta-subunit and nucleotide sequence of corresponding cDNA.";
RL Bioorg. Khim. 16:118-120(1990).
CC -!- FUNCTION: Necessary for the formation of a functional phosphodiesterase
CC holoenzyme (By similarity). Involved in retinal circadian rhythm
CC photoentrainment via modulation of UVA and orange light-induced phase-
CC shift of the retina clock (By similarity). May participate in processes
CC of transmission and amplification of the visual signal (By similarity).
CC {ECO:0000250|UniProtKB:P23440, ECO:0000250|UniProtKB:P35913}.
CC -!- FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the
CC hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the
CC formation of a functional phosphodiesterase holoenzyme (By similarity).
CC Involved in retinal circadian rhythm photoentrainment via modulation of
CC UVA and orange light-induced phase-shift of the retina clock (By
CC similarity). May participate in processes of transmission and
CC amplification of the visual signal (By similarity).
CC {ECO:0000250|UniProtKB:P23440, ECO:0000250|UniProtKB:P35913}.
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:P35913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000250|UniProtKB:P35913};
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: Oligomer composed of two catalytic chains (alpha and beta), an
CC inhibitory chain (gamma) and the delta chain.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P35913}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P35913}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P35913}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; J05553; AAA30440.1; -; mRNA.
DR EMBL; X57146; CAA40436.1; -; mRNA.
DR PIR; A36617; A36617.
DR RefSeq; NP_776843.1; NM_174418.1.
DR PDB; 6MZB; EM; 3.40 A; B=1-853.
DR PDB; 7JSN; EM; 3.20 A; B=1-853.
DR PDBsum; 6MZB; -.
DR PDBsum; 7JSN; -.
DR AlphaFoldDB; P23439; -.
DR SMR; P23439; -.
DR IntAct; P23439; 2.
DR MINT; P23439; -.
DR STRING; 9913.ENSBTAP00000052098; -.
DR BindingDB; P23439; -.
DR ChEMBL; CHEMBL2096979; -.
DR DrugCentral; P23439; -.
DR iPTMnet; P23439; -.
DR PRIDE; P23439; -.
DR GeneID; 281974; -.
DR KEGG; bta:281974; -.
DR CTD; 5158; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P23439; -.
DR OrthoDB; 904682at2759; -.
DR PRO; PR:P23439; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Acetylation; Cell projection; cGMP; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Methylation; Prenylation; Reference proteome;
KW Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..850
FT /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit beta"
FT /id="PRO_0000023344"
FT PROPEP 851..853
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023345"
FT DOMAIN 71..220
FT /note="GAF 1"
FT DOMAIN 252..429
FT /note="GAF 2"
FT DOMAIN 481..814
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT ACT_SITE 557
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:2165490"
FT MOD_RES 850
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 850
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 483..484
FT /note="DE -> EQ (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:6MZB"
FT TURN 23..34
FT /evidence="ECO:0007829|PDB:6MZB"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6MZB"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 214..246
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 260..267
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 429..455
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 496..502
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 537..550
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 559..575
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 585..594
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 595..600
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 606..612
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:7JSN"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 624..627
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 640..642
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 644..647
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 650..665
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 669..674
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 677..688
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 692..699
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 703..718
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:7JSN"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 729..749
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 757..759
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:6MZB"
FT HELIX 767..777
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 779..789
FT /evidence="ECO:0007829|PDB:7JSN"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:6MZB"
FT HELIX 794..821
FT /evidence="ECO:0007829|PDB:7JSN"
SQ SEQUENCE 853 AA; 98331 MW; C4B3F22CFFE7F2FB CRC64;
MSLSEGQVHR FLDQNPGFAD QYFGRKLSPE DVANACEDGC PEGCTSFREL CQVEESAALF
ELVQDMQENV NMERVVFKIL RRLCSILHAD RCSLFMYRQR NGVAELATRL FSVQPDSVLE
DCLVPPDSEI VFPLDIGVVG HVAQTKKMVN VQDVMECPHF SSFADELTDY VTRNILATPI
MNGKDVVAVI MAVNKLDGPC FTSEDEDVFL KYLNFGTLNL KIYHLSYLHN CETRRGQVLL
WSANKVFEEL TDIERQFHKA FYTVRAYLNC DRYSVGLLDM TKEKEFFDVW PVLMGEAQAY
SGPRTPDGRE ILFYKVIDYI LHGKEDIKVI PSPPADHWAL ASGLPTYVAE SGFICNIMNA
PADEMFNFQE GPLDDSGWIV KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DEQDEVLMES
LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDR EEIQLILPTR ERLGKEPADC
EEDELGKILK EVLPGPAKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL
VRFLFSVSKG YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLSEE TLNIYQNLNR RQHEHVIHLM
DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DRKSWVEYLS LETTRKEIVM AMMMTACDLS
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT
FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEDQKKETT AKKVGTEICN
GGPAPRSSTC RIL
