ID A0A0L8GD80_OCTBM Unreviewed; 1150 AA.
AC A0A0L8GD80;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=OCBIM_22036126mg {ECO:0000313|EMBL:KOF74490.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF74490.1};
RN [1] {ECO:0000313|EMBL:KOF74490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF74490.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF74490.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000583};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
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:0000256|RuleBase:RU363067};
CC -!- SUBUNIT: Interacts with PrBP. {ECO:0000256|ARBA:ARBA00038662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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DR EMBL; KQ422647; KOF74490.1; -; Genomic_DNA.
DR RefSeq; XP_014782378.1; XM_014926892.1.
DR AlphaFoldDB; A0A0L8GD80; -.
DR STRING; 37653.A0A0L8GD80; -.
DR EnsemblMetazoa; Ocbimv22036126m; Ocbimv22036126m.p; Ocbimv22036126m.g.
DR EnsemblMetazoa; XM_014926892.1; XP_014782378.1; LOC106877858.
DR OrthoDB; 5479253at2759; -.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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 PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF216; PHOSPHODIESTERASE; 1.
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 SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289}.
FT DOMAIN 451..772
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 880..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 526..530
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 567
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 677
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 729
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1150 AA; 131928 MW; 9A6EB182D49C78DC CRC64;
MSTDLTEEDI RQFLDDNPQF VDNWLSEHGM EEIATDFSKL RVLSKTALKF LSILSLEQDI
NVYLDKDTEP ELPARKMNLF RDILKLVHSD IDSTRVTKKI LQSACILLRC HKTSLLLTQG
FGKKRFLISR TSNVATRSQL GEIDNIEGDT IHLPFGKGIV GFVAENECLV NIKEAWRDPR
VQKNMGETDY QIRSILSVPV FDKNGRVIGV VKALNKLNED NFDSTDENLF ECFSKICALN
LNNDRFFKAA QGENKRHQML LKLSRCFSRN GEHFQKLVSE ILQYAMKMLD CDNISIYLSD
NADDSSQLTK SANVLQFLKG DTKVKDAPID PRFVSLIERN MNSASMVNVV SLSNSYDRTK
RKTKITLEGD IQNWIICVTI HANCNTVIGY MMFLRKTIDI FSENDINMLE TFAIFCGLAI
YNNHLYKSCN KIVSSHDVAY ELLQLHSTCG EEEAYEMQHQ DIRTTSYYKL YSYDFISFLY
LENEQVILSA LMFLEMNALN SLKISKFNLY RWILTVKKNY RPVPYHNWQH AVNVTQAMFS
MLTTGRLQIY FKEFELVCLL VACLFHDIDH RGTNNAFQVN TASPLATLYN TSIMECHHIN
RSIMILENED TNIFRNISAE KYRQGLKFIE KAILATDLVL YFEKRNLFRQ QIEDGNKTFE
SQESVELLIS MMMTAADLIA ITKPWEFQKM TAMLIANEFF TQGDMETASD IPLLPLMDRN
NIHEIPQMQV GFIDFVCTMI YKSFSELHEE LEPLYDGMLN NRAHWAGIAN GDEEFDAEKE
YNLALKLFYL EEAISCTTSP MLHVNVATQT VLTYLNLEQE QQTIQTILSY PIEELVTVND
LTIPVSPEIE MIPKATKNCQ TEDRSPSLSE AFVQTYVPAT RTGEASPAEP PTQIFRRQPS
TATKSGDYSE SETAVSSLTK SSVSRSPFPT RRSSCFDELL YERRQELELE KGKSFRNTLC
LEKPLSLKRT SRIILPPNPV RRESTQTRSS DYIFHRSSSS LRLSIGEISQ KEEILFENIS
RKYSFKSETS PKSSIMENVL EPVKNENVRE KSKDADTPIG KEVRILSPKK KKASWTSAYE
GNGSTKGRIP VARRSLSITK DRMDSVYRTR SNSGMQKQIS QNIEFRRRKC VKVASKDVQK
GKRLAICVIC
//
