ID H2RBC5_PANTR Unreviewed; 673 AA.
AC H2RBC5; A0A2J8KKZ1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE4D {ECO:0000313|Ensembl:ENSPTRP00000055480.3,
GN ECO:0000313|VGNC:VGNC:54161};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000055480.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000055480.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000055480.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000256|ARBA:ARBA00033681};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000256|ARBA:ARBA00033681};
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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE4 subfamily. {ECO:0000256|ARBA:ARBA00009517}.
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DR EMBL; AACZ04069335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04069342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016810035.1; XM_016954546.1.
DR RefSeq; XP_016810036.1; XM_016954547.1.
DR AlphaFoldDB; H2RBC5; -.
DR SMR; H2RBC5; -.
DR Ensembl; ENSPTRT00000063934.3; ENSPTRP00000055480.3; ENSPTRG00000016900.6.
DR VGNC; VGNC:54161; PDE4D.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000155674; -.
DR HOGENOM; CLU_005940_7_3_1; -.
DR OMA; FNTDEGG; -.
DR OrthoDB; 240889at2759; -.
DR TreeFam; TF314638; -.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000016900; Expressed in skeletal muscle tissue and 21 other cell types or tissues.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR040844; PDE4_UCR.
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:SF91; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4D; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF18100; PDE4_UCR; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
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 cAMP {ECO:0000256|ARBA:ARBA00023149};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 250..579
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 326..330
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 367
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 484
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 535
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 673 AA; 76467 MW; BDC04171BA91A297 CRC64;
MMHVNNFPFR RHSWICFDVD NGTSAGRSPL DPMTSPGSGL ILQANFVHSQ RRESFLYRSD
SDYDLSPKSM SRNSSIASDI HGDDLIVTPF AQVLASLRTV RNNFAALTNL QDRAPSKRSP
MCNQPSINKA TITEEAYQKL ASETLEELDW CLDQLETLQT RHSVSEMASN KFKRMLNREL
THLSEMSRSG NQVSEFISNT FLDKQHEVEI PSPTQKEKEK KKRPMSQISG VKKLMHSSSL
TNSSIPRFGV KTEQEDVLAK ELEDVNKWGL HVFRIAELSG NRPLTVIMHT IFQERDLLKT
FKIPVDTLIT YLMTLEDHYH ADVAYHNNIH AADVVQSTHV LLSTPALEAV FTDLEILAAI
FASAIHDVDH PGVSNQFLIN TNSELALMYN DSSVLENHHL AVGFKLLQEE NCDIFQNLTK
KQRQSLRKMV IDIVLATDMS KHMNLLADLK TMVETKKVTS SGVLLLDNYS DRIQVLQNMV
HCADLSNPTK PLQLYRQWTD RIMEEFFRQG DRERERGMEI SPMCDKHNAS VEKSQVGFID
YIVHPLWETW ADLVHPDAQD ILDTLEDNRE WYQSTIPQSP SPAPDDPEEG RQGQTEKFQF
ELTLEEDGES DTEKDSGSQV EEDTSCSDSK TLCTQDSEST EIPLDEQVEE EAVGEEEESQ
PEACVIDDRS PDT
//
