ID A0A1L8G297_XENLA Unreviewed; 792 AA.
AC A0A1L8G297;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=pde10a.S {ECO:0000313|RefSeq:XP_018120773.1,
GN ECO:0000313|Xenbase:XB-GENE-17336730};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018120773.1};
RN [1] {ECO:0000313|RefSeq:XP_018120773.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018120773.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018120773.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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DR RefSeq; XP_018120773.1; XM_018265284.2.
DR AlphaFoldDB; A0A1L8G297; -.
DR STRING; 8355.A0A1L8G297; -.
DR PaxDb; 8355-A0A1L8G297; -.
DR GeneID; 108717870; -.
DR KEGG; xla:108717870; -.
DR AGR; Xenbase:XB-GENE-17336730; -.
DR CTD; 108717870; -.
DR Xenbase; XB-GENE-17336730; pde10a.S.
DR OMA; HNWAHGW; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 108717870; Expressed in blastula and 11 other cell types or tissues.
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:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE 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 Hydrolase {ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR623088-3,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT ACT_SITE 523
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 523..527
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 562
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 672
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 724
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 792 AA; 90147 MW; CBAC7C98FDA48D12 CRC64;
MEDGPSSAGC FRRFTDCFLS TSLTDEKVKA YLSLHPQVLD EFVSESVSPE TVEKWMKKKS
KNEDMTRTEV SRQYQDTNMQ GVVYELNSYM EQRLDAGGDN KLLLYELSDI IKTATKADGF
ALFFLGECNN SLCLFTPTGT KDGQTQLTSV GPVEYGTTVS AHVAKSRNTV LVEDILGDER
FPKGTGLDSG TRIQSVLCLP IVTAIGDLIG ILELHRHWGR ESFHLCHQQV ATANLAWASV
AIHQVQVCRG LAKQTELNDF LLDVSKTYFD NIVAIDTLLE HIMIYAKNLV NADRCALFQV
DQKNKELYSD LFDIGEEDEG KPVFKKTKEI RFSIEKGIAG QVARTGEVLN IPDAYADPRF
NREVDVYTGY TTRNILCMPI VIRGSIIGVV QMVNKLSGSA FSKTDENNFK MFAVFCALAL
HCANMYHRIR HSECIYRVTL EKLSYHSICT SDEWQNLMNC TLPVSLCREI ELYHFDIQPF
EDLWPAIYVY MIHQSCGETC FELEKLCRFT MSVKKNYRRV PYHNWKHAVT VSHCMYLILR
NNQEIFTDLE RKGLLVACLC HDLDHRGYSN SYLQKFDHPL AALYSTSTME QHHFSQTVSI
LQLEGHNIFS NLSSNEYEQV LEIIRKAIIA TDLALYFGNR KHLEDLHQMG ALNLNNQSHR
DRMIGLMMTA CDLCSVTKLW PITRLIADDI YAEFWAEGDE MKRLGISPIP MMDRDKKDDI
PQGQMGFYNA VAIPCYTTLS EIFPSTRPLL QACKENLSQW EKVSRGEDTT VWIPSQSVPT
ESSDSLPVKI DD
//
