ID Q5XH00_XENLA Unreviewed; 859 AA.
AC Q5XH00;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=pde5a.S {ECO:0000313|RefSeq:NP_001088271.1,
GN ECO:0000313|Xenbase:XB-GENE-865295};
GN Synonyms=LOC495103 {ECO:0000313|EMBL:AAH84276.1}, pde5a
GN {ECO:0000313|RefSeq:NP_001088271.1,
GN ECO:0000313|Xenbase:XB-GENE-865295};
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|EMBL:AAH84276.1};
RN [1] {ECO:0000313|RefSeq:NP_001088271.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH84276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000313|EMBL:AAH84276.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001088271.1}
RP IDENTIFICATION.
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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC 3',5'-cyclic GMP: step 1/1. {ECO:0000256|ARBA:ARBA00037913}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC084276; AAH84276.1; -; mRNA.
DR RefSeq; NP_001088271.1; NM_001094802.1.
DR GeneID; 495103; -.
DR KEGG; xla:495103; -.
DR AGR; Xenbase:XB-GENE-865295; -.
DR CTD; 495103; -.
DR Xenbase; XB-GENE-865295; pde5a.S.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 495103; Expressed in heart and 12 other cell types or tissues.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; 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:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 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 2: Evidence at transcript level;
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
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:UP000186698}.
FT DOMAIN 516..840
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 53..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 593
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 593..597
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 633
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 634
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 634
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 744
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 744
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 797
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 859 AA; 97418 MW; E764794B66E6CDCD CRC64;
MGAADFPVAA TLEPQAESWT ATHSTTGGNV HAGCTLQEMV NAWFAERVHT IPASKEQGKN
NSESNPQVCY SENTTQGTPV RKISASEFDR PLRPIVVKDS VGTLTFLSDS EKKEQMPLQP
PSLSRAGDQC SRLLELVKDI SSHLDVTALC HNIFLHIHEL IAADRYSLFL VCEDSSNKKF
LVSRLFDVAE GTTVEQASNN CIRLEWKKGI VGHVAEFGQP LNIKDAYQDS RFNAEVDQIT
GYKTQSILCM PIKNHREEVV GVAQAINKKS GSNGTFTDQD EKDFAAYLAF CGIVLHNAQL
YETSLLENRR NQVLLDLATL IFEEQQSLEV ILKKIAATIL SFMQAQRCTI FIVDEDSPDT
FSSVFHMESD ELQESANAVK REYDVSKINY MYAQYVANTM EPINIPDICK DTRFPWTNGN
EEKNFKHIQS LLCSPIKNAK KNKVIGVCQL VNKVDENSGK IKAFNRNDEQ FVEAFAIFCG
LAIQNTQMYE VVERAMAKQM VTLEILSYHT SAAEEETTEL QVTAGAIVPS AQSLKLTEFY
FSDFELSDME TTLATSRMFT DLNLVQTFQM KYETLCRWIL SVKKNYRKNV VYHNWRHAFN
TAQCMFAALE TGKIQSKLSD LEILALMIAT LSHDLDHRGV NNSFIQRSEH PLAQLYCHSI
MENHHFDQCL MILNSQGNQI LSGLSVQDYK TVLKMIKKAI LATDLALYIK RRSDFFELVN
KKKFKWDDPS QKELFLSMLM TACDLSAITK PWPVQQRIAE LIAAEFYDQG DKERRELNTE
PIDLMNREKK DKIPSMQVGF IDAVCLELYE ALTQVSESCY PLLDGCQRNK QMWQILAEQQ
EKNLVNGDKS QSEVNCNMD
//
