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Database: UniProt
Entry: A0A2R9AYU8_PANPA
LinkDB: A0A2R9AYU8_PANPA
Original site: A0A2R9AYU8_PANPA 
ID   A0A2R9AYU8_PANPA        Unreviewed;       722 AA.
AC   A0A2R9AYU8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000022248.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000022248.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000022248.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AJFE02069299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02069307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9AYU8; -.
DR   Ensembl; ENSPPAT00000045056.1; ENSPPAP00000022248.1; ENSPPAG00000034143.1.
DR   GeneTree; ENSGT00940000156543; -.
DR   Proteomes; UP000240080; Chromosome 6.
DR   Bgee; ENSPPAG00000034143; Expressed in testis and 6 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   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:UP000240080}.
FT   DOMAIN          385..702
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        458
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         458..462
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         497
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         607
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         607
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         659
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   722 AA;  81879 MW;  30523498307AE328 CRC64;
     MQYLQRAVKQ STIKMMYASA DIQKYICWYQ DTNMQGVVYE LNSYIEQRLD TGGDNQLLLY
     ELSSIIKIAT KADGFALYFL GECNNSLCIF TPPGIKEGKP RLIPAGPITQ GTTVSAYVAK
     SRKTLLVEDI LGDERFPGGT GLESGTRIQS VLCLPIVTAI GDLIGILELY RHWGKEAFCL
     SHQEVATANL AWASVAIHQV QVCRGLAKQT ELNDFLLDIY AKNLVNADRC ALFQVDHKNK
     ELYSDLFDIG EEKEGKPVFK KTKEIRFSIE KGIAGQVART GEVLNIPDAY ADPRFNREVD
     LYTGYTTRNI LCMPIVSRGS VIGVVQMVNK ISGSAFSKTD ENNFKMFAVF CALALHCANM
     YHRIRHSECI YRVTMEKLSY HSICTSEEWQ GLMQFTLPVR LCKEIELFHF DIGPFENMWP
     GIFVYMVHRS CGTSCFELEK LCRFIMSVKK NYRRVPYHNW KHAVTVAHCM YAILQNNHTL
     FTDLERKGLL IACLCHDLDH RGFSNSYLQK FDHPLAALYS TSTMEQHHFS QTVSILQLEG
     HNIFSTLSSS EYEQVLEIIR KAIIATDLAL YFGNRKQLEE MYQTGSLNLN NQSHRDRVIG
     LMMTACDLCS VTKLWPVTKL TANDIYAEFW AEGDEMKKLG IQPIPMMDRD KKDEVPQGQL
     GFYNAVAIPC YTTLTQILPP TEPLLKACRD NLSQWEKVIR GEETATWISS PSVAQKAAAS
     ED
//
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