ID F1SBW6_PIG Unreviewed; 801 AA.
AC F1SBW6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE10A {ECO:0000313|Ensembl:ENSSSCP00000004352.5,
GN ECO:0000313|VGNC:VGNC:91248};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000004352.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000004352.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000004352.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000004352.5}
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 AlphaFoldDB; F1SBW6; -.
DR PaxDb; 9823-ENSSSCP00000004352; -.
DR Ensembl; ENSSSCT00000004453.5; ENSSSCP00000004352.5; ENSSSCG00000004027.5.
DR VGNC; VGNC:91248; PDE10A.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR HOGENOM; CLU_006980_1_0_1; -.
DR TreeFam; TF316499; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000004027; Expressed in testis and 37 other cell types or tissues.
DR ExpressionAtlas; F1SBW6; baseline and differential.
DR GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
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:UP000008227}.
FT DOMAIN 465..781
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 538..542
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 577
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 687
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 738
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 801 AA; 90476 MW; BF85AD2F4C59C700 CRC64;
MSKKRKALEG GGGGGESPLR EEDPTAWLEG SSEEQGLTDE KVKAYLSLHP QVLDEFVSES
VSAETVEKWL KRKNNKPEDE SAPKEVSRYQ DTNMQGVVYE LNSYIEQRLD TGGDNQLLLY
ELSSIIKIAT KADGFALYFL GECNNSLCVF TPPGIKEGKP RLIPAGPIAQ GTTTSAYVAK
SRKTLLVEDI LGDERFPRGT GLESGTRIQS VLCLPIVTAI GDLIGILELY RHWGKEAFCL
SHQEVATANL AWASVAIHQV QVCRGLAKQT ELNDFLLDVS KTYFDNIVAI DSLLEHIMIY
AKNLVNADRC ALFQVDHKNK ELYSDLFDIG EEKEGKPVFK KTKEIRFSIE KGIAGQVART
GEVLNIPDAY ADPRFNREVD LYTGYTTRNI LCMPIVSRGS VIGVVQMVNK ISGSAFSKTD
ENNFKMFAVF CALALHCANM YHRIRHSECI YRVTMEKLSY HSICTAEEWQ GLMRFNLPVR
LCKEIELFHF DIGPFENMWP GIFVYMVHRS CGTACFELEK LCRFIMSVKK NYRRVPYHNW
KHAVTVAHCM YAILQNNHGL FTDLERKGLL IACLCHDLDH RGFSNSYLQK FDHPLAALYS
TSTMEQHHFS QTVSILQLEG HNIFSTLSSS EYEQVLEIIR KAIIATDLAL YFGNRKQLEE
MYQTGSLNLN NQSHRDRVIG LMMTACDLCS VTKLWPVTKL ANDIYAEFWA EGDEMKKLGI
QPIPMMDRDK KDEVPQGQLG FYNAVAIPCY TTLTQIFPPT EPLLKACRNN LSQWEKVIRG
EESAVWISSP PAAQGEAARE D
//
