ID B4DHV7_HUMAN Unreviewed; 575 AA.
AC B4DHV7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 22-FEB-2023, entry version 80.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58269.1};
RN [1] {ECO:0000313|EMBL:BAG58269.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate nucleus {ECO:0000313|EMBL:BAG58269.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; AK295285; BAG58269.1; -; mRNA.
DR RefSeq; NP_001138764.1; NM_001145292.1.
DR AlphaFoldDB; B4DHV7; -.
DR SMR; B4DHV7; -.
DR PeptideAtlas; B4DHV7; -.
DR DNASU; 5158; -.
DR GeneID; 5158; -.
DR CTD; 5158; -.
DR PharmGKB; PA33134; -.
DR OrthoDB; 5479253at2759; -.
DR BioGRID-ORCS; 5158; 9 hits in 1149 CRISPR screens.
DR GenomeRNAi; 5158; -.
DR Genevisible; B4DHV7; HS.
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; -; 1.
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:SF73; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT BETA; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}.
FT DOMAIN 202..535
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT COILED 518..552
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 278
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 278..282
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 319
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 439
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 492
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 575 AA; 66409 MW; 61A48F882C2613A7 CRC64;
MTKEKEFFDV WSVLMGESQP YSGPRTPDGR EIVFYKVIDY ILHGKEEIKV IPTPSADHWA
LASGLPSYVA ESGFICNIMN ASADEMFKFQ EGALDDSGWL IKNVLSMPIV NKKEEIVGVA
TFYNRKDGKP FDEQDEVLME SLTQFLGWSV MNTDTYDKMN KLENRKDIAQ DMVLYHVKCD
GDEIQLILPT RARLGKEPAD CDEDELGEIL KEELPGPTTF DIYEFHFSDL ECTELDLVKC
GIQMYYELGV VRKFQIPQEV LVRFLFSISK GYRRITYHNW RHGFNVAQTM FTLLMTGKLK
SYYTDLEAFA MVTAGLCHDI DHRGTNNLYQ MKSQNPLAKL HGSSILERHH LEFGKFLLSE
ETLNIYQNLN RRQHEHVIHL MDIAIIATDL ALYFKKRAMF QKIVDESKNY QDKKSWVEYL
SLETTRKEIV MAMMMTACDL SAITKPWEVQ SKVALLVAAE FWEQGDLERT VLDQQPIPMM
DRNKAAELPK LQVGFIDFVC TFVYKEFSRF HEEILPMFDR LQNNRKEWKA LADEYEAKVK
ALEEKEEEER VAAKKVGTEI CNGGPAPKSS TCCIL
//
