ID   B3KSS6_HUMAN            Unreviewed;       709 AA.
AC   B3KSS6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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:BAG52838.1};
RN   [1] {ECO:0000313|EMBL:BAG52838.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M.,
RA   Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S.,
RA   Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S.,
RA   Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H.,
RA   Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M.,
RA   Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M.,
RA   Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y.,
RA   Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N.,
RA   Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S.,
RA   Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T.,
RA   Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M.,
RA   Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y.,
RA   Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y.,
RA   Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T.,
RA   Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00033675};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000256|ARBA:ARBA00033675};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; Evidence={ECO:0000256|ARBA:ARBA00033684};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000256|ARBA:ARBA00033684};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00033709};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC         Evidence={ECO:0000256|ARBA:ARBA00033709};
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       PDE1 subfamily. {ECO:0000256|ARBA:ARBA00010664}.
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; AK094180; BAG52838.1; -; mRNA.
DR   AlphaFoldDB; B3KSS6; -.
DR   PeptideAtlas; B3KSS6; -.
DR   DNASU; 5137; -.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:RHEA.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:RHEA.
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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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   InterPro; IPR013706; PDEase_N.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF32; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1C; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; B3KSS6; HS.
PE   2: Evidence at transcript level;
KW   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          151..528
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          453..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          34..64
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        523..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         228..232
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         269
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         376
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         427
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   709 AA;  80730 MW;  EF215083585B7D9B CRC64;
     MESPTKEIEE FESNSLKYLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD
     LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR
     SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI EALKDVDKWS FDVFSLNEAS
     GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV
     HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH
     HLSAAYRLLQ DDEEMNILIN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE
     AIEKPKALSL MLHAADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS
     TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDETSQT GGTGQRRSSL NSISSSDAKR
     SGVKTSGSEG SAPINNSVIS VDYKSFKATW TEVVHINRER WRAKVPKEEK AKKEAEEKAR
     LAAEEQQKEM EAKSQAEEGA SGKAEKKTSG ETKNQVNGTR ANKSDNPRGK NSKAEKSSGE
     QQQNGDFKDG KNKTDKKDHS NIGNDSKKTD GTKQRSHGSP APSTSSTCRL TLPVIKPPLR
     HFKRPAYASS SYAPSVSKKT DEHPARYKML DQRIKMKKIQ NISHNWNRK
//