ID   G3V8J8_RAT              Unreviewed;       671 AA.
AC   G3V8J8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=Pde4c {ECO:0000313|Ensembl:ENSRNOP00000026457.5,
GN   ECO:0000313|RGD:727918};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000026457.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000026457.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026457.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000026457.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000026457.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; EC=3.1.4.53;
CC         Evidence={ECO:0000256|ARBA:ARBA00033681};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000256|ARBA:ARBA00033681};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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 AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE4 subfamily. {ECO:0000256|ARBA:ARBA00009517}.
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DR   RefSeq; NP_001263694.1; NM_001276765.1.
DR   RefSeq; XP_006252930.1; XM_006252868.3.
DR   AlphaFoldDB; G3V8J8; -.
DR   SMR; G3V8J8; -.
DR   Ensembl; ENSRNOT00000026457.7; ENSRNOP00000026457.5; ENSRNOG00000019518.7.
DR   GeneID; 290646; -.
DR   KEGG; rno:290646; -.
DR   CTD; 5143; -.
DR   RGD; 727918; Pde4c.
DR   GeneTree; ENSGT00940000162285; -.
DR   HOGENOM; CLU_005940_5_3_1; -.
DR   OrthoDB; 240889at2759; -.
DR   TreeFam; TF314638; -.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000019518; Expressed in kidney and 19 other cell types or tissues.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
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; IPR040844; PDE4_UCR.
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:SF135; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4C; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF18100; PDE4_UCR; 1.
DR   Pfam; PF00233; PDEase_I; 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.
PE   3: Inferred from homology;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
SQ   SEQUENCE   671 AA;  74238 MW;  0ED8A4FB34962FA9 CRC64;
     MRRSGTTLSF LLTERVREPV DSGVAPVSHL GGGVILRRFS GTLLLPPLSS RLGSSGEAES
     AAPVVFTIGS RGTERSHGSA QSSFDLENGL PSGRGPLDAQ SGSSLGRALQ PPVHHGQRRE
     SFLYRSDSDH EPSPKAVSRT SSAASDLHGE DMIVTPFAQV LASLRTVRSN VAALAHGAGS
     ATRQALLGTP PQSSQQAAPA EESGLQLAQE TLEELDWCLE QLETLQTRRS VGEMASNKFK
     RMLNRELTHL SETSRSGNQV SEYISQTFLD QQAEVELPAP PTEDHPWPMA QITGLRKSCH
     TSLPTAAIPR FGVQTDQEEQ LAKELEDTNK WGFDVFKVAE LSGNRPLTAV IFSVLQERDL
     LKTFQIPADT LLRYLLTLEG HYHSNVAYHN SIHAADVVQS AHVLLGTPAL EAVFTDLEVL
     AAIFACAIHD VDHPGVSNQF LINTNSELAL MYNDSSVLEN HHLAVGFKLL QGENCDIFQN
     LSTKQKLSLR RMVIDMVLAT DMSKHMSLLA DLKTMVETKK VTSLGVLLLD NYSDRIQVLQ
     SLVHCADLSN PAKPLPLYRQ WTERIMAEFF QQGDRERESG LDISPMCDKH TASVEKSQVG
     FIDYIAHPLW ETWADLVHPD AQELLDTLED NREWYQSRVP CSPPHAIGPD RFKFELTLEE
     TEEEEEEDER H
//