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Database: UniProt
Entry: A0A1S3ANR2_ERIEU
LinkDB: A0A1S3ANR2_ERIEU
Original site: A0A1S3ANR2_ERIEU 
ID   A0A1S3ANR2_ERIEU        Unreviewed;       815 AA.
AC   A0A1S3ANR2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=PDE3A {ECO:0000313|RefSeq:XP_007538325.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007538325.1};
RN   [1] {ECO:0000313|RefSeq:XP_007538325.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_007538325.1; XM_007538263.2.
DR   AlphaFoldDB; A0A1S3ANR2; -.
DR   STRING; 9365.ENSEEUP00000008189; -.
DR   CTD; 5139; -.
DR   eggNOG; ENOG502QSV8; Eukaryota.
DR   InParanoid; A0A1S3ANR2; -.
DR   OrthoDB; 5479253at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
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:SF104; PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT   DOMAIN          342..767
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          102..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..807
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  90285 MW;  23CAED659FDD392D CRC64;
     MESSGTSITV DIAVMGEAHG LITDLLADPS LPPNVCTSLR AVSNLLSTQL TFPAVHKPRA
     SPVVSFSDSI TCSDSEESSE KDKLAIPRRL RRSLPPGLLR RVSSTWTTTT SATGLPTLEP
     APVRRDRSAS IKLHEAPSSS AISSDSWSNP ASMTLTKSRS FTSSFAISVA NHVKAKKQNR
     PGALTTISPV PSPCASPLQG TPASSPVSKT SAAQFPEPAG TLAKQGLSSH RALTYTQSAP
     DLSPQILTPP VLCSSCGRPY SQENPANRPL EGSSTAVQTA SRTDDTTQVT SDYETNNNSD
     SSDIVQNEDE TECSRDQLRK ASACNTCMPK NMIFLEKLIL APEPLVMDNL DSVMEQLSTW
     NFPIFDLVEK IGRKCGRILS QVSYRLFEDM GLFEAFKIPI REFMNYFHAL EIGYREIPYH
     NRIHATDVLH AVWYLTTQPI PGLSTVISDH GSASDSDSDS GFTHSHMGYV FSKMYNVQDD
     KYGCLSGNIP ALELMALYVA AAMHDYDHPG RTNAFLVATS APQAVLYNDR SVLENHHAAA
     AWNLFMSRPE YNFLVNLDHV EFKHFRFLVI EAILATDLKK HFDFVARFNA KVNDDVGIDW
     TNENDRLLVC QMCIKLADIN GPAKCKELHL QWTEGIVNEF YEQGDEEASL GLPISPFMDR
     SAPQLANLQE SFISHIVGPL CNSYDSAGLM PGKWVEDSDE SGDTDDPEED EEEVVVEEVE
     EGPIEEEACE NNEPSRKKTF KRRKIYCQIT QHLLQNHKMW KKVMEEEQRM AGMESQSLDP
     PPQQHPSDQI QAIKEEEEEK GKPRGEEVPP TEPNQ
//
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