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}.
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 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
//