ID A0A1S3GL92_DIPOR Unreviewed; 1024 AA.
AC A0A1S3GL92;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Pde3b {ECO:0000313|RefSeq:XP_012889576.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012889576.1};
RN [1] {ECO:0000313|RefSeq:XP_012889576.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012889576.1};
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_012889576.1; XM_013034122.1.
DR AlphaFoldDB; A0A1S3GL92; -.
DR STRING; 10020.ENSDORP00000020604; -.
DR GeneID; 105999173; -.
DR KEGG; dord:105999173; -.
DR CTD; 5140; -.
DR InParanoid; A0A1S3GL92; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF29; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 641..987
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..947
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 113621 MW; BC6F2C0384458B00 CRC64;
MKKDERDGRA MRCPPPDGAA SPPESLRNGY VKGCVSPLRQ DPPRGFFFHL CRFCNVEPPP
LPPTSPAFVL VLLLLLLLLD AGPQSWAAGA ARLRTLLSVC SLCLSPLFSI ACAFFFLTCF
LTRTQRAPGR GGGGGGSWWL LALPACCYLG DFLAWQWGAW PWGDAAAAPH TPPAGRLVLV
LSCVGLLTLA HPGRLGHSIL VLLFACCVWW VSFASLGALP AGLRPLLSGL VGAIGCLLAL
GLDHFFHIRE APQHPRLSSA ADDKVPVIRP RRRSSCVSLG ESAATYYGSG KMFRRPSLPC
ISREQMILWD WDLKQWHKPH YQNSGGGNGI DLSVLNEARN MVSDLLVDPS LPPQVISSLR
SISSLMGAFS GSCRPKINPL TPFPGFYPYS EIEDPPEKGD RKIHKGISSR NSLPTPQMRR
SSGTSGLLPT EQSSRWERSN GKKPHQEFNI PSQGCYLNGP FSSSFLTVPK QRSSSISLSH
HVGLRRAGAL PSLSPMNSPS YGPVSSGSLT NRSPIEFPDT ADFLSKPSVV LHRSLGNVPS
TPDFNQYCRN SDSNLCNSCG HQILKYVSTC ELDGTDHYSG KSGAEDNRVF LKEPFNLTEI
QQEEETEKSD CRKLFLEGDN CLTEEAQQPN VKDKFNMIML NSKYHNRIHA TDVLHAVWYL
TTRPIPGLQQ IHNNHETGNE IDSDGRVTRG QIAYISSKSC SIPDESYGCL SSNIPALELM
ALYVAAAMHD YDHPGRTNAF LVATNAPQAV LYNDRSVLEN HHAASAWNLY LSRPEYNFLL
NLDHVEFKRF RFLVIEAILA TDLKKHFDFL AEFNAKANDV NSNGIEWNSE NDRLLVCQVC
IKLADINGPA KVRDLHLKWT EGIVNEFYEQ GDEEANLGLP ISPFMDRSSP QLAKLQESFI
THIVGPLCNS YDAAGLLPGQ WIEGEDDDDT ESGDDEDGEE LDTDDEDMGD NLIPKPQRRK
GRRRIFCQLM HHLSENHKIW KEIIEEEEKC KVEGDKLQVE NTLPQADEIQ VIEEADEEEE
PQFE
//
