ID I3M794_ICTTR Unreviewed; 419 AA.
AC I3M794;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000256|ARBA:ARBA00014478, ECO:0000256|PIRNR:PIRNR000970};
DE Short=CNP {ECO:0000256|PIRNR:PIRNR000970};
DE Short=CNPase {ECO:0000256|PIRNR:PIRNR000970};
DE EC=3.1.4.37 {ECO:0000256|ARBA:ARBA00012317, ECO:0000256|PIRNR:PIRNR000970};
GN Name=CNP {ECO:0000313|Ensembl:ENSSTOP00000005459.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000005459.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000005459.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May participate in RNA metabolism in the myelinating cell,
CC CNP is the third most abundant protein in central nervous system
CC myelin. {ECO:0000256|PIRNR:PIRNR000970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-
CC phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37;
CC Evidence={ECO:0000256|ARBA:ARBA00000610,
CC ECO:0000256|PIRNR:PIRNR000970};
CC -!- SUBUNIT: Exists as monomers and homodimers.
CC {ECO:0000256|ARBA:ARBA00011781, ECO:0000256|PIRNR:PIRNR000970}.
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000256|ARBA:ARBA00004223}.
CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC family. {ECO:0000256|ARBA:ARBA00008662, ECO:0000256|PIRNR:PIRNR000970}.
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; AGTP01023479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005321919.1; XM_005321862.2.
DR AlphaFoldDB; I3M794; -.
DR STRING; 43179.ENSSTOP00000005459; -.
DR Ensembl; ENSSTOT00000006102.3; ENSSTOP00000005459.3; ENSSTOG00000006116.3.
DR GeneID; 101962838; -.
DR CTD; 1267; -.
DR eggNOG; KOG2401; Eukaryota.
DR GeneTree; ENSGT00510000048410; -.
DR HOGENOM; CLU_039178_0_0_1; -.
DR InParanoid; I3M794; -.
DR OrthoDB; 5489998at2759; -.
DR TreeFam; TF332157; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR Gene3D; 3.90.1740.10; 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR008431; CNPase.
DR InterPro; IPR047325; CNPase_cat.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10156; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10156:SF0; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF05881; CNPase; 1.
DR PIRSF; PIRSF000970; CNPase; 1.
DR SUPFAM; SSF55144; LigT-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000970};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000970};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR000970}.
FT DOMAIN 185..418
FT /note="Cyclic nucleotide phosphodiesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05881"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-1"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-1"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-2"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-2"
SQ SEQUENCE 419 AA; 47197 MW; A9156BE2C881FF15 CRC64;
MNRSISRKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLHECK TLFILRGLPG
SGKSTLSRVI VDKYHDGTKM VSADAYKITP GARGAFSEEY KRLDEDLAAY CRRNIRVLVL
DDTNHEPERL EQLFELADQY QYQVVLVEPK TTWRLDCTQL KEKNQWQLSA DDLKKLKPGL
EKDFLPLYFG WFLTSKSSEI LRKVGQVFLE ELGNHKAFKK ELRHFISGDE HKEKIDLITY
FGKRPPGVLH CTTKFCQYGK AAGAEDYGQQ DVVKKSYGKA FTLTISALFV TPKTAGARVE
LSEQELLLWP DDVDKLSSDN LPRGSRAHIT LGCAADVEAV QTGIDLLEIV RQEKGGSRGE
EVGDLTRGKL YSLGSGRWML SLAKKMEVKT IFTGYYGKGK PVPTHGSRKG GALQSCIII
//
