ID A0A2Y9LWQ8_DELLE Unreviewed; 420 AA.
AC A0A2Y9LWQ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|RefSeq:XP_022413840.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022413840.1};
RN [1] {ECO:0000313|RefSeq:XP_022413840.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022413840.1};
RG RefSeq;
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 RefSeq; XP_022413840.1; XM_022558132.1.
DR AlphaFoldDB; A0A2Y9LWQ8; -.
DR STRING; 9749.A0A2Y9LWQ8; -.
DR Ensembl; ENSDLET00000015087; ENSDLEP00000013654; ENSDLEG00000010017.
DR KEGG; dle:111166446; -.
DR InParanoid; A0A2Y9LWQ8; -.
DR OrthoDB; 5489998at2759; -.
DR Proteomes; UP000248483; Unplaced.
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:UP000248483};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR000970}.
FT DOMAIN 185..419
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 329
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 331
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-2"
SQ SEQUENCE 420 AA; 47239 MW; AA32793E4D110A58 CRC64;
MNRGFSRKSQ TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE ETVAALQECK TLFILRGLPG
SGKSTLARVI VDRYRDGTKM VSADTYKINP GARGAFSEEY KQLDEDLATY CRRDVRVLVL
DDTNHERERL EQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL
EKDFLPLYFG WFLTKKSSEG LRKAGQAFLE ELGNHKAFKK ELRHFVSGDE PREKIELVTY
FGKRPPGVLH CTTKFCDYGK AAGADEYAQQ DVVKKSYCKA FTLTISALFV TPKTTGARVE
LSEQELALWP NDVDKLSPSD SLSRGSRAHI TLGCAGDVEA VQTGIDLLEI VKQEKGGNRG
EEVGELSRGK LYSLGSGRWM LNLAKKMEVR AIFTGYYGKG KAVPTRGGRK GGAFQSCTII
//
