ID A0A455C642_PHYMC Unreviewed; 400 AA.
AC A0A455C642;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_028355351.1,
GN ECO:0000313|RefSeq:XP_028355352.1, ECO:0000313|RefSeq:XP_028355353.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028355353.1};
RN [1] {ECO:0000313|RefSeq:XP_028355351.1, ECO:0000313|RefSeq:XP_028355352.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028355351.1,
RC ECO:0000313|RefSeq:XP_028355352.1};
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}.
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DR RefSeq; XP_028355351.1; XM_028499550.2.
DR RefSeq; XP_028355352.1; XM_028499551.2.
DR RefSeq; XP_028355353.1; XM_028499552.2.
DR Proteomes; UP000248484; Chromosome 14.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0009214; P:cyclic nucleotide catabolic process; IEA:UniProtKB-UniRule.
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:UP000248484};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR000970}.
FT DOMAIN 165..399
FT /note="Cyclic nucleotide phosphodiesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05881"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-1"
FT ACT_SITE 309
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-2"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000970-2"
SQ SEQUENCE 400 AA; 44823 MW; 7480F653E01347AA CRC64;
MSSSGPKDKP ELQFPFLQDE ETVATLQECK TLFILRGLPG SGKSTLARVI VDRYRDGTKM
VSADTYKITP GARGAFSEEY KRLDEDLAAY CRRDVRVLVL DDTNHERERL EQLFEMADQY
QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL EKDFLPLYFG WFLTKKSSEG
LRKAGQAFLE ELGNHKAFKK ELRHFVSGDE PREKIELVTY FGKRPPGVLH CTTKFCDYGK
AAGAEEYAQQ DVVKKSYCKA FTLTISALFV TPKTTGARVE LSEQELALWP NDVDKLSPSD
SLSRGSRAHI TLGCAGDVEA VQTGIDLLEI VKQEKGGNRG EEVGELSRGK LYSLGSGRWM
LNLAKKMEVR AIFTGYYGKG KAVPTRGGRK GGAFQSCTII
//
