ID A0A7L0JLR6_CHATO Unreviewed; 421 AA. AC A0A7L0JLR6; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-NOV-2024, entry version 16. DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000256|ARBA:ARBA00014478}; DE EC=3.1.4.37 {ECO:0000256|ARBA:ARBA00012317}; DE Flags: Fragment; GN Name=Cnp_0 {ECO:0000313|EMBL:NXK44373.1}; GN ORFNames=CHATOR_R00288 {ECO:0000313|EMBL:NXK44373.1}; OS Chauna torquata (Southern screamer). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anhimidae; OC Chauna. OX NCBI_TaxID=30388 {ECO:0000313|EMBL:NXK44373.1, ECO:0000313|Proteomes:UP000537522}; RN [1] {ECO:0000313|EMBL:NXK44373.1, ECO:0000313|Proteomes:UP000537522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-011-36 {ECO:0000313|EMBL:NXK44373.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXK44373.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'- CC cyclic substrates. May participate in RNA metabolism in the myelinating CC cell, CNP is the third most abundant protein in central nervous system CC myelin. {ECO:0000256|ARBA:ARBA00045937}. 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 -!- SUBUNIT: Exists as monomers and homodimers. CC {ECO:0000256|ARBA:ARBA00011781}. 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NXK44373.1}. 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; VXAL01000611; NXK44373.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7L0JLR6; -. DR Proteomes; UP000537522; Unassembled WGS sequence. 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-EC. DR GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro. DR FunFam; 3.40.50.300:FF:000795; Tetratricopeptide repeat protein 25; 1. DR FunFam; 3.90.1740.10:FF:000001; Tetratricopeptide repeat protein 25; 1. 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; 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}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Methylation {ECO:0000256|ARBA:ARBA00022481}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Prenylation {ECO:0000256|ARBA:ARBA00023289}; KW Reference proteome {ECO:0000313|Proteomes:UP000537522}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}. FT DOMAIN 184..420 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" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXK44373.1" FT NON_TER 421 FT /evidence="ECO:0000313|EMBL:NXK44373.1" SQ SEQUENCE 421 AA; 47651 MW; DCF009F5998E1D42 CRC64; NRGFSKKSHT LLPKIFRKMS TQSAKERPES LQFHFLDDED TISTLKESKT FFILRGLPGS GKSTLAQAIQ DRYKDACKVI SVDSYKITPV IRSSIPEEYS KVDEDLVDYC KRDISVIVLD DTHHERERLD QLFDIADKYR YKVIFAEPKT QWRMDCSQLK EKNQWKLSVE DLKKMKPSLE KEFLPMYFGW FLSKRSSEIL RKAGQVFLDE LGSFKAFKKE SKYFASAIED PKIKIDLTSY FVKRPPGVLH CTTKYTEFGK AAGAEEYAQQ EAVKASYGKS FTLSISALFI TTKTVGARVE LNEQQLLLWP GDADKLLSTD NLPKGSRAHI TLGCANGIEA VQTGLDLLEF VKLEKTGNKG DEVGEIGGGK LQYFDNGMWM LVLSKKIDVR AIFSGYYGKG KLVPTQSTNK RGSAFSSCTI I //