ID   CN37_PONAB              Reviewed;         421 AA.
AC   Q5RFD0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000250|UniProtKB:P09543};
DE            Short=CNP;
DE            Short=CNPase;
DE            EC=3.1.4.37 {ECO:0000250|UniProtKB:P06623};
DE   Flags: Precursor;
GN   Name=CNP {ECO:0000250|UniProtKB:P09543};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-
CC       cyclic substrates (By similarity). May participate in RNA metabolism in
CC       the myelinating cell, CNP is the third most abundant protein in central
CC       nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P06623,
CC       ECO:0000250|UniProtKB:P16330}.
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:0000250|UniProtKB:P06623};
CC   -!- SUBUNIT: Exists as monomers and homodimers.
CC       {ECO:0000250|UniProtKB:P16330}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:P16330}. Melanosome
CC       {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane
CC       structures of brain white matter. {ECO:0000250|UniProtKB:P16330}.
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC       family. {ECO:0000305}.
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DR   EMBL; CR857228; CAH89527.1; -; mRNA.
DR   RefSeq; NP_001124663.1; NM_001131191.1.
DR   AlphaFoldDB; Q5RFD0; -.
DR   SMR; Q5RFD0; -.
DR   STRING; 9601.ENSPPYP00000009449; -.
DR   GeneID; 100171506; -.
DR   KEGG; pon:100171506; -.
DR   CTD; 1267; -.
DR   eggNOG; KOG2401; Eukaryota.
DR   InParanoid; Q5RFD0; -.
DR   OrthoDB; 1248632at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008431; CNPase.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10156; PTHR10156; 1.
DR   Pfam; PF05881; CNPase; 1.
DR   PIRSF; PIRSF000970; CNPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55144; SSF55144; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipoprotein; Membrane; Methylation; Phosphoprotein; Prenylation;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..418
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000290017"
FT   PROPEP          419..421
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000422298"
FT   ACT_SITE        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        330
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09543"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09543"
FT   MOD_RES         110
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P16330"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09543"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13233"
FT   MOD_RES         418
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           418
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  47580 MW;  12180A03D8AD398B CRC64;
     MNRGFSRKSH TFLPKIFFRK MSSSGTKDKP ELQFPFLQDE DTVATLQECK TLFILRGLPG
     SGKSTLARVI VDKYRDGTKM VSADAYKITP GARGAFSEEY KRLDEDLAAY CRRRDIRILV
     LDDTNHERER LEQLFEMADQ YQYQVVLVEP KTAWRLGCAQ LKEKNQWQLS ADDLKKLKPG
     LEKDFLPLYF GWFLTKKSSE TLRKAGQVFL EELGNHKAFK KELRQFIPGD EPREKMDLVT
     YFGKRPPGVL HCTTKFCDYG KAPGAEEYAQ QDVLKKSYSK AFTLTISALF VTPKTTGARV
     ELSEQQLQLW PSDVDKLSPT DNLPRGSRAH ITLGCAADVE AVQTGLDLLE ILRQEKGGSR
     GEEVGELSRG KLYSLGNGRW MLTLAKNMEV RAIFTGYYGK GKPVPTQGSR KGGALQSCTI
     I