CN37_RAT
ID CN37_RAT Reviewed; 420 AA.
AC P13233; Q4V796; Q64575;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000305};
DE Short=CNP;
DE Short=CNPase;
DE EC=3.1.4.37 {ECO:0000250|UniProtKB:P06623};
DE Flags: Precursor;
GN Name=Cnp {ECO:0000312|RGD:2368}; Synonyms=Cnp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3040924; DOI=10.1523/jneurosci.07-09-02703.1987;
RA Bernier L., Alvarez F., Norgard E.M., Raible D.W., Mentaberry A.,
RA Schembri J.G., Sabatini D.D., Colman D.R.;
RT "Molecular cloning of a 2',3'-cyclic nucleotide 3'-phosphodiesterase: mRNAs
RT with different 5' ends encode the same set of proteins in nervous and
RT lymphoid tissues.";
RL J. Neurosci. 7:2703-2710(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7932861; DOI=10.1002/jnr.490380302;
RA Gravel M., DeAngelis D., Braun P.E.;
RT "Molecular cloning and characterization of rat brain 2',3'-cyclic
RT nucleotide 3'-phosphodiesterase isoform 2.";
RL J. Neurosci. Res. 38:243-247(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-15; 20-63; 80-87; 94-112; 117-150; 155-202; 204-216;
RP 224-274; 283-368 AND 379-410, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP ISOPRENYLATION AT CYS-417, AND MUTAGENESIS OF CYS-417.
RX PubMed=7884818; DOI=10.1002/jnr.490390405;
RA De Angelis D.A., Braun P.E.;
RT "Isoprenylation of brain 2',3'-cyclic nucleotide 3'-phosphodiesterase
RT modulates cell morphology.";
RL J. Neurosci. Res. 39:386-397(1994).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-227; SER-239;
RP THR-262 AND SER-358, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP STRUCTURE BY NMR OF 184-398 IN COMPLEX WITH PHOSPHATE, AND MUTAGENESIS OF
RP HIS-250; THR-252; HIS-329; THR-331 AND GLY-344.
RX PubMed=12947117; DOI=10.1074/jbc.m305176200;
RA Kozlov G., Lee J., Elias D., Gravel M., Gutierrez P., Ekiel I., Braun P.E.,
RA Gehring K.;
RT "Structural evidence that brain cyclic nucleotide phosphodiesterase is a
RT member of the 2H phosphodiesterase superfamily.";
RL J. Biol. Chem. 278:46021-46028(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40939.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA40939.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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; M18630; AAA40939.1; ALT_SEQ; mRNA.
DR EMBL; L16532; AAA64429.1; -; mRNA.
DR EMBL; BC098066; AAH98066.1; -; mRNA.
DR PIR; A45670; A45670.
DR PIR; I56577; I56577.
DR RefSeq; NP_036941.1; NM_012809.2.
DR PDB; 2ILX; NMR; -; A=184-398.
DR PDBsum; 2ILX; -.
DR AlphaFoldDB; P13233; -.
DR BMRB; P13233; -.
DR SMR; P13233; -.
DR BioGRID; 247315; 7.
DR IntAct; P13233; 3.
DR MINT; P13233; -.
DR STRING; 10116.ENSRNOP00000023875; -.
DR CarbonylDB; P13233; -.
DR iPTMnet; P13233; -.
DR PhosphoSitePlus; P13233; -.
DR SwissPalm; P13233; -.
DR jPOST; P13233; -.
DR PaxDb; P13233; -.
DR PRIDE; P13233; -.
DR Ensembl; ENSRNOT00000103289; ENSRNOP00000080276; ENSRNOG00000017496.
DR GeneID; 25275; -.
DR KEGG; rno:25275; -.
DR UCSC; RGD:2368; rat.
DR CTD; 1267; -.
DR RGD; 2368; Cnp.
DR eggNOG; KOG2401; Eukaryota.
DR GeneTree; ENSGT00510000048410; -.
DR HOGENOM; CLU_039178_0_0_1; -.
DR InParanoid; P13233; -.
DR OMA; VEPKTSW; -.
DR OrthoDB; 1248632at2759; -.
DR PhylomeDB; P13233; -.
DR TreeFam; TF332157; -.
DR BRENDA; 3.1.4.37; 5301.
DR BRENDA; 3.1.4.58; 5301.
DR EvolutionaryTrace; P13233; -.
DR PRO; PR:P13233; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017496; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P13233; RN.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:RGD.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031143; C:pseudopodium; IDA:RGD.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:RGD.
DR GO; GO:0030551; F:cyclic nucleotide binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Phosphoprotein; Prenylation; Reference proteome; RNA-binding.
FT CHAIN 1..417
FT /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT /id="PRO_0000089963"
FT PROPEP 418..420
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000422299"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT ACT_SITE 329
FT /note="Proton donor"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 417
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 417
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:7884818"
FT MUTAGEN 250
FT /note="H->L: Reduces activity 15000-fold."
FT /evidence="ECO:0000269|PubMed:12947117"
FT MUTAGEN 252
FT /note="T->A: Reduces activity 100-fold."
FT /evidence="ECO:0000269|PubMed:12947117"
FT MUTAGEN 329
FT /note="H->L: Reduces activity 15000-fold."
FT /evidence="ECO:0000269|PubMed:12947117"
FT MUTAGEN 331
FT /note="T->A: Reduces activity 700-fold."
FT /evidence="ECO:0000269|PubMed:12947117"
FT MUTAGEN 344
FT /note="G->A: Alters secondary structure and lowers
FT activity."
FT /evidence="ECO:0000269|PubMed:12947117"
FT MUTAGEN 417
FT /note="C->S: Abolishes binding to myelin."
FT /evidence="ECO:0000269|PubMed:7884818"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 195..213
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2ILX"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:2ILX"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:2ILX"
FT STRAND 379..396
FT /evidence="ECO:0007829|PDB:2ILX"
SQ SEQUENCE 420 AA; 47268 MW; 83001BBA2C057826 CRC64;
MSTSFARKSH TFLPKIFFRK MSSSGAKDKP ELQFPFLQDE DTVATLHECK TLFILRGLPG
SGKSTLARLI VEKYHNGTKM VSADAYKIIP GSRADFSEEY KRLDEDLAGY CRRDIRVLVL
DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSL DDLKKLKPGL
EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLDLVSY
FGKRPPGVLH CTTKFCDYGK ATGAEEYAQQ DVVRRSYGKA FKLSISALFV TPKTAGAQVV
LNEQELQLWP SDLDKPSSSE SLPPGSRAHV TLGCAADVQP VQTGLDLLEI LQQVKGGSQG
EEVGELPRGK LYSLGKGRWM LSLAKKMEVK AIFTGYYGKG KPVPVHGSRK GGAMQICTII
