CN37_BOVIN
ID CN37_BOVIN Reviewed; 400 AA.
AC P06623; Q3SZJ6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 147.
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:0000269|PubMed:6272743};
DE AltName: Full=Elastase 2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000303|PubMed:3029107, ECO:0000303|PubMed:6272743};
DE Flags: Precursor;
GN Name=CNP {ECO:0000250|UniProtKB:P09543};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 150-385.
RC TISSUE=Brain;
RX PubMed=3029107; DOI=10.1016/s0021-9258(18)61498-x;
RA Kurihara T., Fowler A.V., Takahashi Y.;
RT "cDNA cloning and amino acid sequence of bovine brain 2',3'-cyclic-
RT nucleotide 3'-phosphodiesterase.";
RL J. Biol. Chem. 262:3256-3261(1987).
RN [2]
RP ERRATUM OF PUBMED:3029107, AND SEQUENCE REVISION TO 318.
RA Kurihara T., Fowler A.V., Takahashi Y.;
RL J. Biol. Chem. 262:16754-16754(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=2821502; DOI=10.1093/nar/15.17.7204;
RA Vogel U.S., Thompson R.J.;
RT "Nucleotide sequence of bovine retina 2',3'-cyclic nucleotide 3'-
RT phosphohydrolase.";
RL Nucleic Acids Res. 15:7204-7204(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3036592; DOI=10.1016/0014-5793(87)81058-x;
RA Vogel U.S., Thompson R.J.;
RT "Molecular cloning of the myelin specific enzyme 2',3'-cyclic-nucleotide
RT 3'-phosphohydrolase.";
RL FEBS Lett. 218:261-265(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6272743; DOI=10.1042/bj1950153;
RA Kurihara T., Nishizawa Y., Takahashi Y., Odani S.;
RT "Chemical, immunological and catalytic properties of 2':3'-cyclic
RT nucleotide 3'-phosphodiesterase purified from brain white matter.";
RL Biochem. J. 195:153-157(1981).
CC -!- FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-
CC cyclic substrates (PubMed:6272743). May participate in RNA metabolism
CC in the myelinating cell, CNP is the third most abundant protein in
CC central nervous system myelin (By similarity).
CC {ECO:0000250|UniProtKB:P16330, ECO:0000269|PubMed:6272743}.
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:0000269|PubMed:6272743};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for AMP {ECO:0000269|PubMed:6272743};
CC KM=0.40 mM for GMP {ECO:0000269|PubMed:6272743};
CC KM=6.3 mM for CMP {ECO:0000269|PubMed:6272743};
CC KM=7.1 mM for UMP {ECO:0000269|PubMed:6272743};
CC pH dependence:
CC Optimum pH is 6 (in the presence of both hexadecyltrimethylammonium
CC bromide and serum albumin). {ECO:0000269|PubMed:6272743};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:6272743};
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 -!- PTM: Met-1 may be removed after translation.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC family. {ECO:0000305}.
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DR EMBL; J02659; AAA30456.1; ALT_SEQ; mRNA.
DR EMBL; Y00405; CAA68466.1; -; mRNA.
DR EMBL; M27606; AAA30457.1; -; mRNA.
DR EMBL; BC102820; AAI02821.2; -; mRNA.
DR PIR; A26861; ESBOP3.
DR RefSeq; NP_851336.1; NM_180993.2.
DR RefSeq; XP_005220719.1; XM_005220662.2.
DR RefSeq; XP_010814515.1; XM_010816213.2.
DR AlphaFoldDB; P06623; -.
DR SMR; P06623; -.
DR IntAct; P06623; 1.
DR STRING; 9913.ENSBTAP00000036278; -.
DR PaxDb; P06623; -.
DR PRIDE; P06623; -.
DR Ensembl; ENSBTAT00000036420; ENSBTAP00000036278; ENSBTAG00000025762.
DR GeneID; 280752; -.
DR KEGG; bta:280752; -.
DR CTD; 1267; -.
DR VEuPathDB; HostDB:ENSBTAG00000025762; -.
DR VGNC; VGNC:27525; CNP.
DR eggNOG; KOG2401; Eukaryota.
DR GeneTree; ENSGT00510000048410; -.
DR HOGENOM; CLU_039178_0_0_1; -.
DR InParanoid; P06623; -.
DR OMA; VEPKTSW; -.
DR OrthoDB; 1248632at2759; -.
DR TreeFam; TF332157; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000025762; Expressed in floor plate of diencephalon and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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 Direct protein sequencing; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; RNA-binding.
FT CHAIN 1..397
FT /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT /id="PRO_0000089960"
FT PROPEP 398..400
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422295"
FT ACT_SITE 230
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 309
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09543"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13233"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13233"
FT MOD_RES 397
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 397
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 44875 MW; 3448FC367D647CF8 CRC64;
MSSSGAKDKP ELQFPFLQDE ETVATLQECK TLFILRGLPG SGKSTLARFI VDKYRDGTKM
VSADSYKITP GARGSFSEEY KQLDEDLAAC CRRDFRVLVL DDTNHERERL EQLFELADQY
QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL EKDFLPLYFG WFLTKKSSAA
LWKTGQTFLE ELGNHKAFKK ELRHFVSGDE PREKIELVTY FGKRPPGVLH CTTKFCDYGK
AAGAEEYAQQ DVVKKSYCKA FTLTISALFV TPKTTGARVE LSEQQLALWP NDVDKLSPSD
NLPRGSRAHI TLGCAGDVEA VQTGIDLLEI VRQEKGGSRG EEVGELSRGK LYSLGSGRWM
LSLAKKMEVR AIFTGYYGKG KAVPIRSGRK GGSFQSCTII
