ENPP5_RAT
ID ENPP5_RAT Reviewed; 477 AA.
AC P84039; Q5EAN9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 5;
DE Short=E-NPP 5;
DE Short=NPP-5;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=Enpp5;
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 [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 25-42, FUNCTION, LACK OF NUCLEOTIDE PYROPHOSPHATASE AND
RP LYSOPHOLIPASE D ACTIVITY, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Brain {ECO:0000269|PubMed:12927778};
RX PubMed=12927778; DOI=10.1016/s0006-291x(03)01454-2;
RA Ohe Y., Ohnishi H., Okazawa H., Tomizawa K., Kobayashi H., Okawa K.,
RA Matozaki T.;
RT "Characterization of nucleotide pyrophosphatase-5 as an oligomannosidic
RT glycoprotein in rat brain.";
RL Biochem. Biophys. Res. Commun. 308:719-725(2003).
RN [3]
RP PROTEIN SEQUENCE OF 30-45; 103-115; 215-220 AND 394-405, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Can hydrolyze NAD but cannot hydrolyze nucleotide di- and
CC triphosphates (By similarity). May play a role in neuronal cell
CC communication. Lacks nucleotide pyrophosphatase and lysopholipase D
CC activity in vitro (PubMed:12927778). {ECO:0000250|UniProtKB:Q9EQG7,
CC ECO:0000269|PubMed:12927778, ECO:0000303|PubMed:12927778}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9EQG7};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9EQG7};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:12927778}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12927778}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; BC090331; AAH90331.1; -; mRNA.
DR RefSeq; NP_001012762.1; NM_001012744.1.
DR RefSeq; XP_006244669.1; XM_006244607.3.
DR AlphaFoldDB; P84039; -.
DR SMR; P84039; -.
DR STRING; 10116.ENSRNOP00000013703; -.
DR GlyGen; P84039; 8 sites.
DR iPTMnet; P84039; -.
DR PhosphoSitePlus; P84039; -.
DR jPOST; P84039; -.
DR PaxDb; P84039; -.
DR PRIDE; P84039; -.
DR Ensembl; ENSRNOT00000013703; ENSRNOP00000013703; ENSRNOG00000010232.
DR GeneID; 316249; -.
DR KEGG; rno:316249; -.
DR UCSC; RGD:1359199; rat.
DR CTD; 59084; -.
DR RGD; 1359199; Enpp5.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000160562; -.
DR HOGENOM; CLU_017594_1_2_1; -.
DR InParanoid; P84039; -.
DR OMA; DEYVSRD; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; P84039; -.
DR TreeFam; TF330032; -.
DR PRO; PR:P84039; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000010232; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; P84039; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007154; P:cell communication; IDA:UniProtKB.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12927778"
FT CHAIN 25..477
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 5"
FT /id="PRO_0000188572"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000305"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG7"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:12927778"
FT CONFLICT 41
FT /note="D -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 54290 MW; 44DCDDAB98383E1B CRC64;
MIPEFLVVSC TLAALCHSVP LSLQTEQQKV LVVSFDGFRW DYLYKVPTPH FHYVMKNGVH
VKQVTNVFIT KTYPNHYTLV TGLFAENHGI VANDMFDPVL NKSFSLEHMN IYDSKFWEEA
TPLWITNQRA GHASGAAMWP GTDVKIHESY PTHYLPYNES VSFEDRVAKI IEWFTAKDPI
NLGFLYWEEP DDTGHDVGPD SPLMGPVISD IDHKLGYLIK MLKKAKLWNN INLIVTSDHG
MTQCSKERVI ELDQYLDKEH YTLIDHSPVA AILPKEGKFN EVYDALANAH PNLTVYKKEE
IPERWHYKHS DRVQPIVAVA DEGWYILQNK SDEFLLGNHG YDNALAEMHP IFLAHGPAFR
KNFTKEAMNS TDLYSLVCHL LNVTALPHNG SFRNVQDLLS SAAPKAIPYT QSTTLPLGSA
KPGEYEQEES YPYYIGISLG SLIAIVFFVV LIKHLIRSQM HTLQYMQVEV AQPLLQA
