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Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 (E-NPP 1) (Phosphodiesterase I/nucleotide pyrophosphatase 1) (Plasma-cell membrane glycoprotein PC-1) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 ENPP1_RAT               Reviewed;         906 AA.
Q924C3; Q91XQ3; Q920C8;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
22-NOV-2017, entry version 121.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1;
Short=E-NPP 1;
AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 1;
AltName: Full=Plasma-cell membrane glycoprotein PC-1;
Includes:
RecName: Full=Alkaline phosphodiesterase I;
EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000250|UniProtKB:P06802};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=Enpp1; Synonyms=Npps, Pc1, Pdnp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS.
STRAIN=Lewis, Louvain, and Wistar;
PubMed=12121276; DOI=10.1046/j.1365-2370.2002.00330.x;
Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.;
"Structural basis of allotypes of ecto-nucleotide
pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein
PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic
antibodies.";
Eur. J. Immunogenet. 29:307-313(2002).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND THR-238, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: By generating PPi, plays a role in regulating
pyrophosphate levels, and functions in bone mineralization and
soft tissue calcification. PPi inhibits mineralization by binding
to nascent hydroxyapatite (HA) crystals, thereby preventing
further growth of these crystals. Preferentially hydrolyzes ATP,
but can also hydrolyze other nucleoside 5' triphosphates such as
GTP, CTP, TTP and UTP to their corresponding monophosphates with
release of pyrophosphate and diadenosine polyphosphates, and also
3',5'-cAMP to AMP. May also be involved in the regulation of the
availability of nucleotide sugars in the endoplasmic reticulum and
Golgi, and the regulation of purinergic signaling. Appears to
modulate insulin sensitivity. {ECO:0000250|UniProtKB:P22413}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000250|UniProtKB:P06802}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000250|UniProtKB:P06802}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P06802};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000250|UniProtKB:P06802};
-!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
intermediate is formed which inhibits further hydrolysis.
-!- SUBUNIT: Homodimer. The secreted form is monomeric. Interacts with
INSR. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P22413}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P22413}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P22413}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P22413}. Secreted
{ECO:0000250|UniProtKB:P22413}. Note=Targeted to the basolateral
membrane in polarized epithelial cells and in hepatocytes, and to
matrix vesicles in osteoblasts. In bile duct cells and cancer
cells, located to the apical cytoplasmic side. The proteolytically
processed form is secreted. {ECO:0000250|UniProtKB:P22413}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=Q924C3-1; Sequence=Displayed;
Name=1;
IsoId=Q924C3-2; Sequence=VSP_006749;
-!- DOMAIN: The di-leucine motif is required for basolateral targeting
in epithelial cells, and for targeting to matrix vesicles derived
from mineralizing cells. {ECO:0000250}.
-!- PTM: A secreted form is produced through cleavage at Lys-85 by
intracellular processing. {ECO:0000250|UniProtKB:P06802}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF340185; AAK69653.1; -; mRNA.
EMBL; AF340186; AAK69654.1; -; mRNA.
EMBL; AF320054; AAL26912.1; -; mRNA.
RefSeq; NP_445987.1; NM_053535.1. [Q924C3-1]
UniGene; Rn.1199; -.
ProteinModelPortal; Q924C3; -.
SMR; Q924C3; -.
MINT; MINT-4997931; -.
STRING; 10116.ENSRNOP00000019519; -.
iPTMnet; Q924C3; -.
PhosphoSitePlus; Q924C3; -.
PaxDb; Q924C3; -.
PRIDE; Q924C3; -.
GeneID; 85496; -.
KEGG; rno:85496; -.
CTD; 5167; -.
RGD; 628825; Enpp1.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; Q924C3; -.
KO; K01513; -.
PhylomeDB; Q924C3; -.
BRENDA; 3.1.4.1; 5301.
BRENDA; 3.6.1.9; 5301.
SABIO-RK; Q924C3; -.
PRO; PR:Q924C3; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0097440; C:apical dendrite; IDA:RGD.
GO; GO:0097441; C:basilar dendrite; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044297; C:cell body; IDA:RGD.
GO; GO:0042995; C:cell projection; IDA:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004527; F:exonuclease activity; ISO:RGD.
GO; GO:0005158; F:insulin receptor binding; ISO:RGD.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISO:RGD.
GO; GO:0004551; F:nucleotide diphosphatase activity; ISS:UniProtKB.
GO; GO:0004528; F:phosphodiesterase I activity; IDA:RGD.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0046849; P:bone remodeling; ISO:RGD.
GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:RGD.
GO; GO:0071468; P:cellular response to acidic pH; IEP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0030505; P:inorganic diphosphate transport; ISO:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
GO; GO:0046325; P:negative regulation of glucose import; ISO:RGD.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; ISO:RGD.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:RGD.
GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:RGD.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:RGD.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:RGD.
GO; GO:0021772; P:olfactory bulb development; IEP:RGD.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0030730; P:sequestering of triglyceride; ISO:RGD.
GO; GO:0021756; P:striatum development; IEP:RGD.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR020436; Somatomedin_B_chordata.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
PRINTS; PR00022; SOMATOMEDINB.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 2.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 2.
PROSITE; PS00524; SMB_1; 2.
PROSITE; PS50958; SMB_2; 2.
1: Evidence at protein level;
Alternative splicing; Biomineralization; Calcium; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal-anchor; Transmembrane; Transmembrane helix;
Zinc.
CHAIN 1 906 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 1.
/FTId=PRO_0000188566.
TOPO_DOM 1 58 Cytoplasmic. {ECO:0000255}.
TRANSMEM 59 79 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 80 906 Extracellular. {ECO:0000255}.
DOMAIN 86 126 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 127 170 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 173 573 Phosphodiesterase.
REGION 579 628 Linker. {ECO:0000250}.
REGION 635 906 Nuclease.
MOTIF 27 34 Di-leucine motif.
ACT_SITE 238 238 AMP-threonine intermediate.
{ECO:0000250}.
METAL 200 200 Zinc 1; catalytic. {ECO:0000250}.
METAL 238 238 Zinc 1; catalytic. {ECO:0000250}.
METAL 358 358 Zinc 2; catalytic. {ECO:0000250}.
METAL 362 362 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 405 405 Zinc 1; catalytic. {ECO:0000250}.
METAL 406 406 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 517 517 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 781 781 Calcium. {ECO:0000250}.
METAL 783 783 Calcium. {ECO:0000250}.
METAL 785 785 Calcium. {ECO:0000250}.
METAL 787 787 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 789 789 Calcium. {ECO:0000250}.
BINDING 259 259 Substrate. {ECO:0000250}.
BINDING 277 277 Substrate. {ECO:0000250}.
BINDING 322 322 Substrate. {ECO:0000250}.
SITE 84 85 Cleavage. {ECO:0000250}.
SITE 896 896 Essential for catalytic activity.
{ECO:0000250}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 90 104 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 94 122 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 102 115 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 108 114 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 131 148 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 136 166 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 146 159 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 152 158 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 177 223 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 185 397 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 413 512 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 462 849 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 596 653 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 607 707 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 609 692 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 819 829 {ECO:0000255|PROSITE-ProRule:PRU00350}.
VAR_SEQ 630 630 Missing (in isoform 1).
{ECO:0000303|PubMed:12121276}.
/FTId=VSP_006749.
VARIANT 440 442 RPT -> NPP (in strain: Wistar).
VARIANT 457 457 A -> T (in strain: Lewis).
VARIANT 555 555 M -> I (in strain: Lewis).
VARIANT 568 568 E -> G (in strain: Wistar).
VARIANT 583 583 T -> I (in strain: Lewis).
VARIANT 592 592 F -> V (in strain: Lewis).
VARIANT 624 624 N -> K (in strain: Lewis).
VARIANT 640 640 N -> H (in strain: Lewis).
VARIANT 774 774 V -> I (in strain: Lewis).
VARIANT 806 806 N -> I (in strain: Lewis).
VARIANT 850 850 T -> I (in strain: Lewis).
VARIANT 898 898 H -> Q (in strain: Lewis).
SEQUENCE 906 AA; 102942 MW; 71F56780B279A919 CRC64;
MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART AKDPNTYKVL
SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE
TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKAHNDCCI NYSSVCQEKK SWVEEACETI
DAPQCPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP
NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY TLYLEEPDSS
GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN
KYLGDVNNVK VVYGPAARLR PTEVPETYYS FNYEALAKNL SCRETNQHFR PYLKHFLPKR
LHFAKNDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG
AEVDSFENIE VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS
VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH RVCLLHQQQF
LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP LSPMHKCSYY KSTSKLSYGF
LTPPRLNRVS RQIYSEALLT SNIVPMYQSF QVIWQYLHDT VLRRYAQERN GVNVVSGPVF
DFDYDGRYDS SEILKQNTRV IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP
HRPDNIESCT HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP
IFSQED


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