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Q924C3

- ENPP1_RAT

UniProt

Q924C3 - ENPP1_RAT

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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
A dinucleotide + H2O = 2 mononucleotides.

Cofactori

Binds 2 zinc ions per subunit.By similarity

Enzyme regulationi

At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei84 – 852CleavageBy similarity
Metal bindingi200 – 2001Zinc 1; catalyticBy similarity
Active sitei238 – 2381AMP-threonine intermediateBy similarity
Metal bindingi238 – 2381Zinc 1; catalyticBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity
Binding sitei322 – 3221SubstrateBy similarity
Metal bindingi358 – 3581Zinc 2; catalyticBy similarity
Metal bindingi362 – 3621Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi405 – 4051Zinc 1; catalyticBy similarity
Metal bindingi406 – 4061Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi517 – 5171Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi781 – 7811CalciumBy similarity
Metal bindingi783 – 7831CalciumBy similarity
Metal bindingi785 – 7851CalciumBy similarity
Metal bindingi787 – 7871Calcium; via carbonyl oxygenBy similarity
Metal bindingi789 – 7891CalciumBy similarity
Sitei896 – 8961Essential for catalytic activityBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. NADH pyrophosphatase activity Source: UniProtKB-EC
  3. nucleic acid binding Source: InterPro
  4. nucleotide diphosphatase activity Source: UniProtKB
  5. phosphodiesterase I activity Source: UniProtKB
  6. polysaccharide binding Source: InterPro
  7. scavenger receptor activity Source: InterPro
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: UniProtKB
  2. biomineral tissue development Source: UniProtKB-KW
  3. immune response Source: InterPro
  4. nucleic acid phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ924C3.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Short name:
E-NPP 1
Alternative name(s):
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-1
Including the following 2 domains:
Alkaline phosphodiesterase I (EC:3.1.4.1)
Nucleotide pyrophosphatase (EC:3.6.1.9)
Short name:
NPPase
Gene namesi
Name:Enpp1
Synonyms:Npps, Pc1, Pdnp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi628825. Enpp1.

Subcellular locationi

Cell membrane By similarity; Single-pass type II membrane protein By similarity. Basolateral cell membrane By similarity; Single-pass type II membrane protein By similarity. Secreted By similarity
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 (By similarity).By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 906906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1PRO_0000188566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 104PROSITE-ProRule annotation
Disulfide bondi94 ↔ 122PROSITE-ProRule annotation
Disulfide bondi102 ↔ 115PROSITE-ProRule annotation
Disulfide bondi108 ↔ 114PROSITE-ProRule annotation
Disulfide bondi131 ↔ 148PROSITE-ProRule annotation
Disulfide bondi136 ↔ 166PROSITE-ProRule annotation
Disulfide bondi146 ↔ 159PROSITE-ProRule annotation
Disulfide bondi152 ↔ 158PROSITE-ProRule annotation
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi177 ↔ 223PROSITE-ProRule annotation
Disulfide bondi185 ↔ 397PROSITE-ProRule annotation
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi413 ↔ 512PROSITE-ProRule annotation
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi462 ↔ 849PROSITE-ProRule annotation
Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi596 ↔ 653PROSITE-ProRule annotation
Disulfide bondi607 ↔ 707PROSITE-ProRule annotation
Disulfide bondi609 ↔ 692PROSITE-ProRule annotation
Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi819 ↔ 829PROSITE-ProRule annotation

Post-translational modificationi

A secreted form is produced through cleavage at Lys-85 by intracellular processing.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ924C3.
PRIDEiQ924C3.

PTM databases

PhosphoSiteiQ924C3.

Expressioni

Gene expression databases

GenevestigatoriQ924C3.

Interactioni

Subunit structurei

Homodimer. The secreted form is monomeric. Interacts with INSR (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-4997931.

Structurei

3D structure databases

ProteinModelPortaliQ924C3.
SMRiQ924C3. Positions 129-171.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5858CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini80 – 906827ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei59 – 7921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 12641SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 17044SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 573401PhosphodiesteraseAdd
BLAST
Regioni579 – 62850LinkerBy similarityAdd
BLAST
Regioni635 – 906272NucleaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi27 – 348Di-leucine motif

Domaini

The di-leucine motif is required for basolateral targeting in epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.By similarity

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiQ924C3.
KOiK01513.
PhylomeDBiQ924C3.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q924C3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART
60 70 80 90 100
AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS
110 120 130 140 150
NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD
160 170 180 190 200
DCKAHNDCCI NYSSVCQEKK SWVEEACETI DAPQCPAEFE SPPTLLFSLD
210 220 230 240 250
GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP NHYSIVTGLY
260 270 280 290 300
PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG
310 320 330 340 350
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY
360 370 380 390 400
TLYLEEPDSS GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL
410 420 430 440 450
ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTEVPETYYS
460 470 480 490 500
FNYEALAKNL SCRETNQHFR PYLKHFLPKR LHFAKNDRIE PLTFYLDPQW
510 520 530 540 550
QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE
560 570 580 590 600
VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS
610 620 630 640 650
VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH
660 670 680 690 700
RVCLLHQQQF LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP
710 720 730 740 750
LSPMHKCSYY KSTSKLSYGF LTPPRLNRVS RQIYSEALLT SNIVPMYQSF
760 770 780 790 800
QVIWQYLHDT VLRRYAQERN GVNVVSGPVF DFDYDGRYDS SEILKQNTRV
810 820 830 840 850
IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP HRPDNIESCT
860 870 880 890 900
HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP

IFSQED
Length:906
Mass (Da):102,942
Last modified:September 19, 2002 - v2
Checksum:i71F56780B279A919
GO
Isoform 1 (identifier: Q924C3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-630: Missing.

Show »
Length:905
Mass (Da):102,843
Checksum:i46EE88917B4BBCD3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti440 – 4423RPT → NPP in strain: Wistar.
Natural varianti457 – 4571A → T in strain: Lewis.
Natural varianti555 – 5551M → I in strain: Lewis.
Natural varianti568 – 5681E → G in strain: Wistar.
Natural varianti583 – 5831T → I in strain: Lewis.
Natural varianti592 – 5921F → V in strain: Lewis.
Natural varianti624 – 6241N → K in strain: Lewis.
Natural varianti640 – 6401N → H in strain: Lewis.
Natural varianti774 – 7741V → I in strain: Lewis.
Natural varianti806 – 8061N → I in strain: Lewis.
Natural varianti850 – 8501T → I in strain: Lewis.
Natural varianti898 – 8981H → Q in strain: Lewis.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei630 – 6301Missing in isoform 1. 1 PublicationVSP_006749

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF340185 mRNA. Translation: AAK69653.1.
AF340186 mRNA. Translation: AAK69654.1.
AF320054 mRNA. Translation: AAL26912.1.
RefSeqiNP_445987.1. NM_053535.1. [Q924C3-1]
UniGeneiRn.1199.

Genome annotation databases

GeneIDi85496.
KEGGirno:85496.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF340185 mRNA. Translation: AAK69653.1 .
AF340186 mRNA. Translation: AAK69654.1 .
AF320054 mRNA. Translation: AAL26912.1 .
RefSeqi NP_445987.1. NM_053535.1. [Q924C3-1 ]
UniGenei Rn.1199.

3D structure databases

ProteinModelPortali Q924C3.
SMRi Q924C3. Positions 129-171.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4997931.

PTM databases

PhosphoSitei Q924C3.

Proteomic databases

PaxDbi Q924C3.
PRIDEi Q924C3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 85496.
KEGGi rno:85496.

Organism-specific databases

CTDi 5167.
RGDi 628825. Enpp1.

Phylogenomic databases

eggNOGi COG1524.
HOGENOMi HOG000037439.
HOVERGENi HBG051484.
InParanoidi Q924C3.
KOi K01513.
PhylomeDBi Q924C3.

Enzyme and pathway databases

SABIO-RK Q924C3.

Miscellaneous databases

NextBioi 617598.
PROi Q924C3.

Gene expression databases

Genevestigatori Q924C3.

Family and domain databases

Gene3Di 3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
PANTHERi PTHR10151. PTHR10151. 1 hit.
Pfami PF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view ]
PRINTSi PR00022. SOMATOMEDINB.
SMARTi SM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.
    Eur. J. Immunogenet. 29:307-313(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS.
    Strain: Lewis, Louvain and Wistar.
  2. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiENPP1_RAT
AccessioniPrimary (citable) accession number: Q924C3
Secondary accession number(s): Q91XQ3, Q920C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: October 29, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-35 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3