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Q924C3

- ENPP1_RAT

UniProt

Q924C3 - ENPP1_RAT

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Protein
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Gene
Enpp1, Npps, Pc1, Pdnp1
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.

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 – 852Cleavage By similarity
Metal bindingi200 – 2001Zinc 1; catalytic By similarity
Active sitei238 – 2381AMP-threonine intermediate By similarity
Metal bindingi238 – 2381Zinc 1; catalytic By similarity
Binding sitei259 – 2591Substrate By similarity
Binding sitei277 – 2771Substrate By similarity
Binding sitei322 – 3221Substrate By similarity
Metal bindingi358 – 3581Zinc 2; catalytic By similarity
Metal bindingi362 – 3621Zinc 2; via tele nitrogen; catalytic By similarity
Metal bindingi405 – 4051Zinc 1; catalytic By similarity
Metal bindingi406 – 4061Zinc 1; via tele nitrogen; catalytic By similarity
Metal bindingi517 – 5171Zinc 2; via tele nitrogen; catalytic By similarity
Metal bindingi781 – 7811Calcium By similarity
Metal bindingi783 – 7831Calcium By similarity
Metal bindingi785 – 7851Calcium By similarity
Metal bindingi787 – 7871Calcium; via carbonyl oxygen By similarity
Metal bindingi789 – 7891Calcium By similarity
Sitei896 – 8961Essential for catalytic activity By similarity

GO - Molecular functioni

  1. NADH pyrophosphatase activity Source: UniProtKB-EC
  2. calcium ion binding Source: UniProtKB
  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; Single-pass type II membrane protein By similarity. Basolateral cell membrane; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5858Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei59 – 7921Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini80 – 906827Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB
  4. integral component of plasma membrane Source: UniProtKB
  5. 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 1
PRO_0000188566Add
BLAST

Amino acid modifications

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

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.

Protein-protein interaction databases

MINTiMINT-4997931.

Structurei

3D structure databases

ProteinModelPortaliQ924C3.
SMRiQ924C3. Positions 129-171.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 12641SMB 1
Add
BLAST
Domaini127 – 17044SMB 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 573401Phosphodiesterase
Add
BLAST
Regioni579 – 62850Linker By similarity
Add
BLAST
Regioni635 – 906272Nuclease
Add
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

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

MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART    50
AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS 100
NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD 150
DCKAHNDCCI NYSSVCQEKK SWVEEACETI DAPQCPAEFE SPPTLLFSLD 200
GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP NHYSIVTGLY 250
PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG 300
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY 350
TLYLEEPDSS GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL 400
ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTEVPETYYS 450
FNYEALAKNL SCRETNQHFR PYLKHFLPKR LHFAKNDRIE PLTFYLDPQW 500
QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE 550
VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS 600
VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH 650
RVCLLHQQQF LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP 700
LSPMHKCSYY KSTSKLSYGF LTPPRLNRVS RQIYSEALLT SNIVPMYQSF 750
QVIWQYLHDT VLRRYAQERN GVNVVSGPVF DFDYDGRYDS SEILKQNTRV 800
IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP HRPDNIESCT 850
HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP 900
IFSQED 906
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.
VSP_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: May 14, 2014
This is version 101 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi