ENPP2_CAEEL
ID ENPP2_CAEEL Reviewed; 743 AA.
AC P90755; Q1NZ14;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase C27A7.3;
DE EC=3.1.-.-;
GN ORFNames=C27A7.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Probable phosphodiesterase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q13822};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q13822};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q13822};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P90755-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P90755-2; Sequence=VSP_020300;
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; Z81041; CAB02785.3; -; Genomic_DNA.
DR EMBL; Z81041; CAJ90515.1; -; Genomic_DNA.
DR PIR; T19495; T19495.
DR RefSeq; NP_001041087.1; NM_001047622.2. [P90755-1]
DR RefSeq; NP_001041088.1; NM_001047623.2. [P90755-2]
DR AlphaFoldDB; P90755; -.
DR SMR; P90755; -.
DR STRING; 6239.C27A7.3a; -.
DR PaxDb; P90755; -.
DR PeptideAtlas; P90755; -.
DR EnsemblMetazoa; C27A7.3a.1; C27A7.3a.1; WBGene00007755. [P90755-1]
DR EnsemblMetazoa; C27A7.3b.1; C27A7.3b.1; WBGene00007755. [P90755-2]
DR GeneID; 179665; -.
DR KEGG; cel:CELE_C27A7.3; -.
DR UCSC; C27A7.3a; c. elegans. [P90755-1]
DR CTD; 179665; -.
DR WormBase; C27A7.3a; CE39479; WBGene00007755; -. [P90755-1]
DR WormBase; C27A7.3b; CE40021; WBGene00007755; -. [P90755-2]
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00970000196710; -.
DR InParanoid; P90755; -.
DR OMA; HCLFWVG; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; P90755; -.
DR Reactome; R-CEL-196843; Vitamin B2 (riboflavin) metabolism.
DR PRO; PR:P90755; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007755; Expressed in adult organism and 1 other tissue.
DR ExpressionAtlas; P90755; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR029897; ENPP_nematoda.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF106; PTHR10151:SF106; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Calcium; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..743
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT C27A7.3"
FT /id="PRO_0000248537"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..743
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 639
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q13822"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020300"
SQ SEQUENCE 743 AA; 84412 MW; 3484943B2A0738E8 CRC64;
MSNRVVDVNS KKTGTSWKKK LMKIVIWSLA MLSFIAGLVL LGLVAAATIS GSKNLPTAEY
KWAGCENLGK CQIDGFSTPP LVILSFDGFA KEYLERRIVK SLELIAECGV KADRVYPSFP
SKTFPNHYTM VTGLYPESHG ITDNYVFDPN LYPELLAMRK HEAKEFYQAE PIWSAYKRLT
GNRVHCLFWV GCYYNITGYM PDVSPDYNQE LPLKERIDTL IGWLKLPETE RPALITAYLH
EPDQAGHMQK NVNQELEEVN NYIDILMKAL HDENLLECVN LVIVSDHGMQ ALNNSIEVET
IVNMDGLVLS KGVVARIHLN ETDRSIDEVA GEIRCKIDGV KVNTINDIPL RKHYSKSKRV
GDIIIEGKPG TSFYKSETNL GDHGYDYHNE NMHTVMFARG PSFLQNVTVP SFQNVQYMNL
WLYLLGLEGT VDNNGTIGFF DSILKNPPIR ENKWDSMEEC LNFGSAEVLQ CDKAEGHDLK
KLSLHLENCK EHQNLPIYSK NNCFQSYCEN SLIIHKNRQD VRKGVIESLT FSFSRNQSVF
ENSFSFVNTK YSIECPKLDT KDNFFTAGSE AISKLANAQY KFPSSFMKSE LISSLLSLKD
ETIKFVDIWV PLSIKTDEYL KHYGKLFVLS GLAVDRNLDG IADDEESKEP THFYRILITC
TGNWLSTNPP LCKKYSDTKA LAFVFPILNK KTTMDCMDSD AILLDYTSTI EDVENIASFQ
FQIGALSHQQ NVYLRRNITT SLW
