ENPP1_CAEEL
ID ENPP1_CAEEL Reviewed; 829 AA.
AC P90754; Q2PJ70;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase C27A7.1;
DE EC=3.1.-.-;
GN ORFNames=C27A7.1;
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], AND ALTERNATIVE SPLICING.
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).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-424, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-424 AND ASN-649, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Probable phosphodiesterase. {ECO:0000250}.
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=P90754-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P90754-2; Sequence=VSP_020299;
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; Z81041; CAB02784.1; -; Genomic_DNA.
DR EMBL; Z81041; CAJ55253.1; -; Genomic_DNA.
DR PIR; T19494; T19494.
DR RefSeq; NP_001041085.1; NM_001047620.2. [P90754-1]
DR RefSeq; NP_001041086.1; NM_001047621.1. [P90754-2]
DR AlphaFoldDB; P90754; -.
DR SMR; P90754; -.
DR BioGRID; 44686; 2.
DR IntAct; P90754; 1.
DR STRING; 6239.C27A7.1a; -.
DR iPTMnet; P90754; -.
DR EPD; P90754; -.
DR PaxDb; P90754; -.
DR EnsemblMetazoa; C27A7.1a.1; C27A7.1a.1; WBGene00007753. [P90754-1]
DR EnsemblMetazoa; C27A7.1b.1; C27A7.1b.1; WBGene00007753. [P90754-2]
DR GeneID; 179663; -.
DR KEGG; cel:CELE_C27A7.1; -.
DR UCSC; C27A7.1a; c. elegans. [P90754-1]
DR CTD; 179663; -.
DR WormBase; C27A7.1a; CE08403; WBGene00007753; -. [P90754-1]
DR WormBase; C27A7.1b; CE39478; WBGene00007753; -. [P90754-2]
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00970000196710; -.
DR InParanoid; P90754; -.
DR OMA; PFRNRID; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; P90754; -.
DR PRO; PR:P90754; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007753; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; P90754; 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 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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..829
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT C27A7.1"
FT /id="PRO_0000248536"
FT TRANSMEM 54..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 439..782
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..12
FT /note="MRRSFYASSTEN -> MKTNLAQ (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020299"
SQ SEQUENCE 829 AA; 93165 MW; ED9961D0D18255F1 CRC64;
MRRSFYASST ENTPMMMTQA RVLSTGTTDN GTIRYDEVDE TKRWFNRRFC FLTVIGIAVL
LLAMVVIVVI VLLLTQLKAA NSNAQNAMSS SKVQLEELTR KLSQPLEQLG PTLERLSNMP
GFPMGPSPTT QTPPGVPPIS PIVTGPNTTP ESPRRSPKAR YEWKGCQNLG KCELSGYTKP
PLVILSLDGF AREYVDRNIV QTLNHIADCG VKADKVYPSY PSKTFPNHYS IVTGLWPESH
GITDNSVFDP TISPVLESMK STKYEKFFEG EPIWSVYKRK TGKKANCLFW VGCAYNNSGY
APDVAPAYNQ ELPFRNRIDT VVEWLKLPVD ERPGLITAYL HEPDNAGHYQ VDEEDVDEKL
AEIDENLDYL MSRLSEEKLL ECINFAILSD HGMQLIDKTY YFQDYLDLKG LITAKGVVGR
VYINDTTISV NDVVDKFRCK IDTVKTNTRS DVPTRKHYSR DPRVGEVLLE GRAGVTFYKS
KADDYELSGD HGYDYFNPKM HTIFYARGPS FKQNTTISPY QNIQYMNLWM NLLGIEGAVE
TNGTIGFFDN ILTNPPRRDN PTNVIGECPM IAFPSVLKCS GNVSAETLNQ LSVKLTNCAF
SPTNIPLYSD NHCFQNYCDN SVIVSRKGND ARRAIIEVLS RDEASNPSNF TFLNAKYQSN
CPSHIPTGSL TIRQNSQLSS MVDERIDVPN NFLLKVLDPL QAKSMEYLNK FGKMYVISGT
ATDINHDGIA DSNGSVITHI YRIMLICNST WLLMNPPLCT DSDSMDTLSF IFPITEQSTI
DCMSSDDILL DYTATIFDVE RISGFQFGIG ALSQNQNTII RRKISTKLW
