ID G3UXY9_MOUSE Unreviewed; 910 AA.
AC G3UXY9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 2 {ECO:0000313|Ensembl:ENSMUSP00000133877.2};
GN Name=Enpp2 {ECO:0000313|Ensembl:ENSMUSP00000133877.2,
GN ECO:0000313|MGI:MGI:1321390};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000133877.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000133877.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133877.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000133877.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133877.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00010594}.
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DR RefSeq; NP_001272924.1; NM_001285995.2.
DR AlphaFoldDB; G3UXY9; -.
DR SMR; G3UXY9; -.
DR MaxQB; G3UXY9; -.
DR PeptideAtlas; G3UXY9; -.
DR ProteomicsDB; 351307; -.
DR Antibodypedia; 13653; 564 antibodies from 39 providers.
DR DNASU; 18606; -.
DR Ensembl; ENSMUST00000173516.8; ENSMUSP00000133877.2; ENSMUSG00000022425.17.
DR GeneID; 18606; -.
DR UCSC; uc007vrp.3; mouse.
DR AGR; MGI:1321390; -.
DR CTD; 5168; -.
DR MGI; MGI:1321390; Enpp2.
DR VEuPathDB; HostDB:ENSMUSG00000022425; -.
DR GeneTree; ENSGT00940000155778; -.
DR OrthoDB; 1366859at2759; -.
DR BioGRID-ORCS; 18606; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Enpp2; mouse.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000022425; Expressed in choroid plexus epithelium and 361 other cell types or tissues.
DR ExpressionAtlas; G3UXY9; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR CDD; cd16018; Enpp; 1.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 4.10.410.20; -; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF21; ECTONUCLEOTIDE PYROPHOSPHATASE_PHOSPHODIESTERASE FAMILY MEMBER 2; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF90188; Somatomedin B domain; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|MaxQB:G3UXY9,
KW ECO:0007829|PeptideAtlas:G3UXY9};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..97
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 98..142
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT REGION 317..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 104635 MW; 7F0252EC6890ED0C CRC64;
MARQGCFGSY QVISLFTFAI GVNLCLGFTA SRIKRAEWDE GPPTVLSDSP WTNTSGSCKG
RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW ECTKDRCGEV RNEENACHCS
EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE IRVPECPAGF VRPPLIIFSV DGFRASYMKK
GSKVMPNIEK LRSCGTHAPY MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAT
FHLRGREKFN HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
SVYAFYSEQP DFSGHKYGPF GPEESSYGSP LTPAKRPKRK VAPKRRQERP VAPPKKRRRK
LHRMDHYTAE TRQDKMTNPL REIDKTVGQL MDGLKQLKLH RCVNVIFVGD HGMEDVTCDR
TEFLSNYLTN VDDITLVPGT LGRIRPKIPN NLKYDPKAII ANLTCKKPDQ HFKPYMKQHL
PKRLHYANNR RIEDLHLLVE RRWHVARKPL DVYKKPSGKC FFQGDHGFDN KVNSMQTVFV
GYGPTFKYRT KVPPFENIEL YNVMCDLLGL KPAPNNGTHG SLNHLLRTNT FRPTLPEEVS
RPNYPGIMYL QSDFDLGCTC DDKNKLEELN KRLHTKGSTE ERHLLYGRPA VLYRTSYDIL
YHTDFESGYS EIFLMPLWTS YTISKQAEVS SIPEHLTNCV RPDVRVSPGF SQNCLAYKND
KQMSYGFLFP PYLSSSPEAK YDAFLVTNMV PMYPAFKRVW TYFQRVLVKK YASERNGVNV
ISGPIFDYNY NGLRDIEDEI KQYVEGSSIP VPTHYYSIIT SCLDFTQPAD KCDGPLSVSS
FILPHRPDND ESCNSSEDES KWVEELMKMH TARVRDIEHL TGLDFYRKTS RSYSEILTLK
TYLHTYESEI
//
