ID H2QWM6_PANTR Unreviewed; 915 AA.
AC H2QWM6; A0A2J8PND5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase 2 {ECO:0000313|EMBL:JAA42340.1, ECO:0000313|Ensembl:ENSPTRP00000035117.2};
GN Name=ENPP2 {ECO:0000313|EMBL:JAA42340.1,
GN ECO:0000313|Ensembl:ENSPTRP00000035117.2, ECO:0000313|VGNC:VGNC:1170};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000035117.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000035117.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA42340.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA42340.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000035117.2}
RP IDENTIFICATION.
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 EMBL; AACZ04067552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABE01002399; JAA42340.1; -; mRNA.
DR RefSeq; XP_519922.2; XM_519922.5.
DR STRING; 9598.ENSPTRP00000035117; -.
DR PaxDb; 9598-ENSPTRP00000035117; -.
DR Ensembl; ENSPTRT00000037991.3; ENSPTRP00000035117.2; ENSPTRG00000020534.5.
DR GeneID; 464353; -.
DR CTD; 5168; -.
DR VGNC; VGNC:1170; ENPP2.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000155778; -.
DR HOGENOM; CLU_012256_0_0_1; -.
DR OrthoDB; 1366859at2759; -.
DR TreeFam; TF330032; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000020534; Expressed in Brodmann (1909) area 10 and 21 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IBA:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IBA:GO_Central.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0030149; P:sphingolipid catabolic process; IEA:Ensembl.
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; 1.
DR PROSITE; PS50958; SMB_2; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 55..98
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 99..143
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..364
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 105188 MW; 0FEB6C54DF5F1E50 CRC64;
MARRSSFQSC QIISLFTFAV GINICLGFTA HRIKRAEGWE EGPPTVLSDS PWTNISGSCK
GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG WECTKDRCGE VRNEENACHC
SEDCLARGDC CTNYQVVCKG ESHWVDDDCE EIKAAECPAG FVRPPLIIFS VDGFRASYMK
KGSKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
TFHLRGREKF NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDNER
PSVYAFYSEQ PDFSGHKYGP FGPEESSYGS PFTPAKRPKR KVAPKRRQER PVAPPKKRRR
KIHRMDHYAA ETRQDKMTNP LREIDKIVGQ LMDGLKQLKL HRCVNVIFVG DHGMEDVTCD
RTEFLSNYLT NVDDITLVPG TLGRIRSKFS NNAKYDPKAI IANLTCKKPD QHFKPYLKQH
LPKRLHYANN RRIEDIHLLV ERRWHVARKP LDVYKKPSGK CFFQGDHGFD NKVNSMQTVF
VGYGPTFKYK TKVPPFENIE LYNVMCDLLG LKPAPNNGTH GSLNHLLRTN TFRPTMPEEV
TRPSYPGIMY LQSDFDLGCT CDDKVEPKNK LDELNKRLHT KGSTEERHLL YGRPAVLYRT
RYDILYHTDF ESGYSQIFLM PLWTSYTVSK QAEVSSIPDH LTSCVRPDVR VSPSFSQNCL
AYKNDKQMSY GFLFPPYLSS SPEAKYDAFL VTNMVPMYPA FKRVWNYFQR VLVKKYASER
NGVNVISGPI FDYDYDGLHD TEDKIKQYVE GSSIPVPTHY YSIITSCLDF TQPADKCDGP
LSVSSFILPH RPDNEESCNS SEDESKWVEE LMKMHTARVR DIEHLTSLDF FRKTSRSYPE
ILTLKTYLHT YESEI
//