ID H2PKC1_PONAB Unreviewed; 872 AA.
AC H2PKC1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 {ECO:0000256|ARBA:ARBA00041154};
DE EC=3.1.4.1 {ECO:0000256|ARBA:ARBA00012029};
DE EC=3.6.1.9 {ECO:0000256|ARBA:ARBA00038862};
DE AltName: Full=Phosphodiesterase I beta {ECO:0000256|ARBA:ARBA00041699};
DE AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3 {ECO:0000256|ARBA:ARBA00041247};
GN Name=ENPP3 {ECO:0000313|Ensembl:ENSPPYP00000019047.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019047.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019047.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019047.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000256|ARBA:ARBA00000983};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00036800};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|ARBA:ARBA00011407}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; H2PKC1; -.
DR Ensembl; ENSPPYT00000019798.3; ENSPPYP00000019047.3; ENSPPYG00000017009.3.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000159640; -.
DR HOGENOM; CLU_012256_0_1_1; -.
DR InParanoid; H2PKC1; -.
DR OMA; PMYKEFK; -.
DR TreeFam; TF330032; -.
DR Proteomes; UP000001595; Chromosome 6.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IEA:Ensembl.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0002276; P:basophil activation involved in immune response; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IEA:Ensembl.
DR GO; GO:0070667; P:negative regulation of mast cell proliferation; IEA:Ensembl.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:Ensembl.
DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic 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; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF107; ECTONUCLEOTIDE PYROPHOSPHATASE_PHOSPHODIESTERASE FAMILY MEMBER 3; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
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 4: Predicted;
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:UP000001595};
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 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..93
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 94..138
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
SQ SEQUENCE 872 AA; 99747 MW; 160C2D1713E77275 CRC64;
MESMLTLAME QPVKKNTLKK YKIACIVLLA LLVIVSLGLG LGLGLRKPEK QGSCRKKCFD
ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRRWMCNK FRCGETRLEA SLCSCSDDCL
QRKDCCADYK SVCQGETSWL EENCDTAQQS QCPEGFDLPP VILFSMDGFR AEYLHTWDTL
MPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS
SKEQNNPAWW HGQPMWLTAM YQGLKAATYF WPGSEAAING SFPSIYMPYN GSVPFEERIS
TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG MLMEGLKQRN
LHNCVNIILL ADHGMEQTYC NKMEYMTDYF PRINFYMYEG PAPRIRAHNI PHDFFSFNSE
EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA KNVRIDKVHL FVDRQWLAVR SKSNTNCGGG
NHGYNNEFRS MEAIFLAHGP SFKEKTEVEP FENIEVYNLM CDLLRIQPAP NNGTHGSLNH
LLKVPFYEPS HAEEVSKFSV CGFANPLPTE SDCLCPHLQN SIQLEQVNQM LNLTQEEITA
TVKVNLPFGR PRVLQKNVDH CLLYHREYVS GFGKAMRMPM WSSYTVPQLG DTSPLPPTVP
DCLRADVRVP PSESQKCSFY LADKNITHGF LYPPASNRTS DSQYDALITS NLVPMYEEFT
KMWDYFHSVL LIKHATERNG VNVVSGPIFD YNYDGHFDAP DITKHLANTD VPIPTHYFVV
LTSCKNKSHT PENCPGWLDV LPFIIPHRPT NMESCPEGKP EALWVEERFT AHIARVRDVE
LLTGLDFYQE KVQPVSEILQ LKTYLPTFET TI
//
