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Database: UniProt
Entry: G3QFA4_GORGO
LinkDB: G3QFA4_GORGO
Original site: G3QFA4_GORGO 
ID   G3QFA4_GORGO            Unreviewed;       752 AA.
AC   G3QFA4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-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:ENSGGOP00000000971.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000971.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000000971.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000000971.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000000971.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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}.
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DR   EMBL; CABD030047892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030047893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030047894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030047895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3QFA4; -.
DR   STRING; 9593.ENSGGOP00000000971; -.
DR   Ensembl; ENSGGOT00000000992.3; ENSGGOP00000000971.3; ENSGGOG00000000982.3.
DR   eggNOG; KOG2645; Eukaryota.
DR   GeneTree; ENSGT00940000159640; -.
DR   HOGENOM; CLU_635447_0_0_1; -.
DR   InParanoid; G3QFA4; -.
DR   OMA; PMYKEFK; -.
DR   TreeFam; TF330032; -.
DR   Proteomes; UP000001519; Chromosome 6.
DR   Bgee; ENSGGOG00000000982; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
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; IBA:GO_Central.
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; IBA:GO_Central.
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   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; 2.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
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; SM00477; NUC; 1.
DR   SMART; SM00201; SO; 2.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   SUPFAM; SSF90188; Somatomedin B domain; 2.
DR   PROSITE; PS00524; SMB_1; 2.
DR   PROSITE; PS50958; SMB_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
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   752 AA;  86026 MW;  565F6E1E5880ADC1 CRC64;
     MESMLTLATE QPVKKNTLKK YKIACIVLLA LLVIMSLGLG LGLGLRKPEK QGSCRKKCFD
     ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNK FRCGETRLEA SLCSCSDDCS
     QRKDCCADYK SVCQGETSWL EENCDTAQQS QCPEGFDLPP VILFSMDGFR AEYLYTWDTL
     MPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS
     SKEQNNPAWW HGQPMWLTAM YQGLKAATYF WPGSEVAING SFPSIYMPYN GSVPFEERIS
     TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG MLMEGLKQRN
     LHNCVNIILL ADHGMDQTYC NKMEYMTDYF PRINFFYMYE GPAPRIRAHN IPHDFFSFNS
     EEIVRNLSCR KPDQHFKPYL TPDLPKRLHY AKNVRIDKVH LFVDRQWLAV RSKSNTNCGG
     GNHGYNNEFR SMEAIFLAHG PSFKKKTEVE PFENIEVYNL MCDLLRIQPA PNNGTHGSLN
     HLLKVPFYEP SHAEEVSKFS VCGFANPLPT ESLDCLCPHL QNSTQLEQVN QMLNLTQEEI
     TATVKVNLPF GRPRVLQKNV DHCLLYHREY VSGFGKAMRM PMWSSYTVPQ LGDTSPLPPT
     VPDCLRADVR VPPSESQKCS VYLADKNITH GFLYPPEGKP EALWVEERFT AHIARVRDVE
     LLTGLDFYQD KVQPVSEILQ LKTYLPTFET TI
//
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