(data stored in ACNUC30567 zone)

HOGENOM: AILMEGL192398_1_1_PE15

ID   AILMEGL192398_1_1_PE15               STANDARD;      PRT;   457 AA.
AC   AILMEGL192398_1_1_PE15; D2GZV9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 5;
DE   Short=NTPDase 5; EC=3.6.1.6;AltName: Full=Guanosine-diphosphatase ENTPD5;
DE   Short=GDPase ENTPD5; EC=3.6.1 42;AltName: Full=Uridine-diphosphatase
DE   ENTPD5; Short=UDPase ENTPD5;Flags: Precursor; (AILMEGL192398_1_1.PE15).
GN   Name=ENTPD5; ORFNames=PANDA_002660;
OS   AILUROPODA MELANOLEUCA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from
CC       the HOGENOM CDS AILMEGL192398_1_1.PE15.
CC       Ailuropoda melanoleuca scaffold GL192398.1 ailMel1 partial sequence
CC       1..863378 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:ENTP5_AILME
CC   -!- FUNCTION: Uridine diphosphatase (UDPase) that promotes protein N-
CC       glycosylation and ATP level regulation. UDP hydrolysis promotes
CC       protein N-glycosylation and folding in the endoplasmic reticulum,
CC       as well as elevated ATP consumption in the cytosol via an ATP
CC       hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP
CC       hydrolysis cycle that converts ATP to AMP and results in a
CC       compensatory increase in aerobic glycolysis. Also hydrolyzes GDP
CC       and IDP but not any other nucleoside di-, mono- or triphosphates,
CC       nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN
CC       signaling pathway by promoting glycolysis in proliferating cells
CC       in response to phosphoinositide 3-kinase (PI3K) signaling (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: GDP + H(2)O = GMP + phosphate.
CC   -!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a
CC       nucleotide + phosphate.
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC   -!- PTM: N-glycosylated; high-mannose type (By similarity).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC   -!- GENE_FAMILY: HOG000220904 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Ailuropoda_melanoleuca;ENSAMEG00000018251;ENSAMET00000020057;ENSAMEP00000019291.
DR   EMBL; GL192398; - ;
DR   UniProtKB/Swiss-Prot; D2GZV9; -.
DR   EMBL; GL192398; EFB27007.1; -; Genomic_DNA.
DR   Ensembl; ENSAMET00000020057; ENSAMEP00000019291; ENSAMEG00000018251.
DR   GeneTree; ENSGT00510000046675; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0004382; F:guanosine-diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0045134; F:uridine-diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0051084; P:'de novo' posttranslational protein folding; ISS:UniProtKB.
DR   GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR   GO; GO:0016049; P:cell growth; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; ISS:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR   GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase cascade; ISS:UniProtKB.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; GDA1_CD39_NTPase; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
DR   HOGENOMDNA; AILMEGL192398_1_1.PE15; -.
KW   ENSAMEG00000018251; ENSAMEP00000019291; D2GZV9_AILME; GL192398;
KW   Calcium; Endoplasmic reticulum; Glycoprotein; Hydrolase; Magnesium;
KW   Signal.
SQ   SEQUENCE   457 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     VFLPLQVYEQ HCCCIKSLDS PHLGKRMATT WGAAFFMLVA SCVCSTVFHR DQQTWFEGVF
     LSSMCPINVS ASTLYGIMFD AGSTGTRIHI YTFVQKIPDK IGQLPILEGE IFESVKPGLS
     AFVDQPKQGA ETVEELLEVA KDSVPRSHWK RTPVVLKATA GLRLLPEQKA EALLFEVREI
     FRKSPFLVPD DSVSIMDGSY EGILAWVTVN FLTGQLHGHS QKTVGTLDLG GASTQITFLP
     QFEKTLEQTP RGYLTSFEMF NSTYKLYTHS YLGFGLKAAR LATLGALETE GIDGHTFRSA
     CLPRWLEAEW IFGGVKYQYG GNKEGEVGFE PCYAEVLRVV QGKLHQPDEV RKSSFYAFSY
     YYDRAADTDM IDYETGGVLK VEDFERKARE VCDNLEKFTS GSPFLCMDLS YITALLKDGF
     GFADSTILQL SKKVNNIETG WALGATFHLL QSLGISH
//

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