ENTP6_RAT
ID ENTP6_RAT Reviewed; 455 AA.
AC Q9ER31;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 6;
DE Short=NTPDase 6;
DE EC=3.6.1.6 {ECO:0000269|PubMed:11042118};
DE AltName: Full=CD39 antigen-like 2;
GN Name=Entpd6; Synonyms=Cd39l2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11042118; DOI=10.1042/bj3510639;
RA Braun N., Fengler S., Ebeling C., Servos J., Zimmermann H.;
RT "Sequencing, functional expression and characterization of rat NTPDase6, a
RT nucleoside diphosphatase and novel member of the ecto-nucleoside
RT triphosphate diphosphohydrolase family.";
RL Biochem. J. 351:639-647(2000).
CC -!- FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates and
CC diphosphates in a calcium- or magnesium-dependent manner. Has a strong
CC preference for nucleoside diphosphates, preferentially hydrolyzes GDP,
CC IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and
CC UTP and virtually no hydrolysis of ATP (PubMed:11042118). The membrane
CC bound form might support glycosylation reactions in the Golgi apparatus
CC and, when released from cells, might catalyze the hydrolysis of
CC extracellular nucleotides (PubMed:11042118).
CC {ECO:0000269|PubMed:11042118}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:11042118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:11042118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:11042118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:11042118};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11042118};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11042118};
CC Note=Strongly and equally activated by either Ca(2+) or Mg(2+).
CC {ECO:0000269|PubMed:11042118};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=211 uM for GDP {ECO:0000269|PubMed:11042118};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11042118}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000269|PubMed:11042118}. Cell membrane
CC {ECO:0000269|PubMed:11042118}; Single-pass type II membrane protein
CC {ECO:0000255}. Note=Exists as a secreted and membrane-bound forms in
CC the medium of transfected cells, the secreted form is predominant.
CC {ECO:0000269|PubMed:11042118}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and brain.
CC {ECO:0000269|PubMed:11042118}.
CC -!- PTM: Might be cleaved at the N-terminus, retained in an intracellular
CC membrane compartment and in addition be released into the extracellular
CC medium. {ECO:0000269|PubMed:11042118}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O75354}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AJ277748; CAC16598.1; -; mRNA.
DR RefSeq; NP_445950.1; NM_053498.1.
DR RefSeq; XP_006235280.1; XM_006235218.3.
DR AlphaFoldDB; Q9ER31; -.
DR SMR; Q9ER31; -.
DR STRING; 10116.ENSRNOP00000009946; -.
DR GlyGen; Q9ER31; 2 sites.
DR PaxDb; Q9ER31; -.
DR PRIDE; Q9ER31; -.
DR Ensembl; ENSRNOT00000009946; ENSRNOP00000009946; ENSRNOG00000007427.
DR GeneID; 85260; -.
DR KEGG; rno:85260; -.
DR UCSC; RGD:619725; rat.
DR CTD; 955; -.
DR RGD; 619725; Entpd6.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; Q9ER31; -.
DR OMA; PFVCMDL; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9ER31; -.
DR TreeFam; TF315029; -.
DR Reactome; R-RNO-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR PRO; PR:Q9ER31; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007427; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q9ER31; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IDA:RGD.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:RGD.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:RGD.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IDA:RGD.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Hydrolase; Magnesium; Membrane; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..455
FT /note="Ectonucleoside triphosphate diphosphohydrolase 6"
FT /id="PRO_0000209914"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..455
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 297..327
FT /evidence="ECO:0000250|UniProtKB:O75354"
FT DISULFID 387..401
FT /evidence="ECO:0000250|UniProtKB:O75354"
SQ SEQUENCE 455 AA; 49899 MW; 19A22E8BAEF0F77B CRC64;
MRKIPNHGTL RMTKVAYPLG LCVGLFIYVA YIKWHRASAA QAFFTIAGAA SGVRWTQQAF
SSPDSATRGH EVFYGIMFDA GSTGTRIHVF QFARPPGETP TLTHETFKAL KPGLSAYADD
VEKSAQGIQE LLNVAKQHIP YDFWKATPLV LKATAGLRLL PGEKAQKLLQ KVKEVFKASP
FLVGDDCVSI MNGTDEGVSA WITVNFLTGS LKTPGSSSVG MLDLGGGSTQ ITFLPRVEGT
LQASPPGHLT ALQMFNRTFK LYSYSYLGLG LMSARLAILG GVEGKPAEDD KELVSPCLSP
RFRGKWEHAE VTYRISGQKA VGLYELCASR VSEVLRNKVH RTEEAQHVDF YAFSYYYDLA
ASFGLIDAEK GGSLVVGDFE IAAKYVCRTL ETQPPSSPFA CMDLTYISLL LHEFGFPGDK
VLKLARKIDN VETSWALGAI FHYIDSLKRQ KVPAL
