ENTP6_MOUSE
ID ENTP6_MOUSE Reviewed; 455 AA.
AC Q3U0P5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 6;
DE Short=NTPDase 6;
DE EC=3.6.1.6 {ECO:0000250|UniProtKB:O75354};
DE AltName: Full=CD39 antigen-like 2;
GN Name=Entpd6 {ECO:0000312|MGI:MGI:1202295}; Synonyms=Cd39l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. The membrane bound form might
CC support glycosylation reactions in the Golgi apparatus and, when
CC released from cells, might catalyze the hydrolysis of extracellular
CC nucleotides. {ECO:0000250|UniProtKB:Q9ER31}.
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:0000250|UniProtKB:O75354};
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:0000250|UniProtKB:O75354};
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:0000250|UniProtKB:O75354};
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:0000250|UniProtKB:O75354};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O75354};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:O75354};
CC Note=Strongly and equally activated by either Ca(2+) or Mg(2+).
CC {ECO:0000250|UniProtKB:O75354};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ER31}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q9ER31}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9ER31}; 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:0000250|UniProtKB:Q9ER31}.
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; AK156685; BAE33807.1; -; mRNA.
DR EMBL; AL845174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16861.1; -.
DR RefSeq; NP_742115.2; NM_172117.5.
DR RefSeq; XP_006498706.1; XM_006498643.2.
DR AlphaFoldDB; Q3U0P5; -.
DR SMR; Q3U0P5; -.
DR STRING; 10090.ENSMUSP00000092038; -.
DR PhosphoSitePlus; Q3U0P5; -.
DR EPD; Q3U0P5; -.
DR MaxQB; Q3U0P5; -.
DR PaxDb; Q3U0P5; -.
DR PeptideAtlas; Q3U0P5; -.
DR PRIDE; Q3U0P5; -.
DR ProteomicsDB; 332339; -.
DR Antibodypedia; 24986; 101 antibodies from 26 providers.
DR DNASU; 12497; -.
DR Ensembl; ENSMUST00000094467; ENSMUSP00000092038; ENSMUSG00000033068.
DR GeneID; 12497; -.
DR KEGG; mmu:12497; -.
DR UCSC; uc012cfv.1; mouse.
DR CTD; 955; -.
DR MGI; MGI:1202295; Entpd6.
DR VEuPathDB; HostDB:ENSMUSG00000033068; -.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_0_2_1; -.
DR InParanoid; Q3U0P5; -.
DR OMA; PFVCMDL; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q3U0P5; -.
DR TreeFam; TF315029; -.
DR Reactome; R-MMU-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR BioGRID-ORCS; 12497; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Entpd6; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3U0P5; protein.
DR Bgee; ENSMUSG00000033068; Expressed in spermatocyte and 252 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; ISO:MGI.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:1990003; F:inosine-diphosphatase activity; ISO:MGI.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:MGI.
DR GO; GO:0045134; F:uridine-diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0032026; P:response to magnesium ion; ISO:MGI.
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 ATP-binding; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..455
FT /note="Ectonucleoside triphosphate diphosphohydrolase 6"
FT /id="PRO_0000451958"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical"
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 DISULFID 297..327
FT /evidence="ECO:0000250|UniProtKB:O75354"
FT DISULFID 387..401
FT /evidence="ECO:0000250|UniProtKB:O75354"
SQ SEQUENCE 455 AA; 49799 MW; 6DD02E7E55E7B691 CRC64;
MRKIPNHGTL RMTKVAYPLG LCVGLFIYVA YIKWHRASAA QAFFTIAGAA SGARWTQQAF
SSPGSAARGH EVFYGIMFDA GSTGTRIHVF QFARPPGETP TLTHETFKAL KPGLSAYADD
VEKSAQGIQE LLNVAKQHIP YDFWKATPLV LKATAGLRLL PGEKAQKLLQ KVKEVFKASP
FLVGDDCVSI MNGTDEGVSA WITVNFLTGS LKTPGSSSVG MLDLGGGSTQ ITFLPRVEGT
LQASPPGHLT ALQMFNRTYK LYSYSYLGLG LMSARLAILG GVEGKPAEND KELVSPCLSP
RFRGEWEHAE VTYRISGQKA VGLYELCASR VSEVLRNKVH RTEEAQHVDF YAFSYYYDLA
ASFGLIDAEK GGSLVVGDFE IAAKYVCRTL ETQPPSSPFA CMDLTYISLL LHEFGFPGDK
VLKLARKIDN VETSWALGAI FHYIDSLKRQ KVPAL
