ID   ENTP3_HUMAN             Reviewed;         529 AA.
AC   O75355; B2R8D0; G5E9N0; O60495; Q8N6K2;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 3;
DE            Short=NTPDase 3;
DE            EC=3.6.1.5;
DE   AltName: Full=CD39 antigen-like 3 {ECO:0000303|PubMed:9676430};
DE   AltName: Full=Ecto-ATP diphosphohydrolase 3;
DE            Short=Ecto-ATPDase 3;
DE            Short=Ecto-ATPase 3;
DE   AltName: Full=Ecto-apyrase 3;
DE   AltName: Full=HB6 {ECO:0000303|PubMed:9675246};
GN   Name=ENTPD3; Synonyms=CD39L3 {ECO:0000303|PubMed:9676430};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP   VAL-496.
RC   TISSUE=Keratinocyte;
RX   PubMed=9676430; DOI=10.1006/geno.1998.5317;
RA   Chadwick B.P., Frischauf A.-M.;
RT   "The CD39-like gene family: identification of three new human members
RT   (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the
RT   gene family from Drosophila melanogaster.";
RL   Genomics 50:357-367(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC   TISSUE=Brain;
RX   PubMed=9675246; DOI=10.1016/s0167-4838(98)00063-6;
RA   Smith T.M., Kirley T.L.;
RT   "Cloning, sequencing, and expression of a human brain ecto-apyrase related
RT   to both the ecto-ATPases and CD39 ecto-apyrases.";
RL   Biochim. Biophys. Acta 1386:65-78(1998).
RN   [3]
RP   SEQUENCE REVISION.
RA   Smith T.M., Kirley T.L.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Esophagus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-24.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-187; ASP-219 AND
RP   TRP-459.
RX   PubMed=10231536; DOI=10.1021/bi990171k;
RA   Smith T.M., Lewis Carl S.A., Kirley T.L.;
RT   "Mutagenesis of two conserved tryptophan residues of the E-type ATPases:
RT   inactivation and conversion of an ecto-apyrase to an ecto-NTPase.";
RL   Biochemistry 38:5849-5857(1999).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ARG-67; ARG-143;
RP   ARG-146; GLU-182; ASN-191; SER-224 AND GLN-226.
RX   PubMed=11300774; DOI=10.1021/bi002711f;
RA   Yang F., Hicks-Berger C.A., Smith T.M., Kirley T.L.;
RT   "Site-directed mutagenesis of human nucleoside triphosphate
RT   diphosphohydrolase 3: the importance of residues in the apyrase conserved
RT   regions.";
RL   Biochemistry 40:3943-3950(2001).
RN   [10]
RP   DISULFIDE BONDS.
RX   PubMed=15966724; DOI=10.1021/bi047487z;
RA   Ivanenkov V.V., Meller J., Kirley T.L.;
RT   "Characterization of disulfide bonds in human nucleoside triphosphate
RT   diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural
RT   modeling.";
RL   Biochemistry 44:8998-9012(2005).
CC   -!- FUNCTION: Has a threefold preference for the hydrolysis of ATP over
CC       ADP. {ECO:0000269|PubMed:10231536, ECO:0000269|PubMed:11300774}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC         Evidence={ECO:0000269|PubMed:10231536, ECO:0000269|PubMed:11300774};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:11300774};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11300774};
CC   -!- INTERACTION:
CC       O75355; Q8N205: SYNE4; NbExp=3; IntAct=EBI-10187968, EBI-7131783;
CC       O75355-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12279764, EBI-11343438;
CC       O75355-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12279764, EBI-6942903;
CC       O75355-2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12279764, EBI-781551;
CC       O75355-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12279764, EBI-18304435;
CC       O75355-2; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12279764, EBI-12142257;
CC       O75355-2; Q6P531: GGT6; NbExp=3; IntAct=EBI-12279764, EBI-2868927;
CC       O75355-2; Q99795: GPA33; NbExp=3; IntAct=EBI-12279764, EBI-4289554;
CC       O75355-2; P38484: IFNGR2; NbExp=3; IntAct=EBI-12279764, EBI-3905457;
CC       O75355-2; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12279764, EBI-17490413;
CC       O75355-2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12279764, EBI-2820517;
CC       O75355-2; P15941-11: MUC1; NbExp=3; IntAct=EBI-12279764, EBI-17263240;
CC       O75355-2; P54829: PTPN5; NbExp=3; IntAct=EBI-12279764, EBI-1220572;
CC       O75355-2; P32856-2: STX2; NbExp=3; IntAct=EBI-12279764, EBI-11956649;
CC       O75355-2; Q96A25: TMEM106A; NbExp=3; IntAct=EBI-12279764, EBI-3915978;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFW6};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O75355-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75355-2; Sequence=VSP_054237;
CC   -!- TISSUE SPECIFICITY: Expressed in adult brain, pancreas, spleen and
CC       prostate (PubMed:9676430). Moderate or low expression is seen in most
CC       tissues (PubMed:9676430). Not expressed in liver and peripheral blood
CC       leukocytes (PubMed:9676430). {ECO:0000269|PubMed:9676430}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; AF039917; AAC39884.1; -; mRNA.
DR   EMBL; AF034840; AAC09236.2; -; mRNA.
DR   EMBL; AK313322; BAG36127.1; -; mRNA.
DR   EMBL; AC104186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64600.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW64601.1; -; Genomic_DNA.
DR   EMBL; BC029869; AAH29869.1; -; mRNA.
DR   CCDS; CCDS2691.1; -. [O75355-1]
DR   CCDS; CCDS74919.1; -. [O75355-2]
DR   RefSeq; NP_001239.2; NM_001248.3. [O75355-1]
DR   RefSeq; NP_001278889.1; NM_001291960.1. [O75355-1]
DR   RefSeq; NP_001278890.1; NM_001291961.1. [O75355-2]
DR   AlphaFoldDB; O75355; -.
DR   SMR; O75355; -.
DR   BioGRID; 107394; 16.
DR   IntAct; O75355; 15.
DR   STRING; 9606.ENSP00000301825; -.
DR   BindingDB; O75355; -.
DR   ChEMBL; CHEMBL5897; -.
DR   GlyConnect; 2936; 1 N-Linked glycan (1 site).
DR   GlyCosmos; O75355; 7 sites, 2 glycans.
DR   GlyGen; O75355; 7 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; O75355; -.
DR   PhosphoSitePlus; O75355; -.
DR   SwissPalm; O75355; -.
DR   BioMuta; ENTPD3; -.
DR   jPOST; O75355; -.
DR   MassIVE; O75355; -.
DR   PaxDb; 9606-ENSP00000301825; -.
DR   PeptideAtlas; O75355; -.
DR   ProteomicsDB; 33989; -.
DR   ProteomicsDB; 49922; -. [O75355-1]
DR   Antibodypedia; 29006; 287 antibodies from 32 providers.
DR   DNASU; 956; -.
DR   Ensembl; ENST00000301825.8; ENSP00000301825.3; ENSG00000168032.10. [O75355-1]
DR   Ensembl; ENST00000445129.1; ENSP00000404671.1; ENSG00000168032.10. [O75355-2]
DR   Ensembl; ENST00000456402.5; ENSP00000401565.1; ENSG00000168032.10. [O75355-1]
DR   GeneID; 956; -.
DR   KEGG; hsa:956; -.
DR   MANE-Select; ENST00000301825.8; ENSP00000301825.3; NM_001248.4; NP_001239.2.
DR   UCSC; uc003ckd.5; human. [O75355-1]
DR   AGR; HGNC:3365; -.
DR   CTD; 956; -.
DR   DisGeNET; 956; -.
DR   GeneCards; ENTPD3; -.
DR   HGNC; HGNC:3365; ENTPD3.
DR   HPA; ENSG00000168032; Tissue enhanced (brain, cervix, salivary gland).
DR   MIM; 603161; gene.
DR   neXtProt; NX_O75355; -.
DR   OpenTargets; ENSG00000168032; -.
DR   PharmGKB; PA27800; -.
DR   VEuPathDB; HostDB:ENSG00000168032; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   GeneTree; ENSGT01100000263542; -.
DR   HOGENOM; CLU_010246_2_3_1; -.
DR   InParanoid; O75355; -.
DR   OMA; GNAISDM; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; O75355; -.
DR   TreeFam; TF332859; -.
DR   BRENDA; 3.6.1.5; 2681.
DR   PathwayCommons; O75355; -.
DR   Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR   SABIO-RK; O75355; -.
DR   SignaLink; O75355; -.
DR   BioGRID-ORCS; 956; 7 hits in 1138 CRISPR screens.
DR   GeneWiki; ENTPD3; -.
DR   GenomeRNAi; 956; -.
DR   Pharos; O75355; Tchem.
DR   PRO; PR:O75355; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O75355; Protein.
DR   Bgee; ENSG00000168032; Expressed in islet of Langerhans and 156 other cell types or tissues.
DR   ExpressionAtlas; O75355; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:Ensembl.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF38; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 3; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
DR   Genevisible; O75355; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calcium; Cell membrane; Disulfide bond;
KW   Glycoprotein; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..529
FT                   /note="Ectonucleoside triphosphate diphosphohydrolase 3"
FT                   /id="PRO_0000209910"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..485
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O35795"
FT   BINDING         222..226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O35795"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..116
FT                   /evidence="ECO:0000269|PubMed:15966724"
FT   DISULFID        261..308
FT                   /evidence="ECO:0000269|PubMed:15966724"
FT   DISULFID        289..334
FT                   /evidence="ECO:0000269|PubMed:15966724"
FT   DISULFID        347..353
FT                   /evidence="ECO:0000269|PubMed:15966724"
FT   DISULFID        399..422
FT                   /evidence="ECO:0000269|PubMed:15966724"
FT   VAR_SEQ         452..529
FT                   /note="VGNSSIAWSLGYMLSLTNQIPAESPLIRLPIEPPVFVGTLAFFTAAALLCLA
FT                   FLAYLCSATRRKRHSEHAFDHAVDSD -> E (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054237"
FT   VARIANT         24
FT                   /note="I -> V (in dbSNP:rs17852714)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_070813"
FT   VARIANT         264
FT                   /note="R -> Q (in dbSNP:rs34266806)"
FT                   /id="VAR_061384"
FT   VARIANT         440
FT                   /note="E -> D (in dbSNP:rs4470483)"
FT                   /id="VAR_027541"
FT   VARIANT         496
FT                   /note="A -> V (in dbSNP:rs1047855)"
FT                   /evidence="ECO:0000269|PubMed:9676430"
FT                   /id="VAR_027542"
FT   VARIANT         505
FT                   /note="L -> F (in dbSNP:rs3733167)"
FT                   /id="VAR_027543"
FT   MUTAGEN         67
FT                   /note="R->G: Increase of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         143
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         143
FT                   /note="R->K: Increase of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         146
FT                   /note="R->N: No effect."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         146
FT                   /note="R->P: Increase of ATPase activity, decrease of
FT                   ADPase activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         146
FT                   /note="R->T: Increase of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         182
FT                   /note="E->D: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         182
FT                   /note="E->Q: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         187
FT                   /note="W->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:10231536"
FT   MUTAGEN         191
FT                   /note="N->A: Loss of ATPase activity, increase of ADPase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         219
FT                   /note="D->E: Increase of activity."
FT                   /evidence="ECO:0000269|PubMed:10231536"
FT   MUTAGEN         224
FT                   /note="S->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         226
FT                   /note="Q->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11300774"
FT   MUTAGEN         459
FT                   /note="W->A: Increase of activity, especially the ATP
FT                   hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:10231536"
SQ   SEQUENCE   529 AA;  59105 MW;  5043CF0202978B88 CRC64;
     MFTVLTRQPC EQAGLKALYR TPTIIALVVL LVSIVVLVSI TVIQIHKQEV LPPGLKYGIV
     LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV
     KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ
     EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS
     DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM
     GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ
     PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS
     YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL
     PIEPPVFVGT LAFFTAAALL CLAFLAYLCS ATRRKRHSEH AFDHAVDSD
//