ENTP3_HUMAN
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 03-AUG-2022, entry version 174.
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 GlyGen; O75355; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O75355; -.
DR PhosphoSitePlus; O75355; -.
DR BioMuta; ENTPD3; -.
DR jPOST; O75355; -.
DR MassIVE; O75355; -.
DR PaxDb; O75355; -.
DR PeptideAtlas; O75355; -.
DR PRIDE; O75355; -.
DR ProteomicsDB; 33989; -.
DR ProteomicsDB; 49922; -. [O75355-1]
DR Antibodypedia; 29006; 272 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 CTD; 956; -.
DR DisGeNET; 956; -.
DR GeneCards; ENTPD3; -.
DR HGNC; HGNC:3365; ENTPD3.
DR HPA; ENSG00000168032; Tissue enhanced (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; ENSGT01050000244835; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; O75355; -.
DR OMA; IMGNFLE; -.
DR OrthoDB; 1337265at2759; -.
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 1060 CRISPR screens.
DR GeneWiki; ENTPD3; -.
DR GenomeRNAi; 956; -.
DR Pharos; O75355; Tbio.
DR PRO; PR:O75355; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75355; protein.
DR Bgee; ENSG00000168032; Expressed in islet of Langerhans and 155 other tissues.
DR ExpressionAtlas; O75355; baseline and differential.
DR Genevisible; O75355; HS.
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; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0045134; F:uridine-diphosphatase 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 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 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
