ENTP6_HUMAN
ID ENTP6_HUMAN Reviewed; 484 AA.
AC O75354; A6NCX6; D3DW49; Q5QPJ2; Q5QPJ5; Q7Z5B5; Q8N3H3; Q8TAS7; Q9UJD1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 6;
DE Short=NTPDase 6;
DE EC=3.6.1.6 {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856, ECO:0000269|PubMed:14529283};
DE AltName: Full=CD39 antigen-like 2;
GN Name=ENTPD6; Synonyms=CD39L2, IL6ST2;
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), AND VARIANTS VAL-138 AND GLU-202.
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), GLYCOSYLATION AT ASN-220 AND
RP ASN-284, DISULFIDE BONDS, MUTAGENESIS OF CYS-215, VARIANTS ASN-14 AND
RP GLU-202, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION,
RP SUBSTRATE SPECIFICITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=14529283; DOI=10.1021/bi035137r;
RA Ivanenkov V.V., Murphy-Piedmonte D.M., Kirley T.L.;
RT "Bacterial expression, characterization, and disulfide bond determination
RT of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure
RT and function.";
RL Biochemistry 42:11726-11735(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-202.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-202.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLU-202.
RC TISSUE=Placenta;
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 [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, COFACTOR,
RP CATALYTIC ACTIVITY, FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=11041856; DOI=10.1021/bi000959z;
RA Yeung G., Mulero J.J., McGowan D.W., Bajwa S.S., Ford J.E.;
RT "CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly
RT expressed in the heart.";
RL Biochemistry 39:12916-12923(2000).
RN [8]
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY,
RP COFACTOR, AND GLYCOSYLATION.
RX PubMed=10948193; DOI=10.1074/jbc.m004723200;
RA Hicks-Berger C.A., Chadwick B.P., Frischauf A.M., Kirley T.L.;
RT "Expression and characterization of soluble and membrane-bound human
RT nucleoside triphosphate diphosphohydrolase 6 (CD39L2).";
RL J. Biol. Chem. 275:34041-34045(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:10948193,
CC PubMed:14529283, PubMed:11041856). 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 (PubMed:10948193, PubMed:14529283, PubMed:11041856).
CC {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856,
CC ECO:0000269|PubMed:14529283}.
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:10948193, ECO:0000269|PubMed:11041856,
CC ECO:0000269|PubMed:14529283};
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:10948193, ECO:0000269|PubMed:14529283};
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:10948193, ECO:0000269|PubMed:14529283};
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:10948193, ECO:0000269|PubMed:14529283};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856,
CC ECO:0000269|PubMed:14529283};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856,
CC ECO:0000269|PubMed:14529283};
CC Note=Strongly and equally activated by either Ca(2+) or Mg(2+).
CC {ECO:0000269|PubMed:14529283};
CC -!- ACTIVITY REGULATION: Glycosylation does not appear to be required for
CC enzymatic activity. {ECO:0000269|PubMed:14529283}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for GDP (in the presence of Ca(2+))
CC {ECO:0000269|PubMed:14529283};
CC Vmax=60000 umol/h/mg enzyme with GDP as substrate
CC {ECO:0000269|PubMed:14529283};
CC pH dependence:
CC Optimum pH is 7.0 to 7.4. {ECO:0000269|PubMed:14529283};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10948193}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ER31}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000269|PubMed:10948193,
CC ECO:0000269|PubMed:11041856}. Cell membrane
CC {ECO:0000269|PubMed:10948193, ECO:0000269|PubMed:11041856}; Single-pass
CC type II membrane protein {ECO:0000255}. Note=Exists as a secreted and
CC membrane-bound forms in the medium of transfected cells, the secreted
CC form is predominant. {ECO:0000269|PubMed:10948193,
CC ECO:0000269|PubMed:11041856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75354-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75354-2; Sequence=VSP_039122;
CC Name=3;
CC IsoId=O75354-3; Sequence=VSP_054314;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, but predominantly in
CC heart. {ECO:0000269|PubMed:11041856}.
CC -!- PTM: The secreted form may be produced by intracellular processing.
CC {ECO:0000305|PubMed:11041856}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10948193,
CC ECO:0000269|PubMed:11041856}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF039916; AAC39883.1; -; mRNA.
DR EMBL; AY327581; AAP92131.1; -; mRNA.
DR EMBL; AL834158; CAD38864.2; -; mRNA.
DR EMBL; AL035252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10095.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10097.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10098.1; -; Genomic_DNA.
DR EMBL; BC025980; AAH25980.1; -; mRNA.
DR CCDS; CCDS13170.1; -. [O75354-1]
DR CCDS; CCDS46586.1; -. [O75354-2]
DR CCDS; CCDS82604.1; -. [O75354-3]
DR RefSeq; NP_001107561.1; NM_001114089.3. [O75354-2]
DR RefSeq; NP_001238.2; NM_001247.4. [O75354-1]
DR RefSeq; NP_001304870.1; NM_001317941.2. [O75354-3]
DR RefSeq; NP_001309307.1; NM_001322378.1. [O75354-1]
DR RefSeq; NP_001309308.1; NM_001322379.1.
DR RefSeq; NP_001309309.1; NM_001322380.1.
DR RefSeq; NP_001309310.1; NM_001322381.1.
DR RefSeq; NP_001309311.1; NM_001322382.1.
DR RefSeq; NP_001309312.1; NM_001322383.1.
DR RefSeq; NP_001309313.1; NM_001322384.1.
DR RefSeq; NP_001309314.1; NM_001322385.1.
DR RefSeq; NP_001309315.1; NM_001322386.1.
DR RefSeq; NP_001309316.1; NM_001322387.1.
DR RefSeq; NP_001309317.1; NM_001322388.1.
DR RefSeq; NP_001309318.1; NM_001322389.1.
DR RefSeq; NP_001309319.1; NM_001322390.1.
DR RefSeq; NP_001309320.1; NM_001322391.1.
DR RefSeq; NP_001309321.1; NM_001322392.1.
DR RefSeq; NP_001309322.1; NM_001322393.1.
DR RefSeq; NP_001309323.1; NM_001322394.1.
DR RefSeq; NP_001309324.1; NM_001322395.1.
DR RefSeq; NP_001309325.1; NM_001322396.1.
DR RefSeq; NP_001309326.1; NM_001322397.1.
DR RefSeq; NP_001309327.1; NM_001322398.1.
DR RefSeq; XP_006723728.1; XM_006723665.2. [O75354-3]
DR RefSeq; XP_011527698.1; XM_011529396.1. [O75354-1]
DR RefSeq; XP_011527699.1; XM_011529397.1. [O75354-3]
DR AlphaFoldDB; O75354; -.
DR SMR; O75354; -.
DR BioGRID; 107393; 70.
DR IntAct; O75354; 9.
DR MINT; O75354; -.
DR STRING; 9606.ENSP00000365840; -.
DR GlyGen; O75354; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O75354; -.
DR PhosphoSitePlus; O75354; -.
DR BioMuta; ENTPD6; -.
DR EPD; O75354; -.
DR jPOST; O75354; -.
DR MassIVE; O75354; -.
DR MaxQB; O75354; -.
DR PaxDb; O75354; -.
DR PeptideAtlas; O75354; -.
DR PRIDE; O75354; -.
DR ProteomicsDB; 49920; -. [O75354-1]
DR ProteomicsDB; 49921; -. [O75354-2]
DR ProteomicsDB; 63663; -.
DR Antibodypedia; 24986; 101 antibodies from 26 providers.
DR DNASU; 955; -.
DR Ensembl; ENST00000354989.9; ENSP00000347084.5; ENSG00000197586.13. [O75354-2]
DR Ensembl; ENST00000360031.6; ENSP00000353131.2; ENSG00000197586.13. [O75354-3]
DR Ensembl; ENST00000376652.9; ENSP00000365840.4; ENSG00000197586.13. [O75354-1]
DR GeneID; 955; -.
DR KEGG; hsa:955; -.
DR MANE-Select; ENST00000376652.9; ENSP00000365840.4; NM_001247.5; NP_001238.3.
DR UCSC; uc002wuj.3; human. [O75354-1]
DR CTD; 955; -.
DR DisGeNET; 955; -.
DR GeneCards; ENTPD6; -.
DR HGNC; HGNC:3368; ENTPD6.
DR HPA; ENSG00000197586; Low tissue specificity.
DR MIM; 603160; gene.
DR neXtProt; NX_O75354; -.
DR OpenTargets; ENSG00000197586; -.
DR PharmGKB; PA27803; -.
DR VEuPathDB; HostDB:ENSG00000197586; -.
DR eggNOG; KOG1385; Eukaryota.
DR GeneTree; ENSGT01050000244835; -.
DR InParanoid; O75354; -.
DR OMA; PFVCMDL; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; O75354; -.
DR TreeFam; TF315029; -.
DR BRENDA; 3.6.1.6; 2681.
DR PathwayCommons; O75354; -.
DR Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SignaLink; O75354; -.
DR BioGRID-ORCS; 955; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; ENTPD6; human.
DR GeneWiki; ENTPD6; -.
DR GenomeRNAi; 955; -.
DR Pharos; O75354; Tbio.
DR PRO; PR:O75354; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O75354; protein.
DR Bgee; ENSG00000197586; Expressed in apex of heart and 173 other tissues.
DR ExpressionAtlas; O75354; baseline and differential.
DR Genevisible; O75354; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
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:UniProtKB.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IEA:Ensembl.
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:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; 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; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Magnesium; Membrane; Reference proteome;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Ectonucleoside triphosphate diphosphohydrolase 6"
FT /id="PRO_0000209913"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..484
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14529283"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14529283"
FT DISULFID 325..356
FT /evidence="ECO:0000269|PubMed:14529283"
FT DISULFID 416..430
FT /evidence="ECO:0000269|PubMed:14529283"
FT VAR_SEQ 1..18
FT /note="MKKGIRYETSRKTSYIFQ -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039122"
FT VAR_SEQ 19
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054314"
FT VARIANT 14
FT /note="S -> N (in dbSNP:rs2076559)"
FT /evidence="ECO:0000269|PubMed:14529283"
FT /id="VAR_027812"
FT VARIANT 138
FT /note="L -> V (in dbSNP:rs1044567)"
FT /evidence="ECO:0000269|PubMed:9676430"
FT /id="VAR_017863"
FT VARIANT 157
FT /note="R -> Q (in dbSNP:rs34007133)"
FT /id="VAR_050309"
FT VARIANT 202
FT /note="K -> E (in dbSNP:rs6050446)"
FT /evidence="ECO:0000269|PubMed:14529283,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9676430, ECO:0000269|Ref.5"
FT /id="VAR_027813"
FT VARIANT 323
FT /note="S -> N (in dbSNP:rs6138541)"
FT /id="VAR_027814"
FT MUTAGEN 215
FT /note="C->S: Does not affect nucleoside-triphosphatase
FT activity. Does not affeet KM for GDP."
FT /evidence="ECO:0000269|PubMed:14529283"
SQ SEQUENCE 484 AA; 53246 MW; 3CBA96040BC196CB CRC64;
MKKGIRYETS RKTSYIFQQP QHGPWQTRMR KISNHGSLRV AKVAYPLGLC VGVFIYVAYI
KWHRATATQA FFSITRAAPG ARWGQQAHSP LGTAADGHEV FYGIMFDAGS TGTRVHVFQF
TRPPRETPTL THETFKALKP GLSAYADDVE KSAQGIRELL DVAKQDIPFD FWKATPLVLK
ATAGLRLLPG EKAQKLLQKV KKVFKASPFL VGDDCVSIMN GTDEGVSAWI TINFLTGSLK
TPGGSSVGML DLGGGSTQIA FLPRVEGTLQ ASPPGYLTAL RMFNRTYKLY SYSYLGLGLM
SARLAILGGV EGQPAKDGKE LVSPCLSPSF KGEWEHAEVT YRVSGQKAAA SLHELCAARV
SEVLQNRVHR TEEVKHVDFY AFSYYYDLAA GVGLIDAEKG GSLVVGDFEI AAKYVCRTLE
TQPQSSPFSC MDLTYVSLLL QEFGFPRSKV LKLTRKIDNV ETSWALGAIF HYIDSLNRQK
SPAS
