MCE1_HUMAN
ID MCE1_HUMAN Reviewed; 597 AA.
AC O60942; E1P513; E1P514; O43483; O60257; O60351; Q5TCW8; Q8WUM8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=mRNA-capping enzyme;
DE AltName: Full=HCAP1;
DE AltName: Full=HCE;
DE Includes:
DE RecName: Full=mRNA 5'-triphosphate monophosphatase;
DE EC=3.6.1.74 {ECO:0000269|PubMed:9473487};
DE AltName: Full=mRNA 5'-phosphatase;
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50 {ECO:0000269|PubMed:9473487};
DE AltName: Full=GTP--RNA guanylyltransferase;
DE Short=GTase;
GN Name=RNGTT; Synonyms=CAP1A;
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).
RX PubMed=9371772; DOI=10.1073/pnas.94.24.12898;
RA Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J.;
RT "Mammalian capping enzyme complements mutant Saccharomyces cerevisiae
RT lacking mRNA guanylyltransferase and selectively binds the elongating form
RT of RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12898-12903(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), MUTAGENESIS OF LYS-294;
RP ARG-299; GLU-345; LYS-458 AND LYS-460, AND FUNCTION.
RX PubMed=9512541; DOI=10.1093/nar/26.7.1700;
RA Yamada-Okabe T., Doi R., Shimmi O., Arisawa M., Yamada-Okabe H.;
RT "Isolation and characterization of a human cDNA for mRNA 5'-capping
RT enzyme.";
RL Nucleic Acids Res. 26:1700-1706(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9473487; DOI=10.1006/bbrc.1997.8038;
RA Tsukamoto T., Shibagaki Y., Murakoshi T., Suzuki M., Nakamura A., Gotoh H.,
RA Mizumoto K.;
RT "Cloning and characterization of two human cDNAs encoding the mRNA capping
RT enzyme.";
RL Biochem. Biophys. Res. Commun. 243:101-108(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-594.
RC TISSUE=Skin;
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 INTERACTION WITH RNMT.
RX PubMed=9705270; DOI=10.1074/jbc.273.34.21443;
RA Pillutla R.C., Yue Z., Maldonado E., Shatkin A.J.;
RT "Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA
RT polymerase IIo complexes.";
RL J. Biol. Chem. 273:21443-21446(1998).
RN [8]
RP INTERACTION WITH SUPT5H.
RX PubMed=10421630; DOI=10.1101/gad.13.14.1774;
RA Wen Y., Shatkin A.J.;
RT "Transcription elongation factor hSPT5 stimulates mRNA capping.";
RL Genes Dev. 13:1774-1779(1999).
RN [9]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=11278368; DOI=10.1074/jbc.m007901200;
RA Chiu Y.-L., Coronel E., Ho C.K., Shuman S., Rana T.M.;
RT "HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates
RT capping of TAR RNA.";
RL J. Biol. Chem. 276:12959-12966(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 229-567, CATALYTIC ACTIVITY,
RP FUNCTION, MUTAGENESIS OF GLU-234; LYS-458; LYS-460; ARG-528; ARG-530;
RP ASP-532 AND LYS-533, AND ACTIVE SITE.
RX PubMed=21636784; DOI=10.1073/pnas.1106610108;
RA Chu C., Das K., Tyminski J.R., Bauman J.D., Guan R., Qiu W.,
RA Montelione G.T., Arnold E., Shatkin A.J.;
RT "Structure of the guanylyltransferase domain of human mRNA capping
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10104-10108(2011).
CC -!- FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-
CC triphosphate monophosphatase activity in the N-terminal part and mRNA
CC guanylyltransferase activity in the C-terminal part. Catalyzes the
CC first two steps of cap formation: by removing the gamma-phosphate from
CC the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and
CC by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of
CC RNA via a covalent enzyme-GMP reaction intermediate.
CC {ECO:0000269|PubMed:21636784, ECO:0000269|PubMed:9473487,
CC ECO:0000269|PubMed:9512541}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC diphospho-ribonucleoside in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC Evidence={ECO:0000269|PubMed:9473487};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC Evidence={ECO:0000305|PubMed:9473487};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000269|PubMed:9473487};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000305|PubMed:9473487};
CC -!- SUBUNIT: Interacts with POLR2A (via C-terminus); this enhances
CC guanylyltransferase activity. Binds (via GTase domain) to the
CC elongating phosphorylated form of RNA polymerase II; can form direct
CC interactions with the phosphorylated POLR2A C-terminal domain and
CC indirect interactions via bound RNA (By similarity). Interacts with
CC SUPT5H and RNMT. Interacts with HIV-1 Tat. {ECO:0000250,
CC ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:9705270}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:11278368}.
CC -!- INTERACTION:
CC O60942; Q92624: APPBP2; NbExp=3; IntAct=EBI-1237132, EBI-743771;
CC O60942; P16333-1: NCK1; NbExp=2; IntAct=EBI-1237132, EBI-15578122;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=HCE1, HCAP1A;
CC IsoId=O60942-1; Sequence=Displayed;
CC Name=2; Synonyms=HCE1A;
CC IsoId=O60942-2; Sequence=VSP_003202;
CC Name=3; Synonyms=HCE1B;
CC IsoId=O60942-3; Sequence=VSP_003202, VSP_003203;
CC Name=4; Synonyms=HCAP1B;
CC IsoId=O60942-4; Sequence=VSP_003204;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 4 (at a lesser extent) are
CC expressed in cerebrum, cerebellum, thyroid, lung, heart, liver, kidney,
CC spleen, large intestine, testis, skin and muscle.
CC -!- MISCELLANEOUS: Isoform 2 to isoform 4 lack mRNA 5'-guanylyltransferase
CC activity due to disruptions of the GTase domain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the non-receptor
CC class of the protein-tyrosine phosphatase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase
CC family. {ECO:0000305}.
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DR EMBL; AF025654; AAB91559.1; -; mRNA.
DR EMBL; AB009022; BAA25894.1; -; mRNA.
DR EMBL; AB009023; BAA25895.1; -; mRNA.
DR EMBL; AB009024; BAA25896.1; -; mRNA.
DR EMBL; AB012142; BAA25198.1; -; mRNA.
DR EMBL; AB012143; BAA25199.1; -; mRNA.
DR EMBL; AL079342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48566.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48567.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48569.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48570.1; -; Genomic_DNA.
DR EMBL; BC019954; AAH19954.1; -; mRNA.
DR CCDS; CCDS5017.1; -. [O60942-1]
DR CCDS; CCDS69153.1; -. [O60942-2]
DR PIR; JC5936; JC5936.
DR PIR; JC5937; JC5937.
DR RefSeq; NP_001273355.1; NM_001286426.1. [O60942-2]
DR RefSeq; NP_001273357.1; NM_001286428.1.
DR RefSeq; NP_003791.3; NM_003800.4. [O60942-1]
DR PDB; 2C46; X-ray; 1.60 A; A/B/C/D=1-219.
DR PDB; 3S24; X-ray; 3.01 A; A/B/C/D/E/F/G=229-567.
DR PDBsum; 2C46; -.
DR PDBsum; 3S24; -.
DR AlphaFoldDB; O60942; -.
DR SMR; O60942; -.
DR BioGRID; 114270; 112.
DR DIP; DIP-61014N; -.
DR IntAct; O60942; 27.
DR MINT; O60942; -.
DR STRING; 9606.ENSP00000358497; -.
DR DEPOD; RNGTT; -.
DR GlyGen; O60942; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60942; -.
DR MetOSite; O60942; -.
DR PhosphoSitePlus; O60942; -.
DR BioMuta; RNGTT; -.
DR EPD; O60942; -.
DR jPOST; O60942; -.
DR MassIVE; O60942; -.
DR MaxQB; O60942; -.
DR PaxDb; O60942; -.
DR PeptideAtlas; O60942; -.
DR PRIDE; O60942; -.
DR ProteomicsDB; 49688; -. [O60942-1]
DR ProteomicsDB; 49689; -. [O60942-2]
DR ProteomicsDB; 49690; -. [O60942-3]
DR ProteomicsDB; 49691; -. [O60942-4]
DR Antibodypedia; 1158; 166 antibodies from 30 providers.
DR DNASU; 8732; -.
DR Ensembl; ENST00000369475.7; ENSP00000358487.4; ENSG00000111880.16. [O60942-2]
DR Ensembl; ENST00000369485.9; ENSP00000358497.4; ENSG00000111880.16. [O60942-1]
DR Ensembl; ENST00000538899.2; ENSP00000442609.2; ENSG00000111880.16. [O60942-3]
DR GeneID; 8732; -.
DR KEGG; hsa:8732; -.
DR MANE-Select; ENST00000369485.9; ENSP00000358497.4; NM_003800.5; NP_003791.3.
DR UCSC; uc003pmr.4; human. [O60942-1]
DR CTD; 8732; -.
DR DisGeNET; 8732; -.
DR GeneCards; RNGTT; -.
DR HGNC; HGNC:10073; RNGTT.
DR HPA; ENSG00000111880; Low tissue specificity.
DR MIM; 603512; gene.
DR neXtProt; NX_O60942; -.
DR OpenTargets; ENSG00000111880; -.
DR PharmGKB; PA34446; -.
DR VEuPathDB; HostDB:ENSG00000111880; -.
DR eggNOG; KOG2386; Eukaryota.
DR GeneTree; ENSGT00940000156953; -.
DR HOGENOM; CLU_021710_3_0_1; -.
DR InParanoid; O60942; -.
DR OMA; WMSARLL; -.
DR OrthoDB; 1544021at2759; -.
DR PhylomeDB; O60942; -.
DR TreeFam; TF314914; -.
DR BioCyc; MetaCyc:HS03479-MON; -.
DR BRENDA; 2.7.7.50; 2681.
DR BRENDA; 3.6.1.74; 2681.
DR PathwayCommons; O60942; -.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR SignaLink; O60942; -.
DR SIGNOR; O60942; -.
DR BioGRID-ORCS; 8732; 785 hits in 1060 CRISPR screens.
DR ChiTaRS; RNGTT; human.
DR EvolutionaryTrace; O60942; -.
DR GeneWiki; RNGTT; -.
DR GenomeRNAi; 8732; -.
DR Pharos; O60942; Tbio.
DR PRO; PR:O60942; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60942; protein.
DR Bgee; ENSG00000111880; Expressed in cardia of stomach and 201 other tissues.
DR Genevisible; O60942; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; TAS:Reactome.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0008192; F:RNA guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IDA:UniProtKB.
DR CDD; cd07895; Adenylation_mRNA_capping; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR017074; mRNA_cap_enz_bifunc.
DR InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR InterPro; IPR013846; mRNA_cap_enzyme_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF03919; mRNA_cap_C; 1.
DR Pfam; PF01331; mRNA_cap_enzyme; 1.
DR PIRSF; PIRSF036958; mRNA_capping_HCE; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTP-binding; Host-virus interaction;
KW Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Protein phosphatase;
KW Reference proteome; Transferase.
FT CHAIN 1..597
FT /note="mRNA-capping enzyme"
FT /id="PRO_0000210108"
FT DOMAIN 25..183
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..212
FT /note="TPase"
FT REGION 181..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..597
FT /note="GTase"
FT REGION 330..386
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000250"
FT REGION 570..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 294
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000269|PubMed:21636784"
FT BINDING 299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 343..345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 458..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 528..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 424..446
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9512541"
FT /id="VSP_003202"
FT VAR_SEQ 481..597
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9512541"
FT /id="VSP_003203"
FT VAR_SEQ 504..597
FT /note="TKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTK
FT EMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT -> CLFIFSVLFLDVL
FT LSGIHQNLANNNQHIKISCSSTLGG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9473487"
FT /id="VSP_003204"
FT VARIANT 594
FT /note="R -> H (in dbSNP:rs17856595)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046481"
FT MUTAGEN 234
FT /note="E->A: No effect on GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784"
FT MUTAGEN 294
FT /note="K->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:9512541"
FT MUTAGEN 299
FT /note="R->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:9512541"
FT MUTAGEN 345
FT /note="E->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:9512541"
FT MUTAGEN 458
FT /note="K->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784,
FT ECO:0000269|PubMed:9512541"
FT MUTAGEN 460
FT /note="K->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784,
FT ECO:0000269|PubMed:9512541"
FT MUTAGEN 528
FT /note="R->A: Strongly reduced GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784"
FT MUTAGEN 530
FT /note="R->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784"
FT MUTAGEN 532
FT /note="D->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784"
FT MUTAGEN 533
FT /note="K->A: Loss of GTase activity."
FT /evidence="ECO:0000269|PubMed:21636784"
FT CONFLICT 30
FT /note="M -> I (in Ref. 1; AAB91559)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="P -> T (in Ref. 6; AAH19954)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="Q -> P (in Ref. 1; AAB91559)"
FT /evidence="ECO:0000305"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2C46"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:2C46"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2C46"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3S24"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 339..351
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 354..367
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:3S24"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:3S24"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 466..476
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:3S24"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 539..550
FT /evidence="ECO:0007829|PDB:3S24"
FT HELIX 555..563
FT /evidence="ECO:0007829|PDB:3S24"
SQ SEQUENCE 597 AA; 68557 MW; 51CEEC1B190603DE CRC64;
MAHNKIPPRW LNCPRRGQPV AGRFLPLKTM LGPRYDSQVA EENRFHPSML SNYLKSLKVK
MGLLVDLTNT SRFYDRNDIE KEGIKYIKLQ CKGHGECPTT ENTETFIRLC ERFNERNPPE
LIGVHCTHGF NRTGFLICAF LVEKMDWSIE AAVATFAQAR PPGIYKGDYL KELFRRYGDI
EEAPPPPLLP DWCFEDDEDE DEDEDGKKES EPGSSASFGK RRKERLKLGA IFLEGVTVKG
VTQVTTQPKL GEVQQKCHQF CGWEGSGFPG AQPVSMDKQN IKLLDLKPYK VSWKADGTRY
MMLIDGTNEV FMIDRDNSVF HVSNLEFPFR KDLRMHLSNT LLDGEMIIDR VNGQAVPRYL
IYDIIKFNSQ PVGDCDFNVR LQCIEREIIS PRHEKMKTGL IDKTQEPFSV RNKPFFDICT
SRKLLEGNFA KEVSHEMDGL IFQPTGKYKP GRCDDILKWK PPSLNSVDFR LKITRMGGEG
LLPQNVGLLY VGGYERPFAQ IKVTKELKQY DNKIIECKFE NNSWVFMRQR TDKSFPNAYN
TAMAVCNSIS NPVTKEMLFE FIDRCTAASQ GQKRKHHLDP DTELMPPPPP KRPRPLT
