ID UGGG1_HUMAN Reviewed; 1555 AA.
AC Q9NYU2; Q53QP2; Q53SL3; Q8IW30; Q9H8I4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE Short=UGT1;
DE Short=hUGT1;
DE EC=2.4.1.- {ECO:0000269|PubMed:24415556};
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=UGGT1;
GN Synonyms=GT, UGCGL1, UGGT, UGT1 {ECO:0000303|PubMed:10694380},
GN UGTR {ECO:0000250|UniProtKB:Q9JLA3};
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] {ECO:0000305, ECO:0000312|EMBL:AAF66232.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-1452; GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND
RP ASN-1457.
RC TISSUE=Fetal liver {ECO:0000312|EMBL:AAF66232.1};
RX PubMed=10694380; DOI=10.1021/bi9916473;
RA Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J.;
RT "Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase
RT differ in mRNA expression and enzymatic activity.";
RL Biochemistry 39:2149-2163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3] {ECO:0000312|EMBL:AAH41098.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH41098.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB14632.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2).
RC TISSUE=Placenta {ECO:0000312|EMBL:BAB14632.1};
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP INTERACTION WITH METTL23.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SELENOF, AND MUTAGENESIS OF
RP ASP-1358.
RX PubMed=24415556; DOI=10.1093/glycob/cwt163;
RA Takeda Y., Seko A., Hachisu M., Daikoku S., Izumi M., Koizumi A.,
RA Fujikawa K., Kajihara Y., Ito Y.;
RT "Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are
RT enzymatically active.";
RL Glycobiology 24:344-350(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the protein,
CC thus providing quality control for protein folding in the endoplasmic
CC reticulum. Reglucosylated proteins are recognized by calreticulin for
CC recycling to the endoplasmic reticulum and refolding or degradation.
CC {ECO:0000269|PubMed:10694380}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000269|PubMed:10694380};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10694380};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10694380};
CC -!- ACTIVITY REGULATION: Catalytic activity is enhanced by complex
CC formation with SELENOF. {ECO:0000269|PubMed:24415556}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10694380, ECO:0000269|PubMed:15815621}.
CC -!- SUBUNIT: Monomer as well as in a tight complex with SELENOF
CC (PubMed:24415556). Interacts with METTL23 (PubMed:23349634). Part of a
CC large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX (By
CC similarity). {ECO:0000250|UniProtKB:Q9JLA3,
CC ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:24415556}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:10694380}. Endoplasmic reticulum-
CC Golgi intermediate compartment {ECO:0000255|PROSITE-ProRule:PRU10138,
CC ECO:0000269|PubMed:10694380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYU2-2; Sequence=VSP_036508;
CC -!- TISSUE SPECIFICITY: Higher levels in pancreas, skeletal muscle, kidney,
CC and brain. Low levels in lung and heart. {ECO:0000269|PubMed:10694380}.
CC -!- INDUCTION: By tunicamycin and A23187. Induced 3-4 fold 10 hours after
CC treatment. {ECO:0000269|PubMed:10694380}.
CC -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000269|PubMed:10694380}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB14632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF227905; AAF66232.1; -; mRNA.
DR EMBL; AC017079; AAY14735.1; -; Genomic_DNA.
DR EMBL; AC108059; AAY14885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041098; AAH41098.1; -; mRNA.
DR EMBL; AK023671; BAB14632.1; ALT_INIT; mRNA.
DR CCDS; CCDS2154.1; -. [Q9NYU2-1]
DR RefSeq; NP_064505.1; NM_020120.3. [Q9NYU2-1]
DR AlphaFoldDB; Q9NYU2; -.
DR SMR; Q9NYU2; -.
DR BioGRID; 121217; 217.
DR IntAct; Q9NYU2; 70.
DR MINT; Q9NYU2; -.
DR STRING; 9606.ENSP00000259253; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR GlyConnect; 1871; 6 N-Linked glycans (1 site).
DR GlyCosmos; Q9NYU2; 4 sites, 7 glycans.
DR GlyGen; Q9NYU2; 7 sites, 7 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; Q9NYU2; -.
DR MetOSite; Q9NYU2; -.
DR PhosphoSitePlus; Q9NYU2; -.
DR SwissPalm; Q9NYU2; -.
DR BioMuta; UGGT1; -.
DR DMDM; 224471872; -.
DR CPTAC; CPTAC-290; -.
DR EPD; Q9NYU2; -.
DR jPOST; Q9NYU2; -.
DR MassIVE; Q9NYU2; -.
DR MaxQB; Q9NYU2; -.
DR PaxDb; 9606-ENSP00000259253; -.
DR PeptideAtlas; Q9NYU2; -.
DR PRIDE; Q9NYU2; -.
DR ProteomicsDB; 83277; -. [Q9NYU2-1]
DR ProteomicsDB; 83278; -. [Q9NYU2-2]
DR Pumba; Q9NYU2; -.
DR Antibodypedia; 2454; 159 antibodies from 27 providers.
DR DNASU; 56886; -.
DR Ensembl; ENST00000259253.11; ENSP00000259253.6; ENSG00000136731.13. [Q9NYU2-1]
DR GeneID; 56886; -.
DR KEGG; hsa:56886; -.
DR MANE-Select; ENST00000259253.11; ENSP00000259253.6; NM_020120.4; NP_064505.1.
DR UCSC; uc002tps.4; human. [Q9NYU2-1]
DR AGR; HGNC:15663; -.
DR CTD; 56886; -.
DR DisGeNET; 56886; -.
DR GeneCards; UGGT1; -.
DR HGNC; HGNC:15663; UGGT1.
DR HPA; ENSG00000136731; Low tissue specificity.
DR MIM; 605897; gene.
DR neXtProt; NX_Q9NYU2; -.
DR OpenTargets; ENSG00000136731; -.
DR PharmGKB; PA38014; -.
DR VEuPathDB; HostDB:ENSG00000136731; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR InParanoid; Q9NYU2; -.
DR OMA; KNFYRYV; -.
DR OrthoDB; 1734at2759; -.
DR PhylomeDB; Q9NYU2; -.
DR TreeFam; TF300320; -.
DR PathwayCommons; Q9NYU2; -.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; Q9NYU2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 56886; 16 hits in 1161 CRISPR screens.
DR ChiTaRS; UGGT1; human.
DR GenomeRNAi; 56886; -.
DR Pharos; Q9NYU2; Tbio.
DR PRO; PR:Q9NYU2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NYU2; Protein.
DR Bgee; ENSG00000136731; Expressed in calcaneal tendon and 189 other cell types or tissues.
DR ExpressionAtlas; Q9NYU2; baseline and differential.
DR Genevisible; Q9NYU2; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; TAS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF3; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..42
FT /evidence="ECO:0000250"
FT CHAIN 43..1555
FT /note="UDP-glucose:glycoprotein glucosyltransferase 1"
FT /id="PRO_0000012271"
FT REGION 1244..1555
FT /note="Glucosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 1534..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1552..1555
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036508"
FT MUTAGEN 1358
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24415556"
FT MUTAGEN 1452..1457
FT /note="Missing: Inactive."
FT MUTAGEN 1452
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:10694380"
FT MUTAGEN 1453
FT /note="Q->A: 4% active."
FT /evidence="ECO:0000269|PubMed:10694380"
FT MUTAGEN 1454
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:10694380"
FT MUTAGEN 1455
FT /note="L->A: 2% active."
FT /evidence="ECO:0000269|PubMed:10694380"
FT MUTAGEN 1456
FT /note="P->A: 41% active."
FT /evidence="ECO:0000269|PubMed:10694380"
FT MUTAGEN 1457
FT /note="N->A: 7% active."
FT /evidence="ECO:0000269|PubMed:10694380"
FT CONFLICT 1487
FT /note="A -> T (in Ref. 4; BAB14632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1555 AA; 177190 MW; 0A5274A4A65152D3 CRC64;
MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS LTTKWFSTPL
LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH AILEAAFQFL SPLQQNLFKF
CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF FSVHGKKTCE SDTLEALLLT ASERPKPLLF
KGDHRYPSSN PESPVVIFYS EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS QNFPTKARAI
TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM DLDTQDIFSL FDVLRNEARV
MEGLHRLGIE GLSLHNVLKL NIQPSEADYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE LETITMHKIL
ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL TAERDYLDLT ASNNFFVDDY
ARFTILDSQG KTAAVANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIKHQKSSNN VRISMINNPA KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE
ALAAGADIAE FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA QRLAPLLLVL AQLINMNLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTSD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
VIVDTIVMAN LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF
KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ DKDDIINIFS
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMANEY NFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ KREEL
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