ID   CEGT_HUMAN              Reviewed;         394 AA.
AC   Q16739; Q5T258;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Ceramide glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.80 {ECO:0000269|PubMed:8643456};
DE   AltName: Full=GLCT-1;
DE   AltName: Full=Glucosylceramide synthase;
DE            Short=GCS {ECO:0000303|PubMed:33361282};
DE   AltName: Full=Glycosylceramide synthase {ECO:0000305};
DE   AltName: Full=UDP-glucose ceramide glucosyltransferase;
DE   AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase;
GN   Name=UGCG {ECO:0000312|HGNC:HGNC:12524};
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Melanoma;
RX   PubMed=8643456; DOI=10.1073/pnas.93.10.4638;
RA   Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.;
RT   "Expression cloning of a cDNA for human ceramide glucosyltransferase that
RT   catalyzes the first glycosylation step of glycosphingolipid synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:4638-4643(1996).
RN   [2]
RP   ERRATUM OF PUBMED:8643456.
RX   PubMed=8901638; DOI=10.1073/pnas.93.22.12654;
RA   Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.;
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12654-12654(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   FUNCTION.
RX   PubMed=1532799; DOI=10.1083/jcb.117.2.259;
RA   Jeckel D., Karrenbauer A., Burger K.N., van Meer G., Wieland F.;
RT   "Glucosylceramide is synthesized at the cytosolic surface of various Golgi
RT   subfractions.";
RL   J. Cell Biol. 117:259-267(1992).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9545298; DOI=10.1074/jbc.273.16.9651;
RA   Watanabe R., Wu K., Paul P., Marks D.L., Kobayashi T., Pittelkow M.R.,
RA   Pagano R.E.;
RT   "Up-regulation of glucosylceramide synthase expression and activity during
RT   human keratinocyte differentiation.";
RL   J. Biol. Chem. 273:9651-9655(1998).
RN   [9]
RP   INTERACTION WITH RTN1, AND SUBCELLULAR LOCATION.
RX   PubMed=12873973;
RA   Di Sano F., Fazi B., Citro G., Lovat P.E., Cesareni G., Piacentini M.;
RT   "Glucosylceramide synthase and its functional interaction with RTN-1C
RT   regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells.";
RL   Cancer Res. 63:3860-3865(2003).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=33361282; DOI=10.1194/jlr.ra120001043;
RA   Boer D.E., Mirzaian M., Ferraz M.J., Zwiers K.C., Baks M.V., Hazeu M.D.,
RA   Ottenhoff R., Marques A.R.A., Meijer R., Roos J.C.P., Cox T.M., Boot R.G.,
RA   Pannu N., Overkleeft H.S., Artola M., Aerts J.M.;
RT   "Human glucocerebrosidase mediates formation of xylosyl-cholesterol by
RT   beta-xylosidase and transxylosidase reactions.";
RL   J. Lipid Res. 62:100018-100018(2021).
CC   -!- FUNCTION: Participates in the initial step of the glucosylceramide-
CC       based glycosphingolipid/GSL synthetic pathway at the cytosolic surface
CC       of the Golgi (PubMed:8643456, PubMed:1532799). Catalyzes the transfer
CC       of glucose from UDP-glucose to ceramide to produce
CC       glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-
CC       4-enine) (PubMed:1532799, PubMed:8643456). GlcCer is the core component
CC       of glycosphingolipids/GSLs, amphipathic molecules consisting of a
CC       ceramide lipid moiety embedded in the outer leaflet of the membrane,
CC       linked to one of hundreds of different externally oriented
CC       oligosaccharide structures (PubMed:8643456). Glycosphingolipids are
CC       essential components of membrane microdomains that mediate membrane
CC       trafficking and signal transduction, implicated in many fundamental
CC       cellular processes, including growth, differentiation, migration,
CC       morphogenesis, cell-to-cell and cell-to-matrix interactions (By
CC       similarity). They are required for instance in the proper development
CC       and functioning of the nervous system (By similarity). As an example of
CC       their role in signal transduction, they regulate the leptin
CC       receptor/LEPR in the leptin-mediated signaling pathway (By similarity).
CC       They also play an important role in the establishment of the skin
CC       barrier regulating keratinocyte differentiation and the proper assembly
CC       of the cornified envelope (By similarity). The biosynthesis of GSLs is
CC       also required for the proper intestinal endocytic uptake of nutritional
CC       lipids (By similarity). Catalyzes the synthesis of
CC       xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-
CC       enine) using UDP-Xyl as xylose donor (PubMed:33361282).
CC       {ECO:0000250|UniProtKB:O88693, ECO:0000269|PubMed:1532799,
CC       ECO:0000269|PubMed:33361282, ECO:0000269|PubMed:8643456,
CC       ECO:0000303|PubMed:8643456}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-
CC         glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC         Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801,
CC         ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80;
CC         Evidence={ECO:0000269|PubMed:8643456};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089;
CC         Evidence={ECO:0000269|PubMed:8643456};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + UDP-alpha-D-xylose = a beta-D-
CC         xylosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC         Xref=Rhea:RHEA:70243, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:189068;
CC         Evidence={ECO:0000269|PubMed:33361282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244;
CC         Evidence={ECO:0000269|PubMed:33361282};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(9Z-octadecenoyl)-sphing-4-enine + UDP-alpha-D-xylose =
CC         beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + H(+) +
CC         UDP; Xref=Rhea:RHEA:70247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:77996, ChEBI:CHEBI:189081;
CC         Evidence={ECO:0000269|PubMed:33361282};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248;
CC         Evidence={ECO:0000269|PubMed:33361282};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000305|PubMed:33361282, ECO:0000305|PubMed:8643456}.
CC   -!- SUBUNIT: Interacts with RTN1; regulates the ceramide
CC       glucosyltransferase activity of UGCG. {ECO:0000269|PubMed:12873973}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:12873973}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9R0E0}.
CC   -!- TISSUE SPECIFICITY: Found in all tissues examined.
CC       {ECO:0000269|PubMed:8643456}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte differentiation.
CC       {ECO:0000269|PubMed:9545298}.
CC   -!- DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS
CC       active site, involved in catalysis and UDP-sugar binding.
CC       {ECO:0000250|UniProtKB:Q9R0E0}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; D50840; BAA09451.1; -; mRNA.
DR   EMBL; AK314847; BAG37364.1; -; mRNA.
DR   EMBL; AL442066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471105; EAW59091.1; -; Genomic_DNA.
DR   EMBL; BC038711; AAH38711.1; -; mRNA.
DR   CCDS; CCDS6782.1; -.
DR   RefSeq; NP_003349.1; NM_003358.2.
DR   AlphaFoldDB; Q16739; -.
DR   SMR; Q16739; -.
DR   BioGRID; 113204; 36.
DR   IntAct; Q16739; 14.
DR   MINT; Q16739; -.
DR   STRING; 9606.ENSP00000363397; -.
DR   BindingDB; Q16739; -.
DR   ChEMBL; CHEMBL2063; -.
DR   DrugBank; DB09039; Eliglustat.
DR   DrugBank; DB00419; Miglustat.
DR   DrugCentral; Q16739; -.
DR   GuidetoPHARMACOLOGY; 2528; -.
DR   SwissLipids; SLP:000000674; -.
DR   SwissLipids; SLP:000000675; -.
DR   CAZy; GT21; Glycosyltransferase Family 21.
DR   TCDB; 4.D.1.4.1; the putative vectorial glycosyl polymerization (vgp) family.
DR   iPTMnet; Q16739; -.
DR   PhosphoSitePlus; Q16739; -.
DR   SwissPalm; Q16739; -.
DR   BioMuta; UGCG; -.
DR   DMDM; 2498228; -.
DR   EPD; Q16739; -.
DR   jPOST; Q16739; -.
DR   MassIVE; Q16739; -.
DR   MaxQB; Q16739; -.
DR   PaxDb; 9606-ENSP00000363397; -.
DR   PeptideAtlas; Q16739; -.
DR   ProteomicsDB; 61050; -.
DR   Pumba; Q16739; -.
DR   Antibodypedia; 15178; 252 antibodies from 30 providers.
DR   DNASU; 7357; -.
DR   Ensembl; ENST00000374279.4; ENSP00000363397.3; ENSG00000148154.10.
DR   GeneID; 7357; -.
DR   KEGG; hsa:7357; -.
DR   MANE-Select; ENST00000374279.4; ENSP00000363397.3; NM_003358.3; NP_003349.1.
DR   UCSC; uc004bft.4; human.
DR   AGR; HGNC:12524; -.
DR   CTD; 7357; -.
DR   DisGeNET; 7357; -.
DR   GeneCards; UGCG; -.
DR   HGNC; HGNC:12524; UGCG.
DR   HPA; ENSG00000148154; Tissue enhanced (bone).
DR   MIM; 602874; gene.
DR   neXtProt; NX_Q16739; -.
DR   OpenTargets; ENSG00000148154; -.
DR   PharmGKB; PA37169; -.
DR   VEuPathDB; HostDB:ENSG00000148154; -.
DR   eggNOG; KOG2547; Eukaryota.
DR   GeneTree; ENSGT00390000012898; -.
DR   HOGENOM; CLU_030898_0_0_1; -.
DR   InParanoid; Q16739; -.
DR   OMA; HGSMPFH; -.
DR   OrthoDB; 2786173at2759; -.
DR   PhylomeDB; Q16739; -.
DR   TreeFam; TF314564; -.
DR   BioCyc; MetaCyc:HS07494-MONOMER; -.
DR   BRENDA; 2.4.1.80; 2681.
DR   PathwayCommons; Q16739; -.
DR   Reactome; R-HSA-9840309; Glycosphingolipid biosynthesis.
DR   SignaLink; Q16739; -.
DR   SIGNOR; Q16739; -.
DR   UniPathway; UPA00222; -.
DR   BioGRID-ORCS; 7357; 57 hits in 1176 CRISPR screens.
DR   ChiTaRS; UGCG; human.
DR   GeneWiki; UGCG; -.
DR   GenomeRNAi; 7357; -.
DR   Pharos; Q16739; Tclin.
DR   PRO; PR:Q16739; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q16739; Protein.
DR   Bgee; ENSG00000148154; Expressed in upper leg skin and 187 other cell types or tissues.
DR   ExpressionAtlas; Q16739; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0008120; F:ceramide glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:1903575; P:cornified envelope assembly; ISS:UniProtKB.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR   GO; GO:0006679; P:glucosylceramide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:Reactome.
DR   GO; GO:0098856; P:intestinal lipid absorption; ISS:UniProtKB.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR   GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
DR   GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB.
DR   CDD; cd02520; Glucosylceramide_synthase; 1.
DR   InterPro; IPR025993; Ceramide_glucosylTrfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF13506; Glyco_transf_21; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q16739; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..394
FT                   /note="Ceramide glucosyltransferase"
FT                   /id="PRO_0000059176"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..195
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..287
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..309
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..394
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   MOTIF           92
FT                   /note="D1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           144
FT                   /note="D2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           236
FT                   /note="D3"
FT                   /evidence="ECO:0000305"
FT   MOTIF           272..276
FT                   /note="(Q/R)XXRW"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT   SITE            193
FT                   /note="May play an important role in binding to the
FT                   inhibitors DEPC and PDMP"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O88693"
SQ   SEQUENCE   394 AA;  44854 MW;  3B998569F8A96449 CRC64;
     MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK
     GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG
     INPKINNLMP GYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF
     AATLEQVYFG TSHPRYYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA
     KAIADRGWRF AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS
     LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT
     IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV
//