GenomeNet

Database: UniProt
Entry: S7P136_MYOBR
LinkDB: S7P136_MYOBR
Original site: S7P136_MYOBR 
ID   S7P136_MYOBR            Unreviewed;       384 AA.
AC   S7P136;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00012699};
DE            EC=2.4.1.80 {ECO:0000256|ARBA:ARBA00012699};
GN   ORFNames=D623_10031550 {ECO:0000313|EMBL:EPQ03663.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ03663.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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:0000256|ARBA:ARBA00033713};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248;
CC         Evidence={ECO:0000256|ARBA:ARBA00033713};
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:0000256|ARBA:ARBA00033670};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244;
CC         Evidence={ECO:0000256|ARBA:ARBA00033670};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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; KE161425; EPQ03663.1; -; Genomic_DNA.
DR   RefSeq; XP_014389875.1; XM_014534389.1.
DR   AlphaFoldDB; S7P136; -.
DR   GeneID; 102249980; -.
DR   KEGG; myb:102249980; -.
DR   CTD; 7357; -.
DR   eggNOG; KOG2547; Eukaryota.
DR   OrthoDB; 2786173at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008120; F:ceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
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.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPQ03663.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   384 AA;  43791 MW;  BED27CA9C5857BC0 CRC64;
     MALFGFSLFL VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK GVDPNLINNL
     ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG INPKINNLMP
     GYEVAKYDLI WICDSGIRVL PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG
     TSHPRSYISA HVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWRF
     AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS LIIGWAAHHV
     FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT IYIFLSALWD
     PTISWRTGRY RLRCGGTAEE ILDV
//
DBGET integrated database retrieval system