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Database: UniProt
Entry: H2PT21_PONAB
LinkDB: H2PT21_PONAB
Original site: H2PT21_PONAB 
ID   H2PT21_PONAB            Unreviewed;       391 AA.
AC   H2PT21;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00012699};
DE            EC=2.4.1.80 {ECO:0000256|ARBA:ARBA00012699};
GN   Name=UGCG {ECO:0000313|Ensembl:ENSPPYP00000021849.3};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000021849.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000021849.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPPYP00000021849.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; H2PT21; -.
DR   Ensembl; ENSPPYT00000022746.3; ENSPPYP00000021849.3; ENSPPYG00000019502.3.
DR   eggNOG; KOG2547; Eukaryota.
DR   GeneTree; ENSGT00390000012898; -.
DR   HOGENOM; CLU_030898_0_0_1; -.
DR   InParanoid; H2PT21; -.
DR   OMA; HGSMPFH; -.
DR   TreeFam; TF314564; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
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:1903575; P:cornified envelope assembly; IEA:Ensembl.
DR   GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR   GO; GO:0006679; P:glucosylceramide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0098856; P:intestinal lipid absorption; IEA:Ensembl.
DR   GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0033210; P:leptin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:Ensembl.
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:UP000001595};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   391 AA;  44636 MW;  A4C36BB87A231AAD 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
     KAIADRGWKF AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS
     LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT
     IYIFLSALWD PTISWRTGRY RLRCGVIHFL Q
//
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