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Database: UniProt
Entry: A0A3Q1JFD0_ANATE
LinkDB: A0A3Q1JFD0_ANATE
Original site: A0A3Q1JFD0_ANATE 
ID   A0A3Q1JFD0_ANATE        Unreviewed;       394 AA.
AC   A0A3Q1JFD0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00012699};
DE            EC=2.4.1.80 {ECO:0000256|ARBA:ARBA00012699};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000033717.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000033717.1}
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; A0A3Q1JFD0; -.
DR   STRING; 64144.ENSATEP00000033717; -.
DR   Ensembl; ENSATET00000034206.2; ENSATEP00000033717.1; ENSATEG00000023209.2.
DR   GeneTree; ENSGT00390000012898; -.
DR   InParanoid; A0A3Q1JFD0; -.
DR   OMA; HGSMPFH; -.
DR   OrthoDB; 2786173at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000265040; Unplaced.
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:UP000265040};
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        6..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   394 AA;  44379 MW;  CEAF72985DAE3343 CRC64;
     MAVLDLAMQG FAVFGFILFF VLWLMHFMSI IYVRLHLHKK RSEAKQSFTQ LAGVSLLKPL
     KGVDPNLISN LETFFTLDYP KYEILLCVQD TDDPAVDVCK KLLGKYPNVD ARLFIGGKKV
     GINPKINNLM PGYEGAKYGL VWICDSGIRV KPDTLTDLTN HMTEKVGLVH GLPYVADRQG
     FAATLEQVYF GTSHPRSYIS ANVTGIKCVT GMSCLMRKDV LDQAGGLVAF AQYIAEDYFM
     AKAIADRGWK FSMATQVALQ NSGSYSIGQF QSRMIRWTKL RINMLPGTVL EPVSECFLAS
     LIIGWAAHHV FRWDMMVFFM CHCLAWFISD YIQLTGIQGA PLCFSKLDFA VAWFIRESMA
     VQIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV
//
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