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A4GAT_MOUSE
ID   A4GAT_MOUSE             Reviewed;         359 AA.
AC   Q67BJ4;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Lactosylceramide 4-alpha-galactosyltransferase;
DE            EC=2.4.1.228 {ECO:0000250|UniProtKB:Q9NPC4};
DE   AltName: Full=Alpha-1,4-N-acetylglucosaminyltransferase;
DE   AltName: Full=Alpha-1,4-galactosyltransferase;
DE   AltName: Full=Alpha4Gal-T1;
DE   AltName: Full=Globotriaosylceramide synthase;
DE            Short=Gb3 synthase;
DE   AltName: Full=UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase;
GN   Name=A4galt {ECO:0000312|EMBL:AAR18365.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:AAR18365.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Y., Abe A., Hiraoka M., Shayman J.A.;
RT   "Mouse Gb3 synthase.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of galactose from UDP-alpha-D-
CC       galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC       (1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside
CC       Gb3Cer (d18:1(4E)). Also able to transfer galactose to
CC       galactosylceramide/beta-D-Gal-(1<->1')-Cer. Globoside Gb3Cer is a
CC       glycosphingolipid of the globo serie, one of the major types of neutral
CC       root structures of glycosphingolipids, that constitute a significant
CC       portion of mammalian cell membranes. {ECO:0000250|UniProtKB:Q9NPC4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-
CC         alpha-D-galactose = globoside Gb3Cer (d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:11924, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC         ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC         EC=2.4.1.228; Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11925;
CC         Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Gal-(1<->1')-Cer + UDP-alpha-D-galactose = alpha-D-Gal-
CC         (1->4)-beta-D-Gal-(1<->1')-Cer + H(+) + UDP; Xref=Rhea:RHEA:60044,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:143593, ChEBI:CHEBI:143594;
CC         Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60045;
CC         Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC   -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q9NPC4}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=a4GalT;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_453";
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DR   EMBL; AY371179; AAR18365.1; -; mRNA.
DR   RefSeq; NP_001004150.1; NM_001004150.3.
DR   RefSeq; NP_001164425.1; NM_001170954.1.
DR   AlphaFoldDB; Q67BJ4; -.
DR   STRING; 10090.ENSMUSP00000129719; -.
DR   CAZy; GT32; Glycosyltransferase Family 32.
DR   GlyGen; Q67BJ4; 2 sites.
DR   iPTMnet; Q67BJ4; -.
DR   PhosphoSitePlus; Q67BJ4; -.
DR   PaxDb; Q67BJ4; -.
DR   PRIDE; Q67BJ4; -.
DR   ProteomicsDB; 296425; -.
DR   Antibodypedia; 239; 235 antibodies from 30 providers.
DR   DNASU; 239559; -.
DR   Ensembl; ENSMUST00000049530; ENSMUSP00000057999; ENSMUSG00000047878.
DR   Ensembl; ENSMUST00000164614; ENSMUSP00000129719; ENSMUSG00000047878.
DR   GeneID; 239559; -.
DR   KEGG; mmu:239559; -.
DR   UCSC; uc007xae.2; mouse.
DR   CTD; 53947; -.
DR   MGI; MGI:3512453; A4galt.
DR   VEuPathDB; HostDB:ENSMUSG00000047878; -.
DR   eggNOG; KOG1928; Eukaryota.
DR   GeneTree; ENSGT00510000047981; -.
DR   HOGENOM; CLU_049512_2_0_1; -.
DR   InParanoid; Q67BJ4; -.
DR   OMA; AFYPIRW; -.
DR   OrthoDB; 1082380at2759; -.
DR   PhylomeDB; Q67BJ4; -.
DR   TreeFam; TF324053; -.
DR   BioGRID-ORCS; 239559; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; A4galt; mouse.
DR   PRO; PR:Q67BJ4; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q67BJ4; protein.
DR   Bgee; ENSMUSG00000047878; Expressed in ectoplacental cone and 118 other tissues.
DR   ExpressionAtlas; Q67BJ4; baseline and differential.
DR   Genevisible; Q67BJ4; MM.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0008378; F:galactosyltransferase activity; ISO:MGI.
DR   GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050512; F:lactosylceramide 4-alpha-galactosyltransferase activity; IDA:MGI.
DR   GO; GO:0015643; F:toxic substance binding; IMP:MGI.
DR   GO; GO:0001576; P:globoside biosynthetic process; IDA:MGI.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007009; P:plasma membrane organization; ISO:MGI.
DR   InterPro; IPR007652; A1-4-GlycosylTfrase_dom.
DR   InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF04572; Gb3_synth; 1.
DR   Pfam; PF04488; Gly_transf_sug; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="Lactosylceramide 4-alpha-galactosyltransferase"
FT                   /id="PRO_0000080579"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..359
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           198..200
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   359 AA;  41366 MW;  B6380E88BF0A4676 CRC64;
     MGISCSHLEE TMSKPPDCLL RMLRGTPRQR VFTFFIISFK FMFLISILIY WHTVGAPKDQ
     REYSLPVDFS CPQLAFPRVS APGNIFFLET SDRTSPNFLF MCSVESAARA HPESQVVVLM
     KGLPRDTTAQ PRNLGISLLS CFPNVWIRPL DLQELFEDTP LAAWYSEARH RWEPYQLPVL
     SDASRIALLW KFGGIYLDTD FIVLKNLLNL TNTLGIQSRY VLNGAFLAFE RKHEFLALCL
     HDFVANYNGW IWGHQGPQLL TRVFKKWCSI QSLEKSHACR GVTALPPEAF YPIPWQNWKK
     YFEDISPEEL TQLLNATYAV HVWNKKSQGT HLEATSKALL AQLHARYCPT THRAMKMYL
 
 
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