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B3GT2_PONAB
ID   B3GT2_PONAB             Reviewed;         422 AA.
AC   Q5R5Y3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Beta-1,3-galactosyltransferase 2;
DE            Short=Beta-1,3-GalTase 2;
DE            Short=Beta3Gal-T2;
DE            Short=Beta3GalT2;
DE            EC=2.4.1.86 {ECO:0000250|UniProtKB:O43825};
DE   AltName: Full=UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2;
GN   Name=B3GALT2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC       UDP-galactose to substrates with a terminal beta-N-acetylglucosamine
CC       (beta-GlcNAc) residue. Can also utilize substrates with a terminal
CC       galactose residue, albeit with lower efficiency. Involved in the
CC       biosynthesis of the carbohydrate moieties of glycolipids and
CC       glycoproteins. Inactive towards substrates with terminal alpha-N-
CC       acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-
CC       GalNAc) residues. {ECO:0000250|UniProtKB:O43825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC         galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC         derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:133506; EC=2.4.1.86;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC         Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-
CC         GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) +
CC         H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:66914; EC=2.4.1.86;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-
CC         alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-
CC         GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:78565, ChEBI:CHEBI:142448;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937;
CC         Evidence={ECO:0000250|UniProtKB:O43825};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; CR860718; CAH92833.1; -; mRNA.
DR   RefSeq; NP_001126654.1; NM_001133182.1.
DR   AlphaFoldDB; Q5R5Y3; -.
DR   SMR; Q5R5Y3; -.
DR   STRING; 9601.ENSPPYP00000000448; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   GeneID; 100173654; -.
DR   KEGG; pon:100173654; -.
DR   CTD; 8707; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   InParanoid; Q5R5Y3; -.
DR   OrthoDB; 1037602at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Unplaced.
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:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045821; B3GT2_N.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF19341; B3GALT2_N; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW   Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..422
FT                   /note="Beta-1,3-galactosyltransferase 2"
FT                   /id="PRO_0000219152"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..422
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          90..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   422 AA;  49239 MW;  F28CEDC31C4A9717 CRC64;
     MLQWRRRHCC FAKMTWNAKR SLFRTHLIGV LSLVFLFAMF LFFNHHDWLP GRAGFKENPV
     TYTFRGFRST KSETNHSSLR NIWKETVPQT LRPQTATNSN NTDLSPQGVT GLENTLSANG
     SIYNEKGTGY PNSYHFKYII NEPEKCQEKS PFLILLIAAE PGQIEARRAI RQTWGNESLA
     PGIQITRIFL LGLSIKLNGY LQRAILEESR QYHDIIQQEY LDTYYNLTIK TLMGMNWVAT
     YCPHIPYVMK TDSDMFVNTE YLINKLLKPD LPPRHNYFTG YLMRGYAPNR NKDSKWYMPP
     DLYPSERYPV FCSGTGYVFS GDLAEKIFKV SLGIRRLHLE DVYVGICLAK LRIDPVPPPN
     EFVFNHWRVS YSSCKYSHLI TSHQFQPSEL IKYWNHLQQN KHNACANAAK EKAGRYRHRK
     LH
 
 
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