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Database: UniProt
Entry: L5M8L1_MYODS
LinkDB: L5M8L1_MYODS
Original site: L5M8L1_MYODS 
ID   L5M8L1_MYODS            Unreviewed;       438 AA.
AC   L5M8L1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 {ECO:0000256|ARBA:ARBA00039292};
DE            EC=2.4.1.102 {ECO:0000256|ARBA:ARBA00038948};
DE            EC=2.4.1.148 {ECO:0000256|ARBA:ARBA00038912};
DE            EC=2.4.1.150 {ECO:0000256|ARBA:ARBA00038907};
DE   AltName: Full=C2GnT-mucin type {ECO:0000256|ARBA:ARBA00041719};
GN   ORFNames=MDA_GLEAN10003504 {ECO:0000313|EMBL:ELK34600.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34600.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Glycosyltransferase that can synthesize all known mucin beta
CC       6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan
CC       branching, 2 important steps in mucin-type biosynthesis. Has also I-
CC       branching enzyme activity by converting linear into branched poly-N-
CC       acetyllactosaminoglycans, leading to introduce the blood group I
CC       antigen during embryonic development. {ECO:0000256|ARBA:ARBA00037166}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC         = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-
CC         glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-seryl-
CC         [protein] + H(+) + UDP; Xref=Rhea:RHEA:56188, Rhea:RHEA-COMP:11691,
CC         Rhea:RHEA-COMP:14412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:87079, ChEBI:CHEBI:139581;
CC         EC=2.4.1.148; Evidence={ECO:0000256|ARBA:ARBA00036128};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC         glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-
CC         beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-
CC         threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56192, Rhea:RHEA-
CC         COMP:11692, Rhea:RHEA-COMP:14413, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:87080,
CC         ChEBI:CHEBI:139580; EC=2.4.1.148;
CC         Evidence={ECO:0000256|ARBA:ARBA00035837};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC         = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC         (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-
CC         COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102;
CC         Evidence={ECO:0000256|ARBA:ARBA00035966};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC         glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-
CC         glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC         [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923,
CC         Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607;
CC         EC=2.4.1.102; Evidence={ECO:0000256|ARBA:ARBA00036642};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC         beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-
CC         D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-
CC         (1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC         Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372;
CC         EC=2.4.1.150; Evidence={ECO:0000256|ARBA:ARBA00036298};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC       {ECO:0000256|ARBA:ARBA00038150}.
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DR   EMBL; KB103034; ELK34600.1; -; Genomic_DNA.
DR   RefSeq; XP_015415685.1; XM_015560199.1.
DR   AlphaFoldDB; L5M8L1; -.
DR   GeneID; 102751306; -.
DR   KEGG; myd:102751306; -.
DR   CTD; 9245; -.
DR   eggNOG; KOG0799; Eukaryota.
DR   OrthoDB; 5403607at2759; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR003406; Glyco_trans_14.
DR   PANTHER; PTHR19297:SF81; BETA-1,3-GALACTOSYL-O-GLYCOSYL-GLYCOPROTEIN BETA-1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE 3; 1.
DR   PANTHER; PTHR19297; GLYCOSYLTRANSFERASE 14 FAMILY MEMBER; 1.
DR   Pfam; PF02485; Branch; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:ELK34600.1};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK34600.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   438 AA;  51186 MW;  52C498A1638A7B55 CRC64;
     MKMTWWKKKL CRQHYLWALG CYLLLAIVAL RFSLRLKCDF DSLDLESKHC RDILYKSLQL
     TARRSINCSR IIQGDKEAVI EALLDRLEVK KKWKPFTDTD YINMTRDCEY FKAKRKFIQY
     PLSKEELDFP IAYSMVVHEK IENFERLLRA VYAPQNIYCV HVDQKSPDTF KEAVRAIISC
     FPNVFIASKL VRVVYASWSR VQADLNCMED LLQSSVPWKY LLNTCGTDFP IKTNAEMVLA
     LKMLNGKNSM ESEIPTEYKR SRWQYHYEVT DTIHVTNKKK DPPPNNLPMF VGNAYIVASR
     GFVQQVFENP KARQLIEWVK DTYSPDEHLW ATLQRAPWMP GSVPYHPKFH MSDMAAIARL
     VKWQGHEGDI SMGAPYAPCS GTHQRAVCIY GVGDLHWILQ NHHLLANKFD PKVDDNVLQC
     LEEYLRYKTI SRLNSEIH
//
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