ID B5XBA8_SALSA Unreviewed; 164 AA.
AC B5XBA8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00012614};
DE EC=2.4.1.141 {ECO:0000256|ARBA:ARBA00012614};
GN Name=ALG13 {ECO:0000313|EMBL:ACI68128.1};
GN Synonyms=alg13 {ECO:0000313|RefSeq:NP_001134591.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI68128.1};
RN [1] {ECO:0000313|EMBL:ACI68128.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:ACI68128.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI68128.1, ECO:0000313|RefSeq:NP_001134591.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:ACI68128.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI68128.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:ACI68128.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001134591.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC EC=2.4.1.141; Evidence={ECO:0000256|ARBA:ARBA00000601};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; BT048327; ACI68128.1; -; mRNA.
DR RefSeq; NP_001134591.1; NM_001141119.2.
DR STRING; 8030.ENSSSAP00000109258; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; 8030-ENSSSAP00000109258; -.
DR GeneID; 100196090; -.
DR KEGG; sasa:100196090; -.
DR OMA; QYKFRPN; -.
DR OrthoDB; 167601at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000077613; Expressed in zone of skin and 15 other cell types or tissues.
DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR039042; Alg13-like.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR PANTHER; PTHR12867; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12867:SF6; N-ACETYLGLUCOSAMINYLDIPHOSPHODOLICHOL N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|EMBL:ACI68128.1,
KW ECO:0000313|RefSeq:NP_001134591.1}.
FT DOMAIN 4..139
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 164 AA; 18069 MW; 3C5A049FEFF91403 CRC64;
MKRVFVTVGT TSFDDLIERV TSPEAVQELK ARGYQHLVLQ VGQGSILPDS DSCHELTLEA
FRFKDSIAEN IKCADLVISH AGAGSCLETL GADKPLLVVV NDKLMDNHQL ELARQLHQDS
HLLYCTPSTL NETLKTMDLA VLSPFLPGQP KHFANFLDRA LGVQ
//
