C1GTA_DANRE
ID C1GTA_DANRE Reviewed; 408 AA.
AC Q08BL3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1-A;
DE EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE AltName: Full=Core 1 O-glycan T-synthase A;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1-A;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1-A;
DE Short=C1GalT1-A;
DE Short=Core 1 beta3-Gal-T1-A;
GN Name=c1galt1a; ORFNames=zgc:153355;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-
CC beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many
CC extended O-glycans in glycoproteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000250|UniProtKB:Q9NS00};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
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DR EMBL; BC124666; AAI24667.1; -; mRNA.
DR RefSeq; NP_001070842.1; NM_001077374.1.
DR AlphaFoldDB; Q08BL3; -.
DR SMR; Q08BL3; -.
DR STRING; 7955.ENSDARP00000053957; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q08BL3; -.
DR GeneID; 557675; -.
DR KEGG; dre:557675; -.
DR CTD; 557675; -.
DR ZFIN; ZDB-GENE-061013-303; c1galt1la.
DR eggNOG; KOG2246; Eukaryota.
DR InParanoid; Q08BL3; -.
DR PhylomeDB; Q08BL3; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q08BL3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
DR InterPro; IPR026842; C1GALT1.
DR InterPro; IPR003378; Fringe-like.
DR PANTHER; PTHR23033:SF44; PTHR23033:SF44; 1.
DR Pfam; PF02434; Fringe; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1-A"
FT /id="PRO_0000285069"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 356..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 46596 MW; 515623072296C2AA CRC64;
MVIMKAGSSR CAFSLGFLVG SCSLYVFLRQ VWFEESFSWQ SNGRSSPSPP ISHEQNSSNL
TWRVEGSALI NLKHPNQPGE DGHIADELFK KVRILCWVMT GPSNLQSKAQ HVKNTWSRHC
NVVLFMSSEE DRSFPTVGLG TGEGRDQLYW KTIRAFHYAL KNHGHEADWF LKADDDTFVV
VDNLRWILSN YTPEQPIYFG KRFKPYTKQG YMSGGAGYVL SKEALRRFVE GFSTKVCTHT
TPVEDLAMGQ CLEKMGVLAG DSRDSLHRET FHPFIPEHHL TGKFSKTFWY WNYCYYPIVE
GPQCCSDLAV SFHYVDPVLM YTLEYYTYHL RPFGYQHRYQ PPVPAVLSLL SQTVKTTTET
QRSEEGAKEK PALTNSVNPR AEEVQTTETS YKITNAAQER NTTHRSAG
