ID   C1GTB_DANRE             Reviewed;         374 AA.
AC   Q7SYI5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1-B;
DE            EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE   AltName: Full=Core 1 O-glycan T-synthase B;
DE   AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1-B;
DE   AltName: Full=Core 1 beta1,3-galactosyltransferase 1-B;
DE            Short=C1GalT1-B;
DE            Short=Core 1 beta3-Gal-T1-B;
GN   Name=c1galt1b; Synonyms=c1galt1; ORFNames=zgc:66485;
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   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC054714; AAH54714.1; -; mRNA.
DR   RefSeq; NP_956345.1; NM_200051.1.
DR   AlphaFoldDB; Q7SYI5; -.
DR   SMR; Q7SYI5; -.
DR   STRING; 7955.ENSDARP00000111673; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q7SYI5; -.
DR   GeneID; 337131; -.
DR   KEGG; dre:337131; -.
DR   CTD; 337131; -.
DR   ZFIN; ZDB-GENE-030131-9075; c1galt1lb.
DR   eggNOG; KOG2246; Eukaryota.
DR   InParanoid; Q7SYI5; -.
DR   OrthoDB; 1407357at2759; -.
DR   PhylomeDB; Q7SYI5; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q7SYI5; -.
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:SF9; PTHR23033:SF9; 1.
DR   Pfam; PF02434; Fringe; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycosyltransferase; Magnesium; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..374
FT                   /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT                   galactosyltransferase 1-B"
FT                   /id="PRO_0000285068"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..374
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  43454 MW;  06D90B2092CE7618 CRC64;
     MKALGARSAF YVGFLVGTCS LYLLLRQAGF TRDSGSREPG THDKTLLEML EEENKNWKKE
     RSALFNLNHP HHTGEDGALA DSLYKRVRIL CWVMTGPDNL EKKARHVKAT WSRHCNIVVF
     ISSVDNPDFP TVGLNTKEGR DQLYWKTIRA FHYVMEKHSD EADWFLKADD DTYVIVDNLR
     WILARHSPED PVYFGRRFKP YVKQGYMSGG AGYVLSKEAL RRFVEGFRTK VCTHTTSVED
     LAMGQCMEKI GVKAGDSRDT MQRETFHPFV PESHLTGTFP KTFWYWNYCY YPIVQGPQCC
     SDLAVSFHYV DASHMYLLEY YTYHLRAFGY KYRYQPPEPN VKAPEKVETR VLEQKDKVEA
     QEEENQSPEL NDKL