ID   G251B_XENLA             Reviewed;         611 AA.
AC   Q5U483;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Procollagen galactosyltransferase 1-B;
DE            EC=2.4.1.50 {ECO:0000250|UniProtKB:Q8NBJ5};
DE   AltName: Full=Collagen beta(1-O)galactosyltransferase 1-B;
DE   AltName: Full=Glycosyltransferase 25 family member 1-B;
DE   AltName: Full=Hydroxylysine galactosyltransferase 1-B;
DE   Flags: Precursor;
GN   Name=colgalt1-b; Synonyms=glt25d1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to
CC       hydroxylysine residues of type I collagen. By acting on collagen
CC       glycosylation, facilitates the formation of collagen triple helix.
CC       {ECO:0000250|UniProtKB:Q8NBJ5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose =
CC         (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) +
CC         UDP; Xref=Rhea:RHEA:12637, Rhea:RHEA-COMP:12752, Rhea:RHEA-
CC         COMP:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:133442, ChEBI:CHEBI:133443; EC=2.4.1.50;
CC         Evidence={ECO:0000250|UniProtKB:Q8NBJ5};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC       {ECO:0000305}.
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DR   EMBL; BC085226; AAH85226.1; -; mRNA.
DR   RefSeq; NP_001088623.1; NM_001095154.1.
DR   AlphaFoldDB; Q5U483; -.
DR   SMR; Q5U483; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   PRIDE; Q5U483; -.
DR   DNASU; 495521; -.
DR   GeneID; 495521; -.
DR   KEGG; xla:495521; -.
DR   CTD; 495521; -.
DR   Xenbase; XB-GENE-6253736; colgalt1.S.
DR   OrthoDB; 931915at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 495521; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0050211; F:procollagen galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:1904028; P:positive regulation of collagen fibril organization; ISS:UniProtKB.
DR   CDD; cd06532; Glyco_transf_25; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002654; Glyco_trans_25.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01755; Glyco_transf_25; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..611
FT                   /note="Procollagen galactosyltransferase 1-B"
FT                   /id="PRO_0000309540"
FT   REGION          576..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           608..611
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        370
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   611 AA;  71607 MW;  63AED42791D52B08 CRC64;
     MSQAGVERLL KGLQILVLVL RLSAGYFPEE RWNPESPFRS PTVLIAVLAR NSEGSLPEVL
     GALDRLHYPK ERISLWVATD HNFDNTSQIL REWLINVQNQ YHHVEWRPQE HPRWFRDEES
     PKHWSHSRYE YVMKLRQAAL TSAREMWADY IFFLDADNLL TNSETLNLLI AENKTVVAPM
     LESRAAYSNF WCGMTTQGYY RRTPAYMPIR RRERQGCFPV PMVHSTFLID LRKEASQQLD
     FYPPHADYTW AFDDIIVFAF SCRQAEVQMF LCNKEIYGYL PVPLRSHSTL LDETDNFLHT
     KLEAMVKGPQ VHPSSFVTIP KKVPDKMSFD EVFLINLKHR QDRRERMKRT LYELQIDFKL
     VDAVYGKMLN QSNVTEMGIK MLPGYKDPYH GRPLTRGEMG CFLSHYNIWK EISERNLEVS
     AVLEDDLRFE IFFKRRLQTL LHDLEIAKLD WDLIYLGRKR MQVDEPEEPV PGVRNLVVSD
     YSYWTLGYLI SLRGARKLLN AEPLGKMLPV DEFLPVMYDK HPISDYSSHF STRDLRAFSV
     EPLLLYPTHY TGDKGYISDT ETSVLWDNVT QPTDWDRAKS RKTHQQEKLR SEALNTPSMG
     SPFDNTARDE L