ID   G251A_XENLA             Reviewed;         611 AA.
AC   A0JPH3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   10-JUN-2026, entry version 68.
DE   RecName: Full=Procollagen galactosyltransferase 1-A;
DE            EC=2.4.1.50 {ECO:0000250|UniProtKB:Q8NBJ5};
DE   AltName: Full=Collagen beta(1-O)galactosyltransferase 1-A;
DE   AltName: Full=Glycosyltransferase 25 family member 1-A;
DE   AltName: Full=Hydroxylysine galactosyltransferase 1-A;
DE   Flags: Precursor;
GN   Name=colgalt1-a; Synonyms=glt25d1-a;
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=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2006) 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] + UDP +
CC         H(+); 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; BC127422; AAI27423.1; -; mRNA.
DR   RefSeq; NP_001096660.1; NM_001103190.1.
DR   AlphaFoldDB; A0JPH3; -.
DR   SMR; A0JPH3; -.
DR   GlyCosmos; A0JPH3; 5 sites, No reported glycans.
DR   DNASU; 100125229; -.
DR   GeneID; 100125229; -.
DR   KEGG; xla:100125229; -.
DR   AGR; Xenbase:XB-GENE-952958; -.
DR   CTD; 100125229; -.
DR   Xenbase; XB-GENE-952958; colgalt1.L.
DR   OrthoDB; 47375at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 100125229; Expressed in internal ear and 19 other cell types or 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; cd00761; Glyco_tranf_GTA_type; 1.
DR   CDD; cd06532; Glyco_transf_25; 1.
DR   FunFam; 3.90.550.10:FF:000048; Glycosyltransferase 25 family member 1; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR050757; Collagen_mod_GT25.
DR   InterPro; IPR002654; Glyco_trans_25.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10730:SF28; PROCOLLAGEN GALACTOSYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR10730; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE/GLYCOSYLTRANSFERASE 25 FAMILY MEMBER; 1.
DR   Pfam; PF13704; Glyco_tranf_2_4; 1.
DR   Pfam; PF01755; Glyco_transf_25; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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-A"
FT                   /id="PRO_0000309539"
FT   REGION          575..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   COMPBIAS        575..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        312
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        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   611 AA;  71389 MW;  64632CE3A3ED9987 CRC64;
     MSQAGVDRLL RGLQLLLLVL RLSAGYFPEE RWNPESSLRN PTVLIALLAR NSEGSLPEVL
     GALDTLHYPK ERISLWVATD HNLDNTTEIL REWLINVQNQ YHHVEWRPQE HPRWFKDEEG
     PKHWSHSRYE YIMKLRQAAL TSAREMWADY IFFLDADNLL TNPETLNLLI AENKTVVAPM
     LDSRAAYSNF WCGMTTQGYY RRTPAYMPIR RRERRGCFPV PMVHSTFLID LRKEASQQLN
     FYPPHADYTW AFDDIIVFAF SCRQADVQMF LCNKEIYGHL PVPLRSHGTL LDEADNFVHT
     KLEVMVKGPP LNLSSFVTIP EKVPDKMSFD EVFLINLKHR QDRRERMKRT LYELQIDYKL
     VDAVYGKTLN QTQVSELGIK MLPDYKDPYH GRPLTRGEMG CFLSHYNIWK EISERNLAVS
     AVFEDDLRFE IYFKRRLQTL LHDLETAKLD WDLIYLGRKR MQVDEPEEPV PGVRNLVVSD
     YSYWTLGYLI SLRGAKKLLN AEPLVKMLPV DEFLPVMYDK HPISDYSSHF SPRDLLAFSV
     EPLLLYPTHY TGDEGYISDT ETSVLWDNLT EPTDWDRAKS RKTQQQEKLR SEALNSPSLG
     SPFDNTARDE L
//