ID   GT251_BOVIN             Reviewed;         623 AA.
AC   A5PK45;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Procollagen galactosyltransferase 1;
DE            EC=2.4.1.50 {ECO:0000250|UniProtKB:Q8NBJ5};
DE   AltName: Full=Collagen beta(1-O)galactosyltransferase 1;
DE   AltName: Full=Glycosyltransferase 25 family member 1;
DE   AltName: Full=Hydroxylysine galactosyltransferase 1;
DE   Flags: Precursor;
GN   Name=COLGALT1; Synonyms=GLT25D1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pancreas;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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. Also
CC       involved in the biosynthesis of collagen type IV.
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}. Note=Colocalized with PLOD3 and mannose binding
CC       lectin. {ECO:0000250|UniProtKB:Q8NBJ5}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8NBJ5}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC       {ECO:0000305}.
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DR   EMBL; BC142350; AAI42351.1; -; mRNA.
DR   RefSeq; NP_001092425.1; NM_001098955.1.
DR   AlphaFoldDB; A5PK45; -.
DR   SMR; A5PK45; -.
DR   STRING; 9913.ENSBTAP00000016841; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   PaxDb; A5PK45; -.
DR   PRIDE; A5PK45; -.
DR   Ensembl; ENSBTAT00000016841; ENSBTAP00000016841; ENSBTAG00000012678.
DR   GeneID; 513167; -.
DR   KEGG; bta:513167; -.
DR   CTD; 79709; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012678; -.
DR   VGNC; VGNC:53572; COLGALT1.
DR   eggNOG; KOG4179; Eukaryota.
DR   GeneTree; ENSGT01030000234558; -.
DR   HOGENOM; CLU_024037_2_0_1; -.
DR   InParanoid; A5PK45; -.
DR   OMA; VVWNNEQ; -.
DR   OrthoDB; 931915at2759; -.
DR   TreeFam; TF313826; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000012678; Expressed in granulosa cell and 103 other tissues.
DR   ExpressionAtlas; A5PK45; baseline and differential.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..623
FT                   /note="Procollagen galactosyltransferase 1"
FT                   /id="PRO_0000309535"
FT   REGION          589..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           620..623
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        589..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   623 AA;  71547 MW;  8DE0E6A8A66A8384 CRC64;
     MAAAPRACKG HGRPLPVLLL LLLLALPPLG GPPGAAAYFP EERWSPESPL QAPRVLIALL
     ARNAAHALPA TLGALERLRH PRERTALWVA TDHNADNTSA VLREWLVAVK GLYHSVEWRP
     SEEPRSYPDE EGPKHWSDSR YEHVMKLRQA ALKSARDMWA DYILFVDADN LILNPDTLTL
     LIAENKTVVA PMLDSRAAYS NFWCGMTSQG YYKRTPAYIP IRKRERRGCF AVPMVHSTFL
     IDLRKAASRN LAFYPPHPDY TWSFDDIIVF AFSCKQAEVQ MYVCNKEVYG FLPVPLRSHS
     TLQDEAESFM HVQLEVMVKH PPSEPSRFIS VPTKTPDKMG FDEVFMINLK RRQDRRERML
     RALEEQEIAC RLVEAVDGKA MNTSQVEALG IQMLPGYRDP YHGRPLTKGE LGCFLSHYNI
     WKEVVDRGLQ KSLVFEDDLR FEIFFKRRLM NLMQDVEREG LDWDLIYVGR KRMQVEHPEK
     AVPRVRNLVE ADYSYWTLAY VISLQGARKL LAARPLSKML PVDEFLPVMF DKHPVSEYKA
     HFSPRDLRAF SVEPLLIYPT HYTGDDGYVS DTETSVVWNN EHVKTDWDRA KSQKMREQQA
     LSREAKNSDV LQSPLDSAAR DEL