ID   GT251_DANRE             Reviewed;         604 AA.
AC   A5PMF6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   10-JUN-2026, entry version 111.
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;
GN   ORFNames=si:ch211-114l13.7, zgc:110667;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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; BX469930; CAN87888.1; -; Genomic_DNA.
DR   RefSeq; NP_001103992.1; NM_001110522.1.
DR   AlphaFoldDB; A5PMF6; -.
DR   SMR; A5PMF6; -.
DR   FunCoup; A5PMF6; 708.
DR   STRING; 7955.ENSDARP00000075565; -.
DR   GlyCosmos; A5PMF6; 4 sites, No reported glycans.
DR   GlyGen; A5PMF6; 4 sites.
DR   PaxDb; 7955-ENSDARP00000075565; -.
DR   PeptideAtlas; A5PMF6; -.
DR   Ensembl; ENSDART00000081122; ENSDARP00000075565; ENSDARG00000058270.
DR   GeneID; 567859; -.
DR   KEGG; dre:567859; -.
DR   AGR; ZFIN:ZDB-GENE-070424-114; -.
DR   CTD; 567859; -.
DR   ZFIN; ZDB-GENE-070424-114; colgalt1b.
DR   eggNOG; KOG4179; Eukaryota.
DR   GeneTree; ENSGT01030000234558; -.
DR   HOGENOM; CLU_024037_2_0_1; -.
DR   InParanoid; A5PMF6; -.
DR   OMA; MVNNPPL; -.
DR   OrthoDB; 47375at2759; -.
DR   PhylomeDB; A5PMF6; -.
DR   Reactome; R-DRE-1650814; Collagen biosynthesis and modifying enzymes.
DR   PRO; PR:A5PMF6; -.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000058270; Expressed in gastrula 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; 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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..604
FT                   /note="Procollagen galactosyltransferase 1"
FT                   /id="PRO_0000309538"
FT   REGION          570..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           601..604
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        570..580
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   604 AA;  70832 MW;  7D9556D629E4BF7D CRC64;
     MHLLCFFFLL LWTGPARSYF PEERWSPESA LLAPRVLVAL VCRNSAHSLP HVLGAIDRLN
     YPKDRMAVWV ATDHNSDNTT EILREWLVNV QNFYHYVEWR PQDEPSVYEG ESGPKHWTNL
     RYEHVMKLRQ AALETAREMW ADYFMLVDCD NLLTNRDVLW KLMRENKTIV APMLESRAAY
     SNFWCGMTSQ GYYKRTPAYM PIRRQERKGC FAVPMVHSTL LLDLRKEASR QLAFFPPHPD
     YTWAFDDIII FAFSARMAEV QMYICNRETY GYFPVPLRSQ NSLQDEAESF LHSQLEVMVR
     NPPIEPSVYL SLMPKQTDKM GFDEVFMINL LRRSDRRERM LRTLYEQEIA CKIITAVDGK
     ALNASQVEAL GIKMLPGYSD PYHGRPLTKG ELGCFLSHYN IWNEIVDRGL QSSLVIEDDL
     RFEVFFKRRL QNLMQEVQSQ QLDWDLIYIG RKRMQVERPE KSVPRIHSLV EADYSYWTLG
     YVISLRGAQK LLRAEPLKKM LPVDEFLPVM YNKHPIEEYM SHFPQRDLRA FSAEPLLIYP
     THYTGDQGYI SDTETSSVWD NESVLTDWDR ARSRKSREQE ELSSEAQNTD VLQSPLDSTA
     RDEL
//