GT251_DANRE
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 03-AUG-2022, entry version 96.
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; 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] + 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}.
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; BX469930; CAN87888.1; -; Genomic_DNA.
DR RefSeq; NP_001103992.1; NM_001110522.1.
DR AlphaFoldDB; A5PMF6; -.
DR SMR; A5PMF6; -.
DR STRING; 7955.ENSDARP00000075565; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR PaxDb; A5PMF6; -.
DR PeptideAtlas; A5PMF6; -.
DR PRIDE; A5PMF6; -.
DR Ensembl; ENSDART00000081122; ENSDARP00000075565; ENSDARG00000058270.
DR GeneID; 567859; -.
DR KEGG; dre:567859; -.
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; 931915at2759; -.
DR PhylomeDB; A5PMF6; -.
DR TreeFam; TF313826; -.
DR PRO; PR:A5PMF6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000058270; Expressed in gastrula 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 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..584
FT /note="Basic and acidic 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
