GT251_MOUSE
ID GT251_MOUSE Reviewed; 617 AA.
AC Q8K297; Q3V3R5; Q6PGL1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK035788; BAE43293.1; -; mRNA.
DR EMBL; BC032165; AAH32165.1; -; mRNA.
DR EMBL; BC056951; AAH56951.1; -; mRNA.
DR CCDS; CCDS22401.1; -.
DR RefSeq; NP_666323.2; NM_146211.3.
DR AlphaFoldDB; Q8K297; -.
DR SMR; Q8K297; -.
DR BioGRID; 231529; 5.
DR IntAct; Q8K297; 2.
DR MINT; Q8K297; -.
DR STRING; 10090.ENSMUSP00000047923; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyConnect; 2606; 2 N-Linked glycans (1 site).
DR GlyGen; Q8K297; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q8K297; -.
DR PhosphoSitePlus; Q8K297; -.
DR EPD; Q8K297; -.
DR MaxQB; Q8K297; -.
DR PaxDb; Q8K297; -.
DR PeptideAtlas; Q8K297; -.
DR PRIDE; Q8K297; -.
DR ProteomicsDB; 271057; -.
DR Antibodypedia; 54139; 48 antibodies from 13 providers.
DR DNASU; 234407; -.
DR Ensembl; ENSMUST00000047903; ENSMUSP00000047923; ENSMUSG00000034807.
DR GeneID; 234407; -.
DR KEGG; mmu:234407; -.
DR UCSC; uc009mee.2; mouse.
DR CTD; 79709; -.
DR MGI; MGI:1924348; Colgalt1.
DR VEuPathDB; HostDB:ENSMUSG00000034807; -.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q8K297; -.
DR OMA; VVWNNEQ; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q8K297; -.
DR TreeFam; TF313826; -.
DR BRENDA; 2.4.1.50; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 234407; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Colgalt1; mouse.
DR PRO; PR:Q8K297; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K297; protein.
DR Bgee; ENSMUSG00000034807; Expressed in vault of skull and 267 other tissues.
DR Genevisible; Q8K297; MM.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..617
FT /note="Procollagen galactosyltransferase 1"
FT /id="PRO_0000309537"
FT REGION 582..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 614..617
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 582..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="S -> L (in Ref. 1; BAE43293)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="D -> A (in Ref. 1; BAE43293)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="T -> P (in Ref. 2; AAH32165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 71061 MW; 828D28E3300D9CC6 CRC64;
MAALPRGSRG LPLLPLLLLL PPLGGPRGAD GYFPEERWSP ESPLQAPRVL IALLARNAAP
ALPATLGALE QLRHPRERTA LWVATDHNTD NTSAILREWL VAVKGLYHSV EWRPAEEPSS
YPDEEGPKHW SDSRYEHVMK LRQAALKSAR DMWADYILFM DIDNLITNPD TLSLLIAENK
TVVAPMLDSR AAYSNFWCGM TSQGYYKRTP AYIPIRKRDR RGCFAVPMVH STFLIDLRKA
ASRNLAFYPT HPDYTWSFDD IIVFAFSCKQ AEVQMYVCNK EVYGFLPVPL RAHSSLQDEA
ESFMHVQLEV MVKHPPVQLS RFISAPRKTS DKMGFDEVFM INLKRRRDRR ERMLRALHEQ
EIDCQLVEAV DGKAMNTSQV EAMGIQMLPG YRDPYHGRPL TKGELGCFLS HYNIWKEVVD
RGLQKSLVFE DDLRFEIFFK RRLMNLMRDV EREGLDWDLI YVGRKRMQVE HPEKAVPHVR
NLVEADYSYW TLAYVISLQG AQKLLAAKPL AKMLPVDEFL PVMFDKHPMS EYKSHFSPRN
LRAFSVEPLL IYPTHYTGDD GYVSDTETSV VWNNEQVKTD WDRAKSQKMR EQQALSREAK
NSDVLQSPLD STARDEL
