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   24-JAN-2024, entry version 144.
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,
RC   Spleen, 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; 6.
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   GlyCosmos; Q8K297; 3 sites, 2 glycans.
DR   GlyGen; Q8K297; 4 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K297; -.
DR   PhosphoSitePlus; Q8K297; -.
DR   SwissPalm; Q8K297; -.
DR   EPD; Q8K297; -.
DR   MaxQB; Q8K297; -.
DR   PaxDb; 10090-ENSMUSP00000047923; -.
DR   PeptideAtlas; Q8K297; -.
DR   ProteomicsDB; 271057; -.
DR   Pumba; Q8K297; -.
DR   Antibodypedia; 54139; 86 antibodies from 14 providers.
DR   DNASU; 234407; -.
DR   Ensembl; ENSMUST00000047903.10; ENSMUSP00000047923.9; ENSMUSG00000034807.10.
DR   GeneID; 234407; -.
DR   KEGG; mmu:234407; -.
DR   UCSC; uc009mee.2; mouse.
DR   AGR; MGI:1924348; -.
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; 5490945at2759; -.
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; 2 hits in 77 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 271 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   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.
DR   Genevisible; Q8K297; MM.
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
//