ID GT251_HUMAN Reviewed; 622 AA. AC Q8NBJ5; Q8NC64; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 20-JUN-2018, entry version 126. DE RecName: Full=Procollagen galactosyltransferase 1; DE EC=2.4.1.50 {ECO:0000269|PubMed:19075007}; DE AltName: Full=Collagen beta(1-O)galactosyltransferase 1; DE Short=ColGalT 1; DE AltName: Full=Glycosyltransferase 25 family member 1; DE AltName: Full=Hydroxylysine galactosyltransferase 1; DE Flags: Precursor; GN Name=COLGALT1; Synonyms=GLT25D1; ORFNames=PSEC0241; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA libraries."; RL DNA Res. 12:117-126(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96 AND ASN-381. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [6] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND RP TISSUE SPECIFICITY. RX PubMed=19075007; DOI=10.1128/MCB.02085-07; RA Schegg B., Huelsmeier A.J., Rutschmann C., Maag C., Hennet T.; RT "Core glycosylation of collagen is initiated by two beta(1- RT O)galactosyltransferases."; RL Mol. Cell. Biol. 29:943-952(2009). RN [7] RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=20470363; DOI=10.1186/1471-2121-11-33; RA Liefhebber J.M., Punt S., Spaan W.J., van Leeuwen H.C.; RT "The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a RT soluble endoplasmic reticulum localized protein."; RL BMC Cell Biol. 11:33-33(2010). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-166; RP ASP-168; PRO-292; ASP-336; ASP-461; ASP-463; ASP-585 AND ASP-587. RX PubMed=22216269; DOI=10.1371/journal.pone.0029390; RA Perrin-Tricaud C., Rutschmann C., Hennet T.; RT "Identification of domains and amino acids essential to the collagen RT galactosyltransferase activity of GLT25D1."; RL PLoS ONE 6:E29390-E29390(2011). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP FUNCTION. RX PubMed=27402836; DOI=10.1074/jbc.M116.723379; RA Baumann S., Hennet T.; RT "Collagen accumulation in osteosarcoma cells lacking GLT25D1 collagen RT galactosyltransferase."; RL J. Biol. Chem. 291:18514-18524(2016). CC -!- FUNCTION: Beta-galactosyltransferase that transfers beta-galactose CC to hydroxylysine residues of type I collagen (PubMed:19075007, CC PubMed:22216269, PubMed:27402836). By acting on collagen CC glycosylation, facilitates the formation of collagen triple helix CC (PubMed:27402836). {ECO:0000269|PubMed:19075007, CC ECO:0000269|PubMed:22216269, ECO:0000269|PubMed:27402836}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + [procollagen]-(2S,5R)- CC 5-hydroxy-L-lysine = UDP + [procollagen]-(2S,5R)-5-O-(beta-D- CC galactosyl)-5-hydroxy-L-lysine. {ECO:0000269|PubMed:19075007}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=18.7 uM for UDP-galactose (at 37 degrees Celsius and pH 7.4) CC {ECO:0000269|PubMed:19075007}; CC KM=29.9 uM for UDP-galactose (at 37 degrees Celsius and pH 7.4) CC {ECO:0000269|PubMed:22216269}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000255|PROSITE-ProRule:PRU10138, CC ECO:0000269|PubMed:20470363}. Note=Colocalized with PLOD3 and CC mannose binding lectin/MBL2. CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in placenta, CC heart, lung and spleen. {ECO:0000269|PubMed:19075007}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:20470363}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family. CC {ECO:0000305}. CC -!- CAUTION: Has no glucosyltransferase activity. {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; AK074941; BAC11307.1; -; mRNA. DR EMBL; AK075541; BAC11684.1; -; mRNA. DR EMBL; AC010618; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84622.1; -; Genomic_DNA. DR EMBL; BC108308; AAI08309.1; -; mRNA. DR CCDS; CCDS12363.1; -. DR RefSeq; NP_078932.2; NM_024656.3. DR UniGene; Hs.418795; -. DR ProteinModelPortal; Q8NBJ5; -. DR BioGrid; 122826; 31. DR IntAct; Q8NBJ5; 14. DR MINT; Q8NBJ5; -. DR STRING; 9606.ENSP00000252599; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR iPTMnet; Q8NBJ5; -. DR PhosphoSitePlus; Q8NBJ5; -. DR BioMuta; COLGALT1; -. DR DMDM; 74715064; -. DR EPD; Q8NBJ5; -. DR MaxQB; Q8NBJ5; -. DR PaxDb; Q8NBJ5; -. DR PeptideAtlas; Q8NBJ5; -. DR PRIDE; Q8NBJ5; -. DR ProteomicsDB; 72778; -. DR TopDownProteomics; Q8NBJ5; -. DR Ensembl; ENST00000252599; ENSP00000252599; ENSG00000130309. DR GeneID; 79709; -. DR KEGG; hsa:79709; -. DR UCSC; uc002nhc.2; human. DR CTD; 79709; -. DR EuPathDB; HostDB:ENSG00000130309.10; -. DR GeneCards; COLGALT1; -. DR HGNC; HGNC:26182; COLGALT1. DR HPA; HPA047821; -. DR MIM; 617531; gene. DR neXtProt; NX_Q8NBJ5; -. DR OpenTargets; ENSG00000130309; -. DR PharmGKB; PA134991138; -. DR eggNOG; KOG4179; Eukaryota. DR eggNOG; ENOG410XQQN; LUCA. DR GeneTree; ENSGT00550000074427; -. DR HOGENOM; HOG000007198; -. DR HOVERGEN; HBG058097; -. DR InParanoid; Q8NBJ5; -. DR KO; K11703; -. DR OMA; MWADYIL; -. DR OrthoDB; EOG091G0SKW; -. DR PhylomeDB; Q8NBJ5; -. DR TreeFam; TF313826; -. DR BioCyc; MetaCyc:ENSG00000130309-MONOMER; -. DR BRENDA; 2.4.1.50; 2681. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR SABIO-RK; Q8NBJ5; -. DR ChiTaRS; COLGALT1; human. DR GenomeRNAi; 79709; -. DR PRO; PR:Q8NBJ5; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000130309; -. DR CleanEx; HS_GLT25D1; -. DR ExpressionAtlas; Q8NBJ5; baseline and differential. DR Genevisible; Q8NBJ5; HS. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0050211; F:procollagen galactosyltransferase activity; IMP:UniProtKB. DR GO; GO:1904028; P:positive regulation of collagen fibril organization; IMP: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 Complete proteome; Endoplasmic reticulum; Glycoprotein; KW Glycosyltransferase; Reference proteome; Signal; Transferase. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 622 Procollagen galactosyltransferase 1. FT /FTId=PRO_0000309536. FT MOTIF 619 622 Endoplasmic reticulum retention motif. FT CARBOHYD 96 96 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 184 184 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 381 381 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT MUTAGEN 166 166 D->A: Loss of galactosyltransferase FT activity; when associated with A-168. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 168 168 D->A: Loss of galactosyltransferase FT activity; when associated with A-166. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 292 292 P->N: Small decrease of FT galactosyltransferase activity. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 336 336 D->S: Small decrease of FT galactosyltransferase activity. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 461 461 D->A: Loss of galactosyltransferase FT activity; when associated with A-463. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 463 463 D->A: Loss of galactosyltransferase FT activity; when associated with A-461. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 585 585 D->A: No effect on galactosyltransferase FT activity; when associated with A-587. FT {ECO:0000269|PubMed:22216269}. FT MUTAGEN 587 587 D->A: No effect on galactosyltransferase FT activity; when associated with A-585. FT {ECO:0000269|PubMed:22216269}. FT CONFLICT 100 100 V -> E (in Ref. 1; BAC11307). FT {ECO:0000305}. FT CONFLICT 220 220 I -> T (in Ref. 1; BAC11307). FT {ECO:0000305}. SQ SEQUENCE 622 AA; 71636 MW; C430974CB1CF5280 CRC64; MAAAPRAGRR RGQPLLALLL LLLAPLPPGA PPGADAYFPE ERWSPESPLQ APRVLIALLA RNAAHALPTT LGALERLRHP RERTALWVAT DHNMDNTSTV LREWLVAVKS LYHSVEWRPA EEPRSYPDEE GPKHWSDSRY EHVMKLRQAA LKSARDMWAD YILFVDADNL ILNPDTLSLL IAENKTVVAP MLDSRAAYSN FWCGMTSQGY YKRTPAYIPI RKRDRRGCFA VPMVHSTFLI DLRKAASRNL AFYPPHPDYT WSFDDIIVFA FSCKQAEVQM YVCNKEEYGF LPVPLRAHST LQDEAESFMH VQLEVMVKHP PAEPSRFISA PTKTPDKMGF DEVFMINLRR RQDRRERMLR ALQAQEIECR LVEAVDGKAM NTSQVEALGI QMLPGYRDPY HGRPLTKGEL GCFLSHYNIW KEVVDRGLQK SLVFEDDLRF EIFFKRRLMN LMRDVEREGL DWDLIYVGRK RMQVEHPEKA VPRVRNLVEA DYSYWTLAYV ISLQGARKLL AAEPLSKMLP VDEFLPVMFD KHPVSEYKAH FSLRNLHAFS VEPLLIYPTH YTGDDGYVSD TETSVVWNNE HVKTDWDRAK SQKMREQQAL SREAKNSDVL QSPLDSAARD EL //