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 11-DEC-2019, entry version 140. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT 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., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [6] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND TISSUE RP 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, MOTIF, 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 soluble RT 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., Buerckstuemmer T., RA 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., Ayoub D., RA 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). RN [12] RP FUNCTION, INVOLVEMENT IN BSVD3, VARIANTS BSVD3 ARG-151; PRO-154 AND RP ARG-377, AND CHARACTERIZATION OF VARIANT BSVD3 ARG-151. RX PubMed=30412317; DOI=10.1002/ana.25367; RA Miyatake S., Schneeberger S., Koyama N., Yokochi K., Ohmura K., Shiina M., RA Mori H., Koshimizu E., Imagawa E., Uchiyama Y., Mitsuhashi S., Frith M.C., RA Fujita A., Satoh M., Taguri M., Tomono Y., Takahashi K., Doi H., RA Takeuchi H., Nakashima M., Mizuguchi T., Takata A., Miyake N., Saitsu H., RA Tanaka F., Ogata K., Hennet T., Matsumoto N.; RT "Biallelic COLGALT1 variants are associated with cerebral small vessel RT disease."; RL Ann. Neurol. 84:843-853(2018). CC -!- FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to CC hydroxylysine residues of type I collagen (PubMed:19075007, CC PubMed:22216269, PubMed:27402836). By acting on collagen glycosylation, CC facilitates the formation of collagen triple helix (PubMed:27402836). CC Also involved in the biosynthesis of collagen type IV CC (PubMed:30412317). {ECO:0000269|PubMed:19075007, CC ECO:0000269|PubMed:22216269, ECO:0000269|PubMed:27402836, CC ECO:0000269|PubMed:30412317}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5R)-5-hydroxy-L-lysyl-[procollagen] + UDP-alpha-D-galactose = CC (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[procollagen] + 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: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 {ECO:0000255|PROSITE- CC ProRule:PRU10138, ECO:0000269|PubMed:20470363}. Note=Colocalized with CC PLOD3 and mannose binding lectin/MBL2. {ECO:0000269|PubMed:20470363}. CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in placenta, heart, CC lung and spleen. {ECO:0000269|PubMed:19075007}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:20470363}. CC -!- DISEASE: Brain small vessel disease 3 (BSVD3) [MIM:618360]: An CC autosomal recessive form of brain small vessel disease, a CC cerebrovascular disorder with variable manifestations reflecting the CC location and severity of the vascular defect. BSVD3 patients may have CC disease onset in utero or early infancy with subsequent global CC developmental delay, spasticity, and porencephaly on brain imaging. CC Other patients may have normal or mildly delayed development with CC sudden onset of intracranial hemorrhage causing acute neurologic CC deterioration. {ECO:0000269|PubMed:30412317}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. 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 BioGrid; 122826; 37. DR CORUM; Q8NBJ5; -. DR IntAct; Q8NBJ5; 18. DR MINT; Q8NBJ5; -. DR STRING; 9606.ENSP00000252599; -. DR CAZy; GT25; Glycosyltransferase Family 25. DR GlyConnect; 1631; -. DR iPTMnet; Q8NBJ5; -. DR PhosphoSitePlus; Q8NBJ5; -. DR BioMuta; COLGALT1; -. DR DMDM; 74715064; -. DR CPTAC; CPTAC-1298; -. DR CPTAC; CPTAC-208; -. DR CPTAC; CPTAC-209; -. DR EPD; Q8NBJ5; -. DR jPOST; Q8NBJ5; -. DR MassIVE; 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 DisGeNET; 79709; -. DR EuPathDB; HostDB:ENSG00000130309.10; -. DR GeneCards; COLGALT1; -. DR HGNC; HGNC:26182; COLGALT1. DR HPA; HPA047821; -. DR MalaCards; COLGALT1; -. DR MIM; 617531; gene. DR MIM; 618360; phenotype. DR neXtProt; NX_Q8NBJ5; -. DR OpenTargets; ENSG00000130309; -. DR PharmGKB; PA134991138; -. DR eggNOG; KOG4179; Eukaryota. DR eggNOG; ENOG410XQQN; LUCA. DR GeneTree; ENSGT00950000182728; -. DR HOGENOM; HOG000007198; -. DR InParanoid; Q8NBJ5; -. DR KO; K11703; -. DR OMA; PEYSWAF; -. DR OrthoDB; 931915at2759; -. 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 Pharos; Q8NBJ5; Tbio. DR PRO; PR:Q8NBJ5; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8NBJ5; protein. DR Bgee; ENSG00000130309; Expressed in 218 organ(s), highest expression level in heart left ventricle. 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 Disease mutation; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; KW Reference proteome; Signal; Transferase. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..622 FT /note="Procollagen galactosyltransferase 1" FT /id="PRO_0000309536" FT MOTIF 619..622 FT /note="Endoplasmic reticulum retention motif" FT /evidence="ECO:0000269|PubMed:20470363" FT CARBOHYD 96 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 381 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VARIANT 151 FT /note="L -> R (in BSVD3; loss of galactosyltransferase FT activity; dbSNP:rs1478523191)" FT /evidence="ECO:0000269|PubMed:30412317" FT /id="VAR_081752" FT VARIANT 154 FT /note="A -> P (in BSVD3; dbSNP:rs181844791)" FT /evidence="ECO:0000269|PubMed:30412317" FT /id="VAR_081753" FT VARIANT 377 FT /note="G -> R (in BSVD3)" FT /evidence="ECO:0000269|PubMed:30412317" FT /id="VAR_081754" FT MUTAGEN 166 FT /note="D->A: Loss of galactosyltransferase activity; when FT associated with A-168." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 168 FT /note="D->A: Loss of galactosyltransferase activity; when FT associated with A-166." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 292 FT /note="P->N: Small decrease of galactosyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 336 FT /note="D->S: Small decrease of galactosyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 461 FT /note="D->A: Loss of galactosyltransferase activity; when FT associated with A-463." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 463 FT /note="D->A: Loss of galactosyltransferase activity; when FT associated with A-461." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 585 FT /note="D->A: No effect on galactosyltransferase activity; FT when associated with A-587." FT /evidence="ECO:0000269|PubMed:22216269" FT MUTAGEN 587 FT /note="D->A: No effect on galactosyltransferase activity; FT when associated with A-585." FT /evidence="ECO:0000269|PubMed:22216269" FT CONFLICT 100 FT /note="V -> E (in Ref. 1; BAC11307)" FT /evidence="ECO:0000305" FT CONFLICT 220 FT /note="I -> T (in Ref. 1; BAC11307)" FT /evidence="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 //