GT251_HUMAN
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 03-AUG-2022, entry version 153.
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-[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: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 variants 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}.
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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 AlphaFoldDB; Q8NBJ5; -.
DR SMR; Q8NBJ5; -.
DR BioGRID; 122826; 86.
DR CORUM; Q8NBJ5; -.
DR IntAct; Q8NBJ5; 33.
DR MINT; Q8NBJ5; -.
DR STRING; 9606.ENSP00000252599; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyConnect; 1631; 8 N-Linked glycans (3 sites).
DR GlyGen; Q8NBJ5; 5 sites, 8 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
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 Antibodypedia; 54139; 48 antibodies from 13 providers.
DR DNASU; 79709; -.
DR Ensembl; ENST00000252599.9; ENSP00000252599.3; ENSG00000130309.12.
DR GeneID; 79709; -.
DR KEGG; hsa:79709; -.
DR MANE-Select; ENST00000252599.9; ENSP00000252599.3; NM_024656.4; NP_078932.2.
DR UCSC; uc002nhc.2; human.
DR CTD; 79709; -.
DR DisGeNET; 79709; -.
DR GeneCards; COLGALT1; -.
DR HGNC; HGNC:26182; COLGALT1.
DR HPA; ENSG00000130309; Low tissue specificity.
DR MalaCards; COLGALT1; -.
DR MIM; 617531; gene.
DR MIM; 618360; phenotype.
DR neXtProt; NX_Q8NBJ5; -.
DR OpenTargets; ENSG00000130309; -.
DR PharmGKB; PA134991138; -.
DR VEuPathDB; HostDB:ENSG00000130309; -.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q8NBJ5; -.
DR OMA; VVWNNEQ; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q8NBJ5; -.
DR TreeFam; TF313826; -.
DR BioCyc; MetaCyc:ENSG00000130309-MON; -.
DR BRENDA; 2.4.1.50; 2681.
DR PathwayCommons; Q8NBJ5; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SABIO-RK; Q8NBJ5; -.
DR SignaLink; Q8NBJ5; -.
DR SIGNOR; Q8NBJ5; -.
DR BioGRID-ORCS; 79709; 10 hits in 1078 CRISPR screens.
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 stromal cell of endometrium and 187 other tissues.
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:0030199; P:collagen fibril organization; TAS:Reactome.
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 variant; 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 REGION 588..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 619..622
FT /note="Endoplasmic reticulum retention motif"
FT /evidence="ECO:0000269|PubMed:20470363"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; dbSNP:rs1568481244)"
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
