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   27-MAR-2024, entry version 162.
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; 166.
DR   CORUM; Q8NBJ5; -.
DR   IntAct; Q8NBJ5; 36.
DR   MINT; Q8NBJ5; -.
DR   STRING; 9606.ENSP00000252599; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   GlyConnect; 1631; 8 N-Linked glycans (3 sites).
DR   GlyCosmos; Q8NBJ5; 3 sites, 8 glycans.
DR   GlyGen; Q8NBJ5; 5 sites, 8 N-linked glycans (3 sites), 2 O-linked glycans (1 site).
DR   iPTMnet; Q8NBJ5; -.
DR   PhosphoSitePlus; Q8NBJ5; -.
DR   SwissPalm; 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; 9606-ENSP00000252599; -.
DR   PeptideAtlas; Q8NBJ5; -.
DR   ProteomicsDB; 72778; -.
DR   Pumba; Q8NBJ5; -.
DR   TopDownProteomics; Q8NBJ5; -.
DR   Antibodypedia; 54139; 86 antibodies from 14 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   AGR; HGNC:26182; -.
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; 5490945at2759; -.
DR   PhylomeDB; Q8NBJ5; -.
DR   TreeFam; TF313826; -.
DR   BioCyc; MetaCyc:ENSG00000130309-MONOMER; -.
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; 13 hits in 1156 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 189 other cell types or tissues.
DR   ExpressionAtlas; Q8NBJ5; baseline and differential.
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; cd00761; Glyco_tranf_GTA_type; 1.
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; Q8NBJ5; HS.
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
//