ID   GT252_HUMAN             Reviewed;         626 AA.
AC   Q8IYK4; O60327; Q9BZR0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   28-JAN-2026, entry version 174.
DE   RecName: Full=Procollagen galactosyltransferase 2;
DE            EC=2.4.1.50 {ECO:0000269|PubMed:19075007};
DE   AltName: Full=Collagen beta(1-O)galactosyltransferase 2;
DE            Short=ColGalT 2;
DE   AltName: Full=Glycosyltransferase 25 family member 2;
DE   AltName: Full=Hydroxylysine galactosyltransferase 2;
DE   Flags: Precursor;
GN   Name=COLGALT2; Synonyms=C1orf17, GLT25D2, KIAA0584;
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 [MRNA].
RX   PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA   Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA   Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA   Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA   Carpten J.D.;
RT   "Cloning and characterization of 13 novel transcripts and the human RGS8
RT   gene from the 1q25 region encompassing the hereditary prostate cancer
RT   (HPC1) locus.";
RL   Genomics 73:211-222(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Duodenum;
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   [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   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   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] ILE-475.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to
CC       hydroxylysine residues of collagen. {ECO:0000269|PubMed:19075007}.
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] + UDP +
CC         H(+); 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=33.5 uM for UDP-galactose {ECO:0000269|PubMed:19075007};
CC   -!- INTERACTION:
CC       Q8IYK4; Q9BXJ4: C1QTNF3; NbExp=2; IntAct=EBI-10263496, EBI-10697546;
CC       Q8IYK4; P37235: HPCAL1; NbExp=4; IntAct=EBI-10263496, EBI-749311;
CC       Q8IYK4; P04279: SEMG1; NbExp=2; IntAct=EBI-10263496, EBI-953955;
CC       Q8IYK4; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10263496, EBI-10173939;
CC       Q8IYK4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10263496, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and skeletal muscle.
CC       {ECO:0000269|PubMed:19075007}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has no glucosyltransferase activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25510.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF288389; AAG60609.1; -; mRNA.
DR   EMBL; AB011156; BAA25510.1; ALT_INIT; mRNA.
DR   EMBL; AL592299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW91172.1; -; Genomic_DNA.
DR   EMBL; BC035672; AAH35672.1; -; mRNA.
DR   CCDS; CCDS1360.1; -.
DR   PIR; T00343; T00343.
DR   RefSeq; NP_001290349.1; NM_001303420.1.
DR   RefSeq; NP_001290350.1; NM_001303421.1.
DR   RefSeq; NP_055916.1; NM_015101.4.
DR   AlphaFoldDB; Q8IYK4; -.
DR   SMR; Q8IYK4; -.
DR   BioGRID; 116746; 67.
DR   FunCoup; Q8IYK4; 439.
DR   IntAct; Q8IYK4; 57.
DR   MINT; Q8IYK4; -.
DR   STRING; 9606.ENSP00000354960; -.
DR   CAZy; GT25; Glycosyltransferase Family 25.
DR   GlyConnect; 1632; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q8IYK4; 4 sites, 1 glycan.
DR   GlyGen; Q8IYK4; 4 sites, 6 N-linked glycans (2 sites).
DR   iPTMnet; Q8IYK4; -.
DR   PhosphoSitePlus; Q8IYK4; -.
DR   BioMuta; COLGALT2; -.
DR   DMDM; 74750765; -.
DR   jPOST; Q8IYK4; -.
DR   MassIVE; Q8IYK4; -.
DR   PaxDb; 9606-ENSP00000354960; -.
DR   PeptideAtlas; Q8IYK4; -.
DR   ProteomicsDB; 71192; -.
DR   Pumba; Q8IYK4; -.
DR   Antibodypedia; 34449; 150 antibodies from 21 providers.
DR   DNASU; 23127; -.
DR   Ensembl; ENST00000361927.9; ENSP00000354960.4; ENSG00000198756.12.
DR   GeneID; 23127; -.
DR   KEGG; hsa:23127; -.
DR   MANE-Select; ENST00000361927.9; ENSP00000354960.4; NM_015101.4; NP_055916.1.
DR   UCSC; uc001gqr.4; human.
DR   AGR; HGNC:16790; -.
DR   ClinPGx; PA25606; -.
DR   CTD; 23127; -.
DR   DisGeNET; 23127; -.
DR   GeneCards; COLGALT2; -.
DR   HGNC; HGNC:16790; COLGALT2.
DR   HPA; ENSG00000198756; Tissue enhanced (brain).
DR   MIM; 617533; gene.
DR   OpenTargets; ENSG00000198756; -.
DR   VEuPathDB; HostDB:ENSG00000198756; -.
DR   eggNOG; KOG4179; Eukaryota.
DR   GeneTree; ENSGT01030000234558; -.
DR   HOGENOM; CLU_024037_2_0_1; -.
DR   InParanoid; Q8IYK4; -.
DR   OMA; QRVYHYV; -.
DR   OrthoDB; 47375at2759; -.
DR   PAN-GO; Q8IYK4; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q8IYK4; -.
DR   BioCyc; MetaCyc:G66-33947-MONOMER; -.
DR   BRENDA; 2.4.1.50; 2681.
DR   PathwayCommons; Q8IYK4; -.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   SABIO-RK; Q8IYK4; -.
DR   SignaLink; Q8IYK4; -.
DR   SIGNOR; Q8IYK4; -.
DR   Agora; ENSG00000198756; -.
DR   BioGRID-ORCS; 23127; 11 hits in 1160 CRISPR screens.
DR   ChiTaRS; COLGALT2; human.
DR   GenomeRNAi; 23127; -.
DR   Pharos; Q8IYK4; Tbio.
DR   PRO; PR:Q8IYK4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8IYK4; protein.
DR   Bgee; ENSG00000198756; Expressed in tibia and 171 other cell types or tissues.
DR   ExpressionAtlas; Q8IYK4; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0050211; F:procollagen galactosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR   CDD; cd00761; Glyco_tranf_GTA_type; 1.
DR   CDD; cd06532; Glyco_transf_25; 1.
DR   FunFam; 3.90.550.10:FF:000048; Glycosyltransferase 25 family member 1; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR050757; Collagen_mod_GT25.
DR   InterPro; IPR002654; Glyco_trans_25.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10730:SF8; PROCOLLAGEN GALACTOSYLTRANSFERASE 2; 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.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Proteomics identification; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..626
FT                   /note="Procollagen galactosyltransferase 2"
FT                   /id="PRO_0000309541"
FT   REGION          604..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           623..626
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         475
FT                   /note="V -> I (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1670086756)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036978"
SQ   SEQUENCE   626 AA;  72924 MW;  697A76DB73F67539 CRC64;
     MAARPAATLA WSLLLLSSAL LREGCRARFV AERDSEDDGE EPVVFPESPL QSPTVLVAVL
     ARNAAHTLPH FLGCLERLDY PKSRMAIWAA TDHNVDNTTE IFREWLKNVQ RLYHYVEWRP
     MDEPESYPDE IGPKHWPTSR FAHVMKLRQA ALRTAREKWS DYILFIDVDN FLTNPQTLNL
     LIAENKTIVA PMLESRGLYS NFWCGITPKG FYKRTPDYVQ IREWKRTGCF PVPMVHSTFL
     IDLRKEASDK LTFYPPHQDY TWTFDDIIVF AFSSRQAGIQ MYLCNREHYG YLPIPLKPHQ
     TLQEDIENLI HVQIEAMIDR PPMEPSQYVS VVPKYPDKMG FDEIFMINLK RRKDRRDRML
     RTLYEQEIEV KIVEAVDGKA LNTSQLKALN IEMLPGYRDP YSSRPLTRGE IGCFLSHYSV
     WKEVIDRELE KTLVIEDDVR FEHQFKKKLM KLMDNIDQAQ LDWELIYIGR KRMQVKEPEK
     AVPNVANLVE ADYSYWTLGY VISLEGAQKL VGANPFGKML PVDEFLPVMY NKHPVAEYKE
     YYESRDLKAF SAEPLLIYPT HYTGQPGYLS DTETSTIWDN ETVATDWDRT HAWKSRKQSR
     IYSNAKNTEA LPPPTSLDTV PSRDEL
//