GT252_HUMAN
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 03-AUG-2022, entry version 158.
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] + 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=33.5 uM for UDP-galactose {ECO:0000269|PubMed:19075007};
CC -!- INTERACTION:
CC Q8IYK4; P37235: HPCAL1; NbExp=4; IntAct=EBI-10263496, EBI-749311;
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_015101.3.
DR AlphaFoldDB; Q8IYK4; -.
DR SMR; Q8IYK4; -.
DR BioGRID; 116746; 65.
DR IntAct; Q8IYK4; 35.
DR MINT; Q8IYK4; -.
DR STRING; 9606.ENSP00000354960; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyConnect; 1632; 1 N-Linked glycan (1 site).
DR GlyGen; Q8IYK4; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8IYK4; -.
DR PhosphoSitePlus; Q8IYK4; -.
DR BioMuta; COLGALT2; -.
DR DMDM; 74750765; -.
DR EPD; Q8IYK4; -.
DR jPOST; Q8IYK4; -.
DR MassIVE; Q8IYK4; -.
DR MaxQB; Q8IYK4; -.
DR PaxDb; Q8IYK4; -.
DR PeptideAtlas; Q8IYK4; -.
DR PRIDE; Q8IYK4; -.
DR ProteomicsDB; 71192; -.
DR Antibodypedia; 34449; 159 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 CTD; 23127; -.
DR DisGeNET; 23127; -.
DR GeneCards; COLGALT2; -.
DR HGNC; HGNC:16790; COLGALT2.
DR HPA; ENSG00000198756; Tissue enriched (brain).
DR MIM; 617533; gene.
DR neXtProt; NX_Q8IYK4; -.
DR OpenTargets; ENSG00000198756; -.
DR PharmGKB; PA25606; -.
DR VEuPathDB; HostDB:ENSG00000198756; -.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q8IYK4; -.
DR OMA; KRTGCFA; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q8IYK4; -.
DR TreeFam; TF313826; -.
DR BioCyc; MetaCyc:G66-33947-MON; -.
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 BioGRID-ORCS; 23127; 11 hits in 1082 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 169 other tissues.
DR ExpressionAtlas; Q8IYK4; baseline and differential.
DR Genevisible; Q8IYK4; HS.
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; 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 Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW 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
FT mutation)"
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
