GT252_MOUSE
ID GT252_MOUSE Reviewed; 625 AA.
AC Q6NVG7; Q8BWD4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Procollagen galactosyltransferase 2;
DE EC=2.4.1.50 {ECO:0000250|UniProtKB:Q8IYK4};
DE AltName: Full=Collagen beta(1-O)galactosyltransferase 2;
DE AltName: Full=Glycosyltransferase 25 family member 2;
DE AltName: Full=Hydroxylysine galactosyltransferase 2;
DE Flags: Precursor;
GN Name=Colgalt2; Synonyms=Glt25d2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to
CC hydroxylysine residues of collagen. {ECO:0000250|UniProtKB:Q8IYK4}.
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:0000250|UniProtKB:Q8IYK4};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC {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; AK052838; BAC35169.1; -; mRNA.
DR EMBL; BC068118; AAH68118.1; -; mRNA.
DR CCDS; CCDS15364.1; -.
DR RefSeq; NP_808424.3; NM_177756.4.
DR AlphaFoldDB; Q6NVG7; -.
DR SMR; Q6NVG7; -.
DR BioGRID; 234612; 2.
DR STRING; 10090.ENSMUSP00000037532; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyGen; Q6NVG7; 4 sites.
DR iPTMnet; Q6NVG7; -.
DR PhosphoSitePlus; Q6NVG7; -.
DR MaxQB; Q6NVG7; -.
DR PaxDb; Q6NVG7; -.
DR PRIDE; Q6NVG7; -.
DR ProteomicsDB; 271110; -.
DR Antibodypedia; 34449; 159 antibodies from 21 providers.
DR DNASU; 269132; -.
DR Ensembl; ENSMUST00000044311; ENSMUSP00000037532; ENSMUSG00000032649.
DR GeneID; 269132; -.
DR KEGG; mmu:269132; -.
DR UCSC; uc007czg.2; mouse.
DR CTD; 23127; -.
DR MGI; MGI:2138232; Colgalt2.
DR VEuPathDB; HostDB:ENSMUSG00000032649; -.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q6NVG7; -.
DR OMA; KRTGCFA; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q6NVG7; -.
DR TreeFam; TF313826; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 269132; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Colgalt2; mouse.
DR PRO; PR:Q6NVG7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6NVG7; protein.
DR Bgee; ENSMUSG00000032649; Expressed in otolith organ and 97 other tissues.
DR ExpressionAtlas; Q6NVG7; baseline and differential.
DR Genevisible; Q6NVG7; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0050211; F:procollagen galactosyltransferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..625
FT /note="Procollagen galactosyltransferase 2"
FT /id="PRO_0000309542"
FT REGION 597..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 622..625
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 398
FT /note="D -> G (in Ref. 1; BAC35169)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="L -> V (in Ref. 2; AAH68118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 72788 MW; CEEAB275790C1F3A CRC64;
MAARLATVAC ALFLLSSALL RLGCRARFAA EPDSDEDGEE TVAFPESPPQ KPTVFVVVLA
RNAAHTLPYF LGCLERLDYP KSRMAIWAAT DHNVDNTTEI LREWLKSVQR LYHYVEWRPM
NEPESYPDEI GPKHWPNSRF SHVMKLRQAA LRTAREKWSD YILFIDVDNF LTNPQTLNLM
IVENKTIVAP MLESRGLYSN FWCGITPQGF YKRTPDYLQI REWKRMGCFP VPMVHSTFLI
DLRKEASDKL AFYPPHQDYT WTFDDIIVFA FSSRQAGIQM YLCNKEHYGY LPIPLKPHQT
LQEDVENLIH VQIEAMIDHP PMEPSQFVSV VPKYPDKMGF DEIFMINLKR RKDRRDRMLR
TLYEQEIEVK IVEAVDGKAL NTSQLKAWNI EMLPGYRDPY SSRPLTRGEI GCFLSHFSVW
KEVIDRELEK TLVIEDDVRF EHQFKRKLMK LMEDIDKAQL DWELIYIGRK RMQVKEPEKA
VPNVVNLVEA DYSYWTLGYA ISLEGAQKLV GADPFGKMLP VDEFLPIMYN KHPVAEYKEY
YESRDLKAFS AEPLLIYPTH YTGQPGYLSD TETSTIWDNE TVATDWDRTH SWKSRKQGHI
RSTAKNTEAL PPPTSLDTVP SRDEL
