C1GLT_RAT
ID C1GLT_RAT Reviewed; 363 AA.
AC Q9JJ05;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE AltName: Full=Core 1 O-glycan T-synthase;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1;
DE Short=C1GalT1;
DE Short=Core 1 beta3-Gal-T1;
GN Name=C1galt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11677243; DOI=10.1074/jbc.m109060200;
RA Ju T., Brewer K., D'Souza A., Cummings R.D., Canfield W.M.;
RT "Cloning and expression of human core 1 beta1,3-galactosyltransferase.";
RL J. Biol. Chem. 277:178-186(2002).
RN [2]
RP PROTEIN SEQUENCE OF 2-21 AND 186-196, FUNCTION, COFACTOR, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=11673471; DOI=10.1074/jbc.m109056200;
RA Ju T., Cummings R.D., Canfield W.M.;
RT "Purification, characterization, and subunit structure of rat core 1
RT Beta1,3-galactosyltransferase.";
RL J. Biol. Chem. 277:169-177(2002).
CC -!- FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-
CC beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many
CC extended O-glycans in glycoproteins. Plays a central role in many
CC processes, such as angiogenesis, thrombopoiesis and kidney homeostasis
CC development. {ECO:0000269|PubMed:11673471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000250|UniProtKB:Q9NS00};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11673471};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=630 uM for UDP-Gal {ECO:0000269|PubMed:11673471};
CC Vmax=206 umol/h/mg enzyme {ECO:0000269|PubMed:11673471};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with the C1GALT1C1
CC chaperone; required for galactosyltransferase activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11673471}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:11673471}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
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DR EMBL; AF157963; AAF81983.1; -; mRNA.
DR RefSeq; NP_075239.1; NM_022950.1.
DR AlphaFoldDB; Q9JJ05; -.
DR SMR; Q9JJ05; -.
DR STRING; 10116.ENSRNOP00000010375; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PhosphoSitePlus; Q9JJ05; -.
DR PaxDb; Q9JJ05; -.
DR PRIDE; Q9JJ05; -.
DR GeneID; 65044; -.
DR KEGG; rno:65044; -.
DR UCSC; RGD:621105; rat.
DR CTD; 56913; -.
DR RGD; 621105; C1galt1.
DR VEuPathDB; HostDB:ENSRNOG00000007804; -.
DR eggNOG; KOG2246; Eukaryota.
DR HOGENOM; CLU_035857_0_0_1; -.
DR InParanoid; Q9JJ05; -.
DR PhylomeDB; Q9JJ05; -.
DR TreeFam; TF317293; -.
DR BRENDA; 2.4.1.122; 5301.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR SABIO-RK; Q9JJ05; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9JJ05; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007804; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; Q9JJ05; baseline and differential.
DR Genevisible; Q9JJ05; RN.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0060576; P:intestinal epithelial cell development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
DR InterPro; IPR026842; C1GALT1.
DR InterPro; IPR003378; Fringe-like.
DR PANTHER; PTHR23033:SF13; PTHR23033:SF13; 1.
DR Pfam; PF02434; Fringe; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycosyltransferase; Magnesium;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11673471"
FT CHAIN 2..363
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1"
FT /id="PRO_0000285066"
FT TOPO_DOM 2..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..363
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 41..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJ06"
SQ SEQUENCE 363 AA; 42311 MW; 9482F69FCE069172 CRC64;
MASKSWLNFL TFLCGSAIGF FLCSQLLNIL LQEQADVQPN MLHNDPHARH SDDSGHNHLK
GQMDFNADSS QHKDENTDVA ENLYQKVKVL CWVMTSPQNL EKKAKHVKAT WAQRCNKVLF
MSSEENKDFP TVGLETKEGR EQLYWKTIKA FQYVHDHYLE DADWFMKADD DTYVILDNLR
WLLSKYNPEQ PIYFGRRFKP YVKQGYMSGG AGYVLSKEAL RRFVDAFKTE KCTHSSSIED
LALGRCMEII KVEAGDSRDP TGKETFHPFV PEHHLIKGYL PKTFWYWNYN YYPPVEGPGC
CSDIAVSFHY VDSTTMYELE YLVYHLRPYG YLYRYQPALP ENILKEINQV NKKEDTKIKL
GNP
