GGTA1_PIG
ID GGTA1_PIG Reviewed; 371 AA.
AC P50127;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=N-acetyllactosaminide alpha-1,3-galactosyltransferase;
DE EC=2.4.1.87 {ECO:0000250|UniProtKB:P14769};
DE AltName: Full=UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase;
DE Short=Galactosyltransferase;
GN Name=GGTA1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Yorkshire; TISSUE=Spleen;
RX PubMed=7528726; DOI=10.1007/bf00182319;
RA Strahan K.M., Gu F., Preece A.F., Gustavsson I., Andersson L.,
RA Gustafsson K.;
RT "cDNA sequence and chromosome localization of pig alpha 1,3
RT galactosyltransferase.";
RL Immunogenetics 41:101-105(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Spleen;
RA Sandrin M.S., Dabkowski P.L., Henning M.M., Mouhtouris E., McKenzie I.F.C.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by
CC catalyzing the transfer of a galactose residue, with an alpha-1,3
CC linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide
CC borne by a glycoprotein or a glycolipid. Preferentially glycosylates
CC proteins, can synthesize galactose-alpha(1,3)-galactose on
CC glycoproteins but cannot synthesize the glycolipid called isogloboside
CC 3 (iGb3) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative +
CC H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507,
CC ChEBI:CHEBI:138024; EC=2.4.1.87;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P14769}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P50127-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P50127-2; Sequence=VSP_001806;
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
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DR EMBL; L36152; AAA73558.1; -; mRNA.
DR EMBL; L36535; AAA58775.1; -; mRNA.
DR PIR; I46583; I46583.
DR RefSeq; NP_001309984.1; NM_001323055.1. [P50127-2]
DR RefSeq; NP_001309985.1; NM_001323056.1. [P50127-2]
DR RefSeq; NP_998975.1; NM_213810.3. [P50127-1]
DR RefSeq; XP_005660456.1; XM_005660399.2. [P50127-1]
DR AlphaFoldDB; P50127; -.
DR SMR; P50127; -.
DR STRING; 9823.ENSSSCP00000005915; -.
DR BindingDB; P50127; -.
DR ChEMBL; CHEMBL2942; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR PaxDb; P50127; -.
DR PeptideAtlas; P50127; -.
DR PRIDE; P50127; -.
DR Ensembl; ENSSSCT00000029057; ENSSSCP00000020866; ENSSSCG00000005518. [P50127-2]
DR Ensembl; ENSSSCT00005061820; ENSSSCP00005038235; ENSSSCG00005038675. [P50127-1]
DR Ensembl; ENSSSCT00005061839; ENSSSCP00005038248; ENSSSCG00005038675. [P50127-1]
DR Ensembl; ENSSSCT00005061845; ENSSSCP00005038252; ENSSSCG00005038675. [P50127-2]
DR Ensembl; ENSSSCT00005061930; ENSSSCP00005038317; ENSSSCG00005038675. [P50127-1]
DR Ensembl; ENSSSCT00015052457; ENSSSCP00015020996; ENSSSCG00015038751. [P50127-2]
DR Ensembl; ENSSSCT00025019506; ENSSSCP00025007906; ENSSSCG00025014580. [P50127-2]
DR Ensembl; ENSSSCT00030036905; ENSSSCP00030016893; ENSSSCG00030026383. [P50127-2]
DR Ensembl; ENSSSCT00035107250; ENSSSCP00035046293; ENSSSCG00035077948. [P50127-1]
DR Ensembl; ENSSSCT00035107277; ENSSSCP00035046308; ENSSSCG00035077948. [P50127-2]
DR Ensembl; ENSSSCT00035107350; ENSSSCP00035046347; ENSSSCG00035077948. [P50127-1]
DR Ensembl; ENSSSCT00035107436; ENSSSCP00035046397; ENSSSCG00035077948. [P50127-1]
DR Ensembl; ENSSSCT00035107503; ENSSSCP00035046449; ENSSSCG00035077948. [P50127-1]
DR Ensembl; ENSSSCT00040073279; ENSSSCP00040031357; ENSSSCG00040054081. [P50127-2]
DR Ensembl; ENSSSCT00045065961; ENSSSCP00045046725; ENSSSCG00045038110. [P50127-2]
DR Ensembl; ENSSSCT00050062623; ENSSSCP00050026879; ENSSSCG00050046023. [P50127-2]
DR Ensembl; ENSSSCT00055031386; ENSSSCP00055024988; ENSSSCG00055015900. [P50127-2]
DR Ensembl; ENSSSCT00060011249; ENSSSCP00060004174; ENSSSCG00060008737. [P50127-2]
DR Ensembl; ENSSSCT00065003518; ENSSSCP00065001292; ENSSSCG00065002556. [P50127-1]
DR Ensembl; ENSSSCT00065003524; ENSSSCP00065001295; ENSSSCG00065002556. [P50127-2]
DR Ensembl; ENSSSCT00065003527; ENSSSCP00065001297; ENSSSCG00065002556. [P50127-2]
DR Ensembl; ENSSSCT00065003559; ENSSSCP00065001318; ENSSSCG00065002556. [P50127-1]
DR Ensembl; ENSSSCT00065003564; ENSSSCP00065001321; ENSSSCG00065002556. [P50127-1]
DR Ensembl; ENSSSCT00065003571; ENSSSCP00065001326; ENSSSCG00065002556. [P50127-1]
DR Ensembl; ENSSSCT00070036262; ENSSSCP00070030316; ENSSSCG00070018338. [P50127-1]
DR Ensembl; ENSSSCT00070036264; ENSSSCP00070030318; ENSSSCG00070018338. [P50127-2]
DR Ensembl; ENSSSCT00070036268; ENSSSCP00070030321; ENSSSCG00070018338. [P50127-2]
DR GeneID; 396733; -.
DR KEGG; ssc:396733; -.
DR CTD; 2681; -.
DR eggNOG; ENOG502QW2H; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_1_0_1; -.
DR InParanoid; P50127; -.
DR OrthoDB; 1204439at2759; -.
DR TreeFam; TF330991; -.
DR BRENDA; 2.4.1.87; 6170.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000005518; Expressed in spleen and 43 other tissues.
DR ExpressionAtlas; P50127; baseline and differential.
DR Genevisible; P50127; SS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047276; F:N-acetyllactosaminide 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..371
FT /note="N-acetyllactosaminide alpha-1,3-
FT galactosyltransferase"
FT /id="PRO_0000157300"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..371
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 137..142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228..230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 250..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 362..368
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 27..39
FT /note="SPEGSLFWIYQSK -> R (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001806"
FT CONFLICT 227
FT /note="M -> I (in Ref. 2; AAA58775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 43764 MW; CFC715E8D89993D4 CRC64;
MNVKGRVVLS MLLVSTVMVV FWEYINSPEG SLFWIYQSKN PEVGSSAQRG WWFPSWFNNG
THSYHEEEDA IGNEKEQRKE DNRGELPLVD WFNPEKRPEV VTITRWKAPV VWEGTYNRAV
LDNYYAKQKI TVGLTVFAVG RYIEHYLEEF LISANTYFMV GHKVIFYIMV DDISRMPLIE
LGPLRSFKVF EIKSEKRWQD ISMMRMKTIG EHILAHIQHE VDFLFCMDVD QVFQNNFGVE
TLGQSVAQLQ AWWYKAHPDE FTYERRKESA AYIPFGQGDF YYHAAIFGGT PTQVLNITQE
CFKGILQDKE NDIEAEWHDE SHLNKYFLLN KPTKILSPEY CWDYHIGMSV DIRIVKIAWQ
KKEYNLVRNN I
