GGTA1_RAT
ID GGTA1_RAT Reviewed; 371 AA.
AC Q3L7M0; Q80WF5; Q8K3Z1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 101.
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; Synonyms=Ggta-1;
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] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12626403; DOI=10.1093/glycob/cwg030;
RA Taylor S.G., McKenzie I.F., Sandrin M.S.;
RT "Characterization of the rat alpha(1,3)galactosyltransferase: evidence for
RT two independent genes encoding glycosyltransferases that synthesize
RT Galalpha(1,3)Gal by two separate glycosylation pathways.";
RL Glycobiology 13:327-337(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BDIX;
RA Le Moullac-Vaidye B., Cailleau-Thomas A., Marionneau S., Le Pendu J.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17206613; DOI=10.1002/cne.21233;
RA Fullmer J.M., Riedl M., Williams F.G., Sandrin M., Elde R.;
RT "Enzymes that synthesize the IB4 epitope are not sufficient to impart IB4
RT binding in dorsal root ganglia of rat.";
RL J. Comp. Neurol. 501:70-82(2007).
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 glycosphingolipid
CC isoglobotrihexosylceramide or isogloboside 3 (iGb3).
CC {ECO:0000269|PubMed:12626403, ECO:0000269|PubMed:17206613}.
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
CC {ECO:0000269|PubMed:17206613}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17206613}. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3L7M0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3L7M0-2; Sequence=VSP_054298, VSP_054299;
CC -!- TISSUE SPECIFICITY: Dorsal root ganglia neurons (at protein level).
CC Expressed in the heart, brain, spleen, kidney, lung and liver.
CC {ECO:0000269|PubMed:12626403, ECO:0000269|PubMed:17206613}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
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DR EMBL; AF488784; AAO49077.1; -; mRNA.
DR EMBL; AF520589; AAM74957.1; -; mRNA.
DR EMBL; AABR06022320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06022321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474001; EDL93143.1; -; Genomic_DNA.
DR EMBL; BC166599; AAI66599.1; -; mRNA.
DR RefSeq; NP_663707.1; NM_145674.1. [Q3L7M0-1]
DR RefSeq; XP_006234095.1; XM_006234033.3. [Q3L7M0-1]
DR RefSeq; XP_006234099.1; XM_006234037.3. [Q3L7M0-1]
DR RefSeq; XP_008759922.1; XM_008761700.2. [Q3L7M0-1]
DR RefSeq; XP_008759923.1; XM_008761701.2. [Q3L7M0-1]
DR RefSeq; XP_017446957.1; XM_017591468.1. [Q3L7M0-1]
DR RefSeq; XP_017446958.1; XM_017591469.1. [Q3L7M0-1]
DR AlphaFoldDB; Q3L7M0; -.
DR SMR; Q3L7M0; -.
DR IntAct; Q3L7M0; 1.
DR STRING; 10116.ENSRNOP00000025983; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; Q3L7M0; 1 site.
DR PhosphoSitePlus; Q3L7M0; -.
DR PaxDb; Q3L7M0; -.
DR Ensembl; ENSRNOT00000025983; ENSRNOP00000025983; ENSRNOG00000019179. [Q3L7M0-1]
DR GeneID; 246766; -.
DR KEGG; rno:246766; -.
DR CTD; 2681; -.
DR RGD; 629476; Ggta1.
DR eggNOG; ENOG502QW2H; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_1_0_1; -.
DR InParanoid; Q3L7M0; -.
DR OMA; TVKISWQ; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; Q3L7M0; -.
DR BRENDA; 2.4.1.88; 5301.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q3L7M0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000019179; Expressed in adult mammalian kidney and 18 other tissues.
DR ExpressionAtlas; Q3L7M0; baseline and differential.
DR Genevisible; Q3L7M0; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031985; C:Golgi cisterna; IDA: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: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; 2.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein 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_0000311974"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..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 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12626403"
FT /id="VSP_054298"
FT VAR_SEQ 61
FT /note="R -> SPEGSFLWIYYTKIPEVGESRRQKVWWFSSWFNNG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12626403"
FT /id="VSP_054299"
SQ SEQUENCE 371 AA; 43542 MW; 66AA62E2501841A9 CRC64;
MVTMPQDLHV KVSMSRSKSE TSLLSSRSGS QEKIMNVKGK IILSVLMVST VLVVFWEYVN
RTHSYQEEDI ERAREKGRNG DSIVEPQLWD WFNPKNRPEV LTVTPWKAPI VWEGTYDTAL
LEKYYARQKI TVGLTVFAVG KYIEHYLEDF LESANKYFMV GHRVIFYVMM DDTSRMPAVH
LSPLHSLQVF EIRSEKRWQD ISMMRMKTIG EHILDHIQHE VDFLFCMDVD QVFQDNFGVE
TLGQLVAQLQ AWWYKASPDE FTYERRELSA AYIPFGEGDF YYHAAVFGGT PVHILNLTRE
CFKGILQDKK HDIEAQWHDE SHLNKYFLFN KPTKILSPEY CWDYHIGLPS DIKNVKIAWQ
TKEYNLVRSN V
