B3GN2_HUMAN
ID B3GN2_HUMAN Reviewed; 397 AA.
AC Q9NY97; Q54AC1; Q9NQQ9; Q9NQR0; Q9NUT9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2;
DE EC=2.4.1.149 {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:9892646};
DE AltName: Full=Beta-1,3-N-acetylglucosaminyltransferase 1;
DE Short=BGnT-1;
DE Short=Beta-1,3-Gn-T1;
DE Short=Beta3Gn-T1;
DE AltName: Full=Beta-1,3-galactosyltransferase 7;
DE Short=Beta-1,3-GalTase 7;
DE Short=Beta3Gal-T7;
DE Short=Beta3GalT7;
DE Short=b3Gal-T7;
DE AltName: Full=Beta-3-Gx-T7;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2;
DE Short=BGnT-2;
DE Short=Beta-1,3-Gn-T2;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 2;
DE Short=Beta3Gn-T2;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7;
GN Name=B3GNT2; Synonyms=B3GALT7, B3GNT1;
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] (ISOFORM 1), FUNCTION, COFACTOR, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Brain;
RX PubMed=9892646; DOI=10.1073/pnas.96.2.406;
RA Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
RA Vliegenthart J.F.G., Berger E.G., Hennet T.;
RT "A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine
RT synthase activity is structurally related to beta-1,3-
RT galactosyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999).
RN [2]
RP SEQUENCE REVISION.
RA Zhou D., Berger E.G., Hennet T.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Amado M., Carneiro F., Clausen H.;
RT "Cloning and expression of two beta-1,3-galactosyltransferases: beta3gal-T5
RT and beta3gal-T6.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Urinary bladder;
RA Gromova I., Gromov P., Celis J.E.;
RT "A novel member of beta-1,3-galactosyltransferase family is down regulated
RT during bladder TCC progression.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=11042166; DOI=10.1074/jbc.m004800200;
RA Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., Yamada Y.,
RA Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., Sasaki K.;
RT "Identification and characterization of three novel beta 1,3-N-
RT acetylglucosaminyltransferases structurally related to the beta 1,3-
RT galactosyltransferase family.";
RL J. Biol. Chem. 276:3498-3507(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-397.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP REVIEW.
RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA Amado M., Almeida R., Schwientek T., Clausen H.;
RT "Identification and characterization of large galactosyltransferase gene
RT families: galactosyltransferases for all functions.";
RL Biochim. Biophys. Acta 1473:35-53(1999).
RN [11]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP INTERACTION WITH B3GNT8, AND MUTAGENESIS OF ASP-245.
RX PubMed=18826941; DOI=10.1074/jbc.m806933200;
RA Seko A., Yamashita K.;
RT "Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by
RT beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-
RT acetyllactosamine chains in differentiated HL-60 cells.";
RL J. Biol. Chem. 283:33094-33100(2008).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=25279697; DOI=10.7554/elife.03943;
RA Praissman J.L., Live D.H., Wang S., Ramiah A., Chinoy Z.S., Boons G.J.,
RA Moremen K.W., Wells L.;
RT "B4GAT1 is the priming enzyme for the LARGE-dependent functional
RT glycosylation of alpha-dystroglycan.";
RL Elife 3:0-0(2014).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
CC synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and
CC elongation of poly-N-acetyllactosamine chains. Shows a marked
CC preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646).
CC Probably constitutes the main polylactosamine synthase.
CC {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:25279697,
CC ECO:0000269|PubMed:9892646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:14389,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:134090; EC=2.4.1.149;
CC Evidence={ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:25279697,
CC ECO:0000269|PubMed:9892646};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9892646};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:25279697}.
CC -!- SUBUNIT: Interacts with B3GNT8; this interaction greatly increases
CC B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity.
CC {ECO:0000269|PubMed:18826941}.
CC -!- INTERACTION:
CC Q9NY97; Q7Z7M8: B3GNT8; NbExp=2; IntAct=EBI-3922389, EBI-20593091;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NY97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY97-2; Sequence=VSP_001791;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11042166}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was indicated as B3Gal-T6 in submitted DNA entries.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-
CC GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_434";
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; AF092051; AAD09764.2; -; mRNA.
DR EMBL; AJ006077; CAB91546.1; -; mRNA.
DR EMBL; AF288208; AAF97253.1; -; mRNA.
DR EMBL; AF288209; AAF97254.1; -; mRNA.
DR EMBL; AB049584; BAB21530.1; -; mRNA.
DR EMBL; BC030579; AAH30579.1; -; mRNA.
DR EMBL; AC093401; AAX93271.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99977.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99978.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99979.1; -; Genomic_DNA.
DR EMBL; BC047933; AAH47933.1; -; mRNA.
DR EMBL; AK002009; BAA92031.1; ALT_INIT; mRNA.
DR CCDS; CCDS1870.1; -. [Q9NY97-1]
DR RefSeq; NP_001306004.1; NM_001319075.1. [Q9NY97-1]
DR RefSeq; NP_006568.2; NM_006577.5. [Q9NY97-1]
DR PDB; 6WMM; X-ray; 1.55 A; A/B=35-397.
DR PDB; 6WMN; X-ray; 2.04 A; A/B/C/D=35-397.
DR PDB; 6WMO; X-ray; 1.85 A; A/B=35-397.
DR PDB; 7JHK; X-ray; 2.34 A; A/B/C/D=45-397.
DR PDB; 7JHL; X-ray; 2.26 A; A/B=45-397.
DR PDB; 7JHM; X-ray; 2.19 A; A/B=45-397.
DR PDB; 7JHN; X-ray; 2.20 A; A=45-397.
DR PDB; 7JHO; X-ray; 1.85 A; A/B=45-397.
DR PDBsum; 6WMM; -.
DR PDBsum; 6WMN; -.
DR PDBsum; 6WMO; -.
DR PDBsum; 7JHK; -.
DR PDBsum; 7JHL; -.
DR PDBsum; 7JHM; -.
DR PDBsum; 7JHN; -.
DR PDBsum; 7JHO; -.
DR AlphaFoldDB; Q9NY97; -.
DR SMR; Q9NY97; -.
DR BioGRID; 115919; 199.
DR IntAct; Q9NY97; 24.
DR STRING; 9606.ENSP00000305595; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyConnect; 1533; 9 N-Linked glycans (6 sites).
DR GlyGen; Q9NY97; 7 sites, 9 N-linked glycans (6 sites).
DR iPTMnet; Q9NY97; -.
DR PhosphoSitePlus; Q9NY97; -.
DR BioMuta; B3GNT2; -.
DR CPTAC; CPTAC-2208; -.
DR EPD; Q9NY97; -.
DR jPOST; Q9NY97; -.
DR MassIVE; Q9NY97; -.
DR MaxQB; Q9NY97; -.
DR PaxDb; Q9NY97; -.
DR PeptideAtlas; Q9NY97; -.
DR PRIDE; Q9NY97; -.
DR ProteomicsDB; 83198; -. [Q9NY97-1]
DR ProteomicsDB; 83199; -. [Q9NY97-2]
DR Antibodypedia; 1107; 187 antibodies from 27 providers.
DR DNASU; 10678; -.
DR Ensembl; ENST00000301998.5; ENSP00000305595.4; ENSG00000170340.11. [Q9NY97-1]
DR Ensembl; ENST00000405767.1; ENSP00000384692.1; ENSG00000170340.11. [Q9NY97-1]
DR GeneID; 10678; -.
DR KEGG; hsa:10678; -.
DR MANE-Select; ENST00000301998.5; ENSP00000305595.4; NM_006577.6; NP_006568.2.
DR UCSC; uc002sbs.4; human. [Q9NY97-1]
DR CTD; 10678; -.
DR DisGeNET; 10678; -.
DR GeneCards; B3GNT2; -.
DR HGNC; HGNC:15629; B3GNT2.
DR HPA; ENSG00000170340; Low tissue specificity.
DR MIM; 605581; gene.
DR neXtProt; NX_Q9NY97; -.
DR OpenTargets; ENSG00000170340; -.
DR PharmGKB; PA25218; -.
DR VEuPathDB; HostDB:ENSG00000170340; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000155345; -.
DR HOGENOM; CLU_036849_5_0_1; -.
DR InParanoid; Q9NY97; -.
DR OMA; DQPDICK; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9NY97; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:ENSG00000170340-MON; -.
DR PathwayCommons; Q9NY97; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9NY97; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10678; 34 hits in 1077 CRISPR screens.
DR ChiTaRS; B3GNT2; human.
DR GeneWiki; B3GNT2; -.
DR GenomeRNAi; 10678; -.
DR Pharos; Q9NY97; Tbio.
DR PRO; PR:Q9NY97; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NY97; protein.
DR Bgee; ENSG00000170340; Expressed in secondary oocyte and 189 other tissues.
DR Genevisible; Q9NY97; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..397
FT /note="N-acetyllactosaminide beta-1,3-N-
FT acetylglucosaminyltransferase 2"
FT /id="PRO_0000219170"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..11
FT /note="MSVGRRRIKLL -> MVSRSLV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_001791"
FT MUTAGEN 245
FT /note="D->A: Loss of enzymatic activity, no loss of B3GNT8-
FT binding."
FT /evidence="ECO:0000269|PubMed:18826941"
FT CONFLICT 11
FT /note="L -> LL (in Ref. 3; CAB91546)"
FT /evidence="ECO:0000305"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7JHO"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:6WMM"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6WMM"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:6WMM"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:6WMM"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 332..342
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:7JHK"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:6WMM"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:6WMM"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:6WMO"
SQ SEQUENCE 397 AA; 46022 MW; B104ECCAE26DC4AC CRC64;
MSVGRRRIKL LGILMMANVF IYFIMEVSKS SSQEKNGKGE VIIPKEKFWK ISTPPEAYWN
REQEKLNRQY NPILSMLTNQ TGEAGRLSNI SHLNYCEPDL RVTSVVTGFN NLPDRFKDFL
LYLRCRNYSL LIDQPDKCAK KPFLLLAIKS LTPHFARRQA IRESWGQESN AGNQTVVRVF
LLGQTPPEDN HPDLSDMLKF ESEKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDTEF
VFKGDDDVFV NTHHILNYLN SLSKTKAKDL FIGDVIHNAG PHRDKKLKYY IPEVVYSGLY
PPYAGGGGFL YSGHLALRLY HITDQVHLYP IDDVYTGMCL QKLGLVPEKH KGFRTFDIEE
KNKNNICSYV DLMLVHSRKP QEMIDIWSQL QSAHLKC
