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   09-APR-2025, entry version 192.
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 + UDP + H(+); 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=3; 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";
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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_001319075.2. [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   PDB; 8SZ3; X-ray; 2.32 A; A/B=1-397.
DR   PDB; 8TIC; X-ray; 2.70 A; A/B/C/D=1-397.
DR   PDB; 8TJC; X-ray; 2.20 A; A/B/C/D=1-397.
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   PDBsum; 8SZ3; -.
DR   PDBsum; 8TIC; -.
DR   PDBsum; 8TJC; -.
DR   AlphaFoldDB; Q9NY97; -.
DR   SMR; Q9NY97; -.
DR   BioGRID; 115919; 600.
DR   IntAct; Q9NY97; 105.
DR   STRING; 9606.ENSP00000305595; -.
DR   ChEMBL; CHEMBL5465363; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   GlyConnect; 1533; 9 N-Linked glycans (6 sites).
DR   GlyCosmos; Q9NY97; 7 sites, 9 glycans.
DR   GlyGen; Q9NY97; 8 sites, 20 N-linked glycans (7 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NY97; -.
DR   PhosphoSitePlus; Q9NY97; -.
DR   BioMuta; B3GNT2; -.
DR   CPTAC; CPTAC-2208; -.
DR   jPOST; Q9NY97; -.
DR   MassIVE; Q9NY97; -.
DR   PaxDb; 9606-ENSP00000305595; -.
DR   PeptideAtlas; Q9NY97; -.
DR   ProteomicsDB; 83198; -. [Q9NY97-1]
DR   ProteomicsDB; 83199; -. [Q9NY97-2]
DR   Pumba; Q9NY97; -.
DR   Antibodypedia; 1107; 205 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   AGR; HGNC:15629; -.
DR   CTD; 10678; -.
DR   DisGeNET; 10678; -.
DR   GeneCards; B3GNT2; -.
DR   HGNC; HGNC:15629; B3GNT2.
DR   HPA; ENSG00000170340; Low tissue specificity.
DR   MalaCards; B3GNT2; -.
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; VSHLNYC; -.
DR   OrthoDB; 2139606at2759; -.
DR   PhylomeDB; Q9NY97; -.
DR   TreeFam; TF318639; -.
DR   BioCyc; MetaCyc:ENSG00000170340-MONOMER; -.
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; 40 hits in 1157 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 191 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0008499; F:N-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase activity; TAS:Reactome.
DR   GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
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:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR   FunFam; 3.90.550.50:FF:000010; Hexosyltransferase; 1.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF25; N-ACETYLLACTOSAMINIDE BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE 2; 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; Proteomics identification;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   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   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:8TJC"
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..356
FT                   /evidence="ECO:0007829|PDB:8TJC"
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
//