ID B3GN3_HUMAN Reviewed; 372 AA. AC Q9Y2A9; B2RAS4; Q6NWU9; Q6NXU9; Q8WWR6; Q9C0J2; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 11-NOV-2015, entry version 134. DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3; DE EC=2.4.1.149 {ECO:0000269|PubMed:11042166}; DE AltName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase; DE EC=2.4.1.146 {ECO:0000269|PubMed:11439191}; DE AltName: Full=Beta-1,3-galactosyltransferase 8; DE Short=Beta-1,3-GalTase 8; DE Short=Beta3Gal-T8; DE Short=Beta3GalT8; DE Short=b3Gal-T8; DE AltName: Full=Beta-3-Gx-T8; DE AltName: Full=Core 1 extending beta-1,3-N-acetylglucosaminyltransferase {ECO:0000303|PubMed:11439191}; DE AltName: Full=Core1-beta3GlcNAcT {ECO:0000303|PubMed:11439191}; DE AltName: Full=Transmembrane protein 3; DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 8; DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3; DE Short=BGnT-3; DE Short=Beta-1,3-Gn-T3; DE Short=Beta-1,3-N-acetylglucosaminyltransferase 3; DE Short=Beta3Gn-T3; DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 8; GN Name=B3GNT3; Synonyms=B3GALT8, TMEM3; ORFNames=UNQ637/PRO1266; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-328. RX PubMed=10072769; DOI=10.1016/S0378-1119(99)00004-9; RA Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.; RT "Selection of cDNAs encoding putative type II membrane proteins on the RT cell surface from a human full-length cDNA bank."; RL Gene 228:161-167(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND VARIANT RP HIS-328. RX PubMed=11439191; DOI=10.1016/S0092-8674(01)00394-4; RA Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G., RA Rabuka D., Hindsgaul O., Marth J.D., Lowe J.B., Fukuda M.; RT "Novel sulfated lymphocyte homing receptors and their control by a RT Core1 extension beta 1,3-N-acetylglucosaminyltransferase."; RL Cell 105:957-969(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Gastric mucosa; RX PubMed=11042166; DOI=10.1074/jbc.M004800200; RA Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., RA Yamada Y., Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., RA 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-328. RA Jensen M.A., Bennett E.P.; RT "Cloning of a new member of the beta 1,3 galactosyltransferase family, RT b1,3Gal-T6."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-328. RA Bennett E.P.; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-328. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-328. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(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 RT gene families: galactosyltransferases for all functions."; RL Biochim. Biophys. Acta 1473:35-53(1999). RN [11] RP VARIANT PHE-317. RX PubMed=25787250; DOI=10.1073/pnas.1503696112; RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W., RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., RA Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T., RA Bjoerklund P., Lifton R.P.; RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in RT insulin-producing adenomas."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015). CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the CC synthesis of poly-N-acetyllactosamine. Has activity for type 2 CC oligosaccharides (PubMed:11042166). Also acts as a core1-1,3-N- CC acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6- CC sulfo sialyl Lewis x on extended core1 O-glycans CC (PubMed:11439191). {ECO:0000269|PubMed:11042166, CC ECO:0000269|PubMed:11439191}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D- CC galactosyl-(1->3)-(N-acetyl-D-glucosaminyl-(1->6))-N-acetyl-D- CC galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta- CC D-galactosyl-(1->3)-(N-acetyl-D-glucosaminyl-(1->6))-N-acetyl-D- CC galactosaminyl-R. {ECO:0000269|PubMed:11439191}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D- CC galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta- CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-D- CC glucosaminyl-R. {ECO:0000269|PubMed:11042166}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; CC Single-pass type II membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in colon, jejunum, stomach, CC esophagus, placenta and trachea. {ECO:0000269|PubMed:11042166}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC82374.1; Type=Frameshift; Positions=194, 196, 202, 204, 209, 215; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database; CC URL="http://jcggdb.jp/rcmg/ggdb/Homolog?cat=symbol&symbol=B3GNT3"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP- CC GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_536"; 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; AB015630; BAA76497.1; -; mRNA. DR EMBL; AF293973; AAK00849.1; -; mRNA. DR EMBL; AB049585; BAB21531.1; -; mRNA. DR EMBL; AJ130847; CAC45044.1; -; mRNA. DR EMBL; AJ278961; CAC82374.1; ALT_FRAME; mRNA. DR EMBL; AY358955; AAQ89314.1; -; mRNA. DR EMBL; AK314323; BAG36971.1; -; mRNA. DR EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC066876; AAH66876.1; -; mRNA. DR EMBL; BC067423; AAH67423.1; -; mRNA. DR CCDS; CCDS12364.1; -. DR RefSeq; NP_055071.2; NM_014256.3. DR RefSeq; XP_011525928.1; XM_011527626.1. DR RefSeq; XP_011525929.1; XM_011527627.1. DR UniGene; Hs.657825; -. DR UniGene; Hs.69009; -. DR ProteinModelPortal; Q9Y2A9; -. DR BioGrid; 115614; 22. DR STRING; 9606.ENSP00000321874; -. DR CAZy; GT31; Glycosyltransferase Family 31. DR PhosphoSite; Q9Y2A9; -. DR BioMuta; B3GNT3; -. DR DMDM; 311033352; -. DR MaxQB; Q9Y2A9; -. DR PaxDb; Q9Y2A9; -. DR PRIDE; Q9Y2A9; -. DR DNASU; 10331; -. DR Ensembl; ENST00000318683; ENSP00000321874; ENSG00000179913. DR Ensembl; ENST00000595387; ENSP00000472638; ENSG00000179913. DR GeneID; 10331; -. DR KEGG; hsa:10331; -. DR UCSC; uc002nhl.1; human. DR CTD; 10331; -. DR GeneCards; B3GNT3; -. DR HGNC; HGNC:13528; B3GNT3. DR HPA; HPA024298; -. DR MIM; 605863; gene. DR neXtProt; NX_Q9Y2A9; -. DR PharmGKB; PA25219; -. DR eggNOG; KOG2287; Eukaryota. DR eggNOG; ENOG410ZZ1B; LUCA. DR GeneTree; ENSGT00760000118879; -. DR HOGENOM; HOG000232195; -. DR HOVERGEN; HBG050653; -. DR InParanoid; Q9Y2A9; -. DR KO; K07970; -. DR OMA; YKHCRDF; -. DR PhylomeDB; Q9Y2A9; -. DR TreeFam; TF318639; -. DR BioCyc; MetaCyc:ENSG00000179913-MONOMER; -. DR BRENDA; 2.4.1.146; 2681. DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis. DR Reactome; R-HSA-913709; O-linked glycosylation of mucins. DR UniPathway; UPA00378; -. DR GeneWiki; Beta-1,3-N-acetylglucosaminyltransferase_3; -. DR GenomeRNAi; 10331; -. DR NextBio; 39169; -. DR PRO; PR:Q9Y2A9; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; Q9Y2A9; -. DR CleanEx; HS_B3GNT3; -. DR ExpressionAtlas; Q9Y2A9; baseline and differential. DR Genevisible; Q9Y2A9; HS. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008378; F:galactosyltransferase activity; IEA:InterPro. DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome. DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome. DR GO; GO:0042339; P:keratan sulfate metabolic 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:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0006493; P:protein O-linked glycosylation; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR InterPro; IPR002659; Glyco_trans_31. DR PANTHER; PTHR11214; PTHR11214; 1. DR Pfam; PF01762; Galactosyl_T; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Membrane; Polymorphism; Reference proteome; Signal-anchor; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 372 N-acetyllactosaminide beta-1,3-N- FT acetylglucosaminyltransferase 3. FT /FTId=PRO_0000219172. FT TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 11 31 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 32 372 Lumenal. {ECO:0000255}. FT CARBOHYD 64 64 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 184 184 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 202 202 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 362 362 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 367 367 N-linked (GlcNAc...). {ECO:0000255}. FT VARIANT 317 317 I -> F. {ECO:0000269|PubMed:25787250}. FT /FTId=VAR_074178. FT VARIANT 328 328 R -> H (in dbSNP:rs36686). FT {ECO:0000269|PubMed:10072769, FT ECO:0000269|PubMed:11439191, FT ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.4, ECO:0000269|Ref.5}. FT /FTId=VAR_022644. FT CONFLICT 89 89 C -> Y (in Ref. 9; AAH66876). FT {ECO:0000305}. FT CONFLICT 355 355 W -> R (in Ref. 9; AAH67423). FT {ECO:0000305}. SQ SEQUENCE 372 AA; 42534 MW; A6E3FE88B2F00F10 CRC64; MKYLRHRRPN ATLILAIGAF TLLLFSLLVS PPTCKVQEQP PAIPEALAWP TPPTRPAPAP CHANTSMVTH PDFATQPQHV QNFLLYRHCR HFPLLQDVPP SKCAQPVFLL LVIKSSPSNY VRRELLRRTW GRERKVRGLQ LRLLFLVGTA SNPHEARKVN RLLELEAQTH GDILQWDFHD SFFNLTLKQV LFLQWQETRC ANASFVLNGD DDVFAHTDNM VFYLQDHDPG RHLFVGQLIQ NVGPIRAFWS KYYVPEVVTQ NERYPPYCGG GGFLLSRFTA AALRRAAHVL DIFPIDDVFL GMCLELEGLK PASHSGIRTS GVRAPSQRLS SFDPCFYRDL LLVHRFLPYE MLLMWDALNQ PNLTCGNQTQ IY //