B3GN8_MOUSE
ID B3GN8_MOUSE Reviewed; 389 AA.
AC Q8R3I9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8;
DE Short=BGnT-8;
DE Short=Beta-1,3-Gn-T8;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 8;
DE Short=Beta3Gn-T8;
DE EC=2.4.1.-;
GN Name=B3gnt8 {ECO:0000312|MGI:MGI:2385269};
GN Synonyms=B3galt7 {ECO:0000312|MGI:MGI:2385269};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAC31246.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31246.1}, and
RC NOD {ECO:0000312|EMBL:BAE32443.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE32443.1}, and
RC Thymus {ECO:0000312|EMBL:BAC31246.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH25206.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH25206.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH25206.1};
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 [3]
RP INTERACTION WITH B3GNT2.
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).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in
CC the elongation of specific branch structures of multiantennary N-
CC glycans. Has strong activity towards tetraantennary N-glycans and 2,6
CC triantennary glycans (By similarity). {ECO:0000250|UniProtKB:Q7Z7M8}.
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with B3GNT2; this interaction greatly increases
CC B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity.
CC {ECO:0000269|PubMed:18826941}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NY97}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9NY97}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
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DR EMBL; AK042388; BAC31246.1; -; mRNA.
DR EMBL; AK154220; BAE32443.1; -; mRNA.
DR EMBL; AK154901; BAE32912.1; -; mRNA.
DR EMBL; BC025206; AAH25206.1; -; mRNA.
DR CCDS; CCDS20989.1; -.
DR RefSeq; NP_001031817.1; NM_001036740.2.
DR RefSeq; NP_666296.1; NM_146184.4.
DR RefSeq; XP_006539916.1; XM_006539853.3.
DR AlphaFoldDB; Q8R3I9; -.
DR SMR; Q8R3I9; -.
DR IntAct; Q8R3I9; 2.
DR STRING; 10090.ENSMUSP00000092277; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8R3I9; 2 sites.
DR PhosphoSitePlus; Q8R3I9; -.
DR MaxQB; Q8R3I9; -.
DR PaxDb; Q8R3I9; -.
DR PRIDE; Q8R3I9; -.
DR ProteomicsDB; 277168; -.
DR Antibodypedia; 70706; 11 antibodies from 8 providers.
DR DNASU; 232984; -.
DR Ensembl; ENSMUST00000076034; ENSMUSP00000092277; ENSMUSG00000059479.
DR Ensembl; ENSMUST00000206940; ENSMUSP00000145797; ENSMUSG00000059479.
DR GeneID; 232984; -.
DR KEGG; mmu:232984; -.
DR UCSC; uc009ftg.1; mouse.
DR CTD; 374907; -.
DR MGI; MGI:2385269; B3gnt8.
DR VEuPathDB; HostDB:ENSMUSG00000059479; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161895; -.
DR HOGENOM; CLU_036849_5_0_1; -.
DR InParanoid; Q8R3I9; -.
DR OMA; WESHRYS; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q8R3I9; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 232984; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q8R3I9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R3I9; protein.
DR Bgee; ENSMUSG00000059479; Expressed in lumbar dorsal root ganglion and 91 other tissues.
DR ExpressionAtlas; Q8R3I9; baseline and differential.
DR Genevisible; Q8R3I9; MM.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; ISS:HGNC-UCL.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="UDP-GlcNAc:betaGal beta-1,3-N-
FT acetylglucosaminyltransferase 8"
FT /id="PRO_0000306382"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..389
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 389 AA; 43370 MW; 62ACD86829600D1C CRC64;
MRCRKCQLCL SALLTLLGLK VYIEWTSESW LKKAEPRGAL PSPTPPNAEP TLPTNLSARL
GQTGPLSSAY WNQQQRQLGV LPSTDCQTWG TVAASEILDF ILYPQELRRF LLSAACRSFP
LWLPAGEGSP VASCSDKDVP YLLLAVKSEP GHFAARQAVR ETWGSPVAGT RLLFLLGSPL
GMGGPDLRSL VTWESRRYGD LLLWDFLDVP YNRTLKDLLL LTWLSHHCPD VNFVLQVQDD
AFVHIPALLE HLQTLPPTWA RSLYLGEIFT QAKPLRKPGG PFYVPKTFFE GDYPAYASGG
GYVISGRLAP WLLQAAARVA PFPFDDVYTG FCFRALGLAP RAHPGFLTAW PAERTRDPCA
VRGLLLVHPV SPQDTIWLWR HLWVPELQC
