B3GN7_MOUSE
ID B3GN7_MOUSE Reviewed; 397 AA.
AC Q8K0J2; Q3U3L9; Q3V283; Q6PA02; Q8BJS5; Q8K437;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7;
DE Short=BGnT-7;
DE Short=Beta-1,3-Gn-T7;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 7;
DE Short=Beta3Gn-T7;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8NFL0};
GN Name=B3gnt7;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=ICR; TISSUE=Placenta;
RX PubMed=12061784; DOI=10.1016/s0006-291x(02)00553-3;
RA Kataoka K., Huh N.-H.;
RT "A novel beta1,3-N-acetylglucosaminyltransferase involved in invasion of
RT cancer cells as assayed in vitro.";
RL Biochem. Biophys. Res. Commun. 294:843-848(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, and Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29625490; DOI=10.1167/iovs.17-22716;
RA Littlechild S.L., Young R.D., Caterson B., Yoshida H., Yamazaki M.,
RA Sakimura K., Quantock A.J., Akama T.O.;
RT "Keratan Sulfate Phenotype in the beta-1,3-N-Acetylglucosaminyltransferase-
RT 7-Null Mouse Cornea.";
RL Invest. Ophthalmol. Vis. Sci. 59:1641-1651(2018).
CC -!- FUNCTION: N-acetyl glucosamine (GlcNAc) transferase that catalyzes the
CC transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-
CC reducing terminal galactose (Gal) in the linearly growing chain of
CC N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4
CC galactosyltransferase and CHST6 and CHST1 sulfotransferases to
CC construct and elongate mono- and disulfated disaccharide units
CC [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-
CC sulfoGlcNAcbeta)1->] within keratan sulfate polymer (By similarity).
CC Involved in biosynthesis of N-linked keratan sulfate proteoglycans in
CC cornea, with an impact on proteoglycan fibril organization and corneal
CC transparency (PubMed:29625490). May play a role in the maintenance of
CC tissue architecture by suppressing cellular motility and invasion
CC (PubMed:12061784). {ECO:0000250|UniProtKB:Q8NFL0,
CC ECO:0000269|PubMed:12061784, ECO:0000269|PubMed:29625490}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8NFL0}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in placenta and colon.
CC Moderately expressed in lung, stomach, small intestine and kidney. Very
CC weakly expressed in cerebrum, cerebellum, heart and testis.
CC {ECO:0000269|PubMed:12061784}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate and have normal developmental and reproductive potential. They
CC develop an abnormal corneal ultrastructure characterized by a lack of
CC keratan sulfate proteoglycans that appears to be compensated by
CC increased amount of elongated, branched electron dense chondroitin
CC sulfate/dermatan sulfate proteoglycan filaments.
CC {ECO:0000269|PubMed:29625490}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AF502429; AAM61769.1; -; mRNA.
DR EMBL; AK080081; BAC37824.1; -; mRNA.
DR EMBL; AK131975; BAE20915.1; -; mRNA.
DR EMBL; AK154691; BAE32766.1; -; mRNA.
DR EMBL; BC031187; AAH31187.1; -; mRNA.
DR EMBL; BC060507; AAH60507.1; -; mRNA.
DR CCDS; CCDS35645.1; -.
DR RefSeq; NP_660257.2; NM_145222.2.
DR AlphaFoldDB; Q8K0J2; -.
DR SMR; Q8K0J2; -.
DR STRING; 10090.ENSMUSP00000108931; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8K0J2; 4 sites.
DR PhosphoSitePlus; Q8K0J2; -.
DR MaxQB; Q8K0J2; -.
DR PaxDb; Q8K0J2; -.
DR PRIDE; Q8K0J2; -.
DR ProteomicsDB; 277097; -.
DR Antibodypedia; 34416; 93 antibodies from 19 providers.
DR DNASU; 227327; -.
DR Ensembl; ENSMUST00000113306; ENSMUSP00000108931; ENSMUSG00000079445.
DR GeneID; 227327; -.
DR KEGG; mmu:227327; -.
DR UCSC; uc007bvk.2; mouse.
DR CTD; 93010; -.
DR MGI; MGI:2384394; B3gnt7.
DR VEuPathDB; HostDB:ENSMUSG00000079445; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000157606; -.
DR HOGENOM; CLU_036849_5_1_1; -.
DR InParanoid; Q8K0J2; -.
DR OMA; YENHIYG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q8K0J2; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.149; 3474.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 227327; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8K0J2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K0J2; protein.
DR Bgee; ENSMUSG00000079445; Expressed in left colon and 68 other tissues.
DR ExpressionAtlas; Q8K0J2; baseline and differential.
DR Genevisible; Q8K0J2; 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:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; ISS:MGI.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..397
FT /note="UDP-GlcNAc:betaGal beta-1,3-N-
FT acetylglucosaminyltransferase 7"
FT /id="PRO_0000264619"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 203
FT /note="D -> N (in Ref. 2; BAC37824)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="F -> S (in Ref. 3; AAH31187)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="I -> T (in Ref. 1; AAM61769)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Y -> H (in Ref. 2; BAE20915)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="Q -> R (in Ref. 3; AAH31187/AAH60507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 45379 MW; A6345D03412DD48B CRC64;
MSLWKKTLYK SVCLALALLV AVTVFQRSVT PGQFLQDPLP PTPGPAKTGN LVNPNSFWKS
SKDVAAPTPT VPRGPQVWDV ITTNCSININ LTHQPWFQSL EPHFRQFLAY RHCRYFPMLL
NHPEKCAGDV YMLVVVKSVI TQHDRREVIR QTWGHEWESA GLGRGAVRTL FLLGTASKQE
ERTHYQQLLA YEDRLYADIL QWDFLDSFFN LTLKEIHFLK WLDIYCPNVP FVFKGDDDVF
VNPTNLLEFL SDRQPQENLF VGDVLKHARP IRKKDNKYYI PAVMYGKATY PPYAGGGGFL
MSGSLARQLH HACDTLELFP IDDVFLGMCL EVLGVKPTGH EGFKTFGISR VRSSRMNKEP
CFYRAMLVVH KLLPAELLAM WDLVHSNLTC SVKFQVL
