B3GN7_HUMAN
ID B3GN7_HUMAN Reviewed; 401 AA.
AC Q8NFL0; B3KWY4; B7WNP0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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:0000269|PubMed:14706853, ECO:0000269|PubMed:17690104};
GN Name=B3GNT7 {ECO:0000303|PubMed:17690104, ECO:0000312|HGNC:HGNC:18811};
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].
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 TISSUE=Thymus;
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 [3]
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 [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=14706853; DOI=10.1016/s0014-5793(03)01440-6;
RA Seko A., Yamashita K.;
RT "Beta1,3-N-acetylglucosaminyltransferase-7 (beta3Gn-T7) acts efficiently on
RT keratan sulfate-related glycans.";
RL FEBS Lett. 556:216-220(2004).
RN [5]
RP FUNCTION, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=17690104; DOI=10.1074/jbc.m703695200;
RA Kitayama K., Hayashida Y., Nishida K., Akama T.O.;
RT "Enzymes responsible for synthesis of corneal keratan sulfate
RT glycosaminoglycans.";
RL J. Biol. Chem. 282:30085-30096(2007).
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 (PubMed:14706853,
CC PubMed:17690104). Involved in biosynthesis of N-linked keratan sulfate
CC proteoglycans in cornea, with an impact on proteoglycan fibril
CC organization and corneal transparency (PubMed:17690104) (By
CC similarity). May play a role in the maintenance of tissue architecture
CC by suppressing cellular motility and invasion (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0J2, ECO:0000269|PubMed:14706853,
CC ECO:0000269|PubMed:17690104}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for
CC Galbeta1->4(SO3->6)GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (L2L2)
CC {ECO:0000269|PubMed:14706853};
CC KM=0.1 mM for
CC Galbeta1->4(SO3->6)GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc
CC (L2L4) {ECO:0000269|PubMed:14706853};
CC KM=0.23 mM for
CC Galbeta1->4GlcNAcbeta1->2(Galbeta1->4GlcNAcbeta1->4)Manalpha1->3[Galb
CC eta1->4GlcNAcbeta1->2(Galbeta1->4GlcNAcbeta1->6)Manalpha1->6]Manbeta1
CC ->4Glc-NAc (tetraGP) {ECO:0000269|PubMed:14706853};
CC Vmax=16.7 pmol/min/mg enzyme toward
CC Galbeta1->4(SO3->6)GlcNAcbeta1->3Galbeta1->4(SO3->6)GlcNAc (L2L2)
CC {ECO:0000269|PubMed:14706853};
CC Vmax=6.5 pmol/min/mg enzyme toward
CC Galbeta1->4(SO3->6)GlcNAcbeta1->3(SO3->6)Galbeta1->4(SO3->6)GlcNAc
CC (L2L4) {ECO:0000269|PubMed:14706853};
CC Vmax=2.9 pmol/min/mg enzyme toward
CC Galbeta1->4GlcNAcbeta1->2(Galbeta1->4GlcNAcbeta1->4)Manalpha1->3[Galb
CC eta1->4GlcNAcbeta1->2(Galbeta1->4GlcNAcbeta1->6)Manalpha1->6]Manbeta1
CC ->4Glc-NAc (tetraGP) {ECO:0000269|PubMed:14706853};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:14706853, ECO:0000305|PubMed:17690104}.
CC -!- INTERACTION:
CC Q8NFL0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-17211590, EBI-13345167;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in corneal epithelial cells.
CC {ECO:0000269|PubMed:17690104}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta 1,3-
CC N-acetylglucosaminyltransferase 7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_562";
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; AF502430; AAM61770.1; -; mRNA.
DR EMBL; AK126207; BAG54296.1; -; mRNA.
DR EMBL; AC017104; AAY24246.1; -; Genomic_DNA.
DR CCDS; CCDS46540.1; -.
DR RefSeq; NP_660279.1; NM_145236.2.
DR AlphaFoldDB; Q8NFL0; -.
DR SMR; Q8NFL0; -.
DR BioGRID; 124994; 29.
DR IntAct; Q8NFL0; 2.
DR STRING; 9606.ENSP00000287590; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8NFL0; 4 sites.
DR iPTMnet; Q8NFL0; -.
DR PhosphoSitePlus; Q8NFL0; -.
DR BioMuta; B3GNT7; -.
DR DMDM; 74723834; -.
DR EPD; Q8NFL0; -.
DR jPOST; Q8NFL0; -.
DR MassIVE; Q8NFL0; -.
DR PaxDb; Q8NFL0; -.
DR PeptideAtlas; Q8NFL0; -.
DR PRIDE; Q8NFL0; -.
DR ProteomicsDB; 73322; -.
DR Antibodypedia; 34416; 93 antibodies from 19 providers.
DR DNASU; 93010; -.
DR Ensembl; ENST00000287590.6; ENSP00000287590.5; ENSG00000156966.7.
DR GeneID; 93010; -.
DR KEGG; hsa:93010; -.
DR MANE-Select; ENST00000287590.6; ENSP00000287590.5; NM_145236.3; NP_660279.1.
DR UCSC; uc002vrs.4; human.
DR CTD; 93010; -.
DR DisGeNET; 93010; -.
DR GeneCards; B3GNT7; -.
DR HGNC; HGNC:18811; B3GNT7.
DR HPA; ENSG00000156966; Tissue enhanced (intestine).
DR MIM; 615313; gene.
DR neXtProt; NX_Q8NFL0; -.
DR OpenTargets; ENSG00000156966; -.
DR PharmGKB; PA38692; -.
DR VEuPathDB; HostDB:ENSG00000156966; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000157606; -.
DR HOGENOM; CLU_036849_5_1_1; -.
DR InParanoid; Q8NFL0; -.
DR OMA; YENHIYG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q8NFL0; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.149; 2681.
DR PathwayCommons; Q8NFL0; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8NFL0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 93010; 14 hits in 1064 CRISPR screens.
DR GenomeRNAi; 93010; -.
DR Pharos; Q8NFL0; Tbio.
DR PRO; PR:Q8NFL0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NFL0; protein.
DR Bgee; ENSG00000156966; Expressed in nasal cavity epithelium and 164 other tissues.
DR Genevisible; Q8NFL0; 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:0008375; F:acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; TAS:Reactome.
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:0018146; P:keratan sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IBA:GO_Central.
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..401
FT /note="UDP-GlcNAc:betaGal beta-1,3-N-
FT acetylglucosaminyltransferase 7"
FT /id="PRO_0000264618"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 35..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 233
FT /note="V -> I (in dbSNP:rs2290130)"
FT /id="VAR_029633"
SQ SEQUENCE 401 AA; 45987 MW; CAF27F0A48DFEE31 CRC64;
MSLWKKTVYR SLCLALALLV AVTVFQRSLT PGQFLQEPPP PTLEPQKAQK PNGQLVNPNN
FWKNPKDVAA PTPMASQGPQ AWDVTTTNCS ANINLTHQPW FQVLEPQFRQ FLFYRHCRYF
PMLLNHPEKC RGDVYLLVVV KSVITQHDRR EAIRQTWGRE RQSAGGGRGA VRTLFLLGTA
SKQEERTHYQ QLLAYEDRLY GDILQWGFLD TFFNLTLKEI HFLKWLDIYC PHVPFIFKGD
DDVFVNPTNL LEFLADRQPQ ENLFVGDVLQ HARPIRRKDN KYYIPGALYG KASYPPYAGG
GGFLMAGSLA RRLHHACDTL ELYPIDDVFL GMCLEVLGVQ PTAHEGFKTF GISRNRNSRM
NKEPCFFRAM LVVHKLLPPE LLAMWGLVHS NLTCSRKLQV L
