B3GN7_RAT
ID B3GN7_RAT Reviewed; 397 AA.
AC Q66H69;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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 (By similarity). May play a role in the maintenance of
CC tissue architecture by suppressing cellular motility and invasion (By
CC similarity). {ECO:0000250|UniProtKB:Q8K0J2,
CC ECO:0000250|UniProtKB:Q8NFL0}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; BC081994; AAH81994.1; -; mRNA.
DR RefSeq; NP_001012134.1; NM_001012134.1.
DR AlphaFoldDB; Q66H69; -.
DR SMR; Q66H69; -.
DR STRING; 10116.ENSRNOP00000024578; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q66H69; 4 sites.
DR PaxDb; Q66H69; -.
DR PRIDE; Q66H69; -.
DR Ensembl; ENSRNOT00000024578; ENSRNOP00000024578; ENSRNOG00000018267.
DR GeneID; 316583; -.
DR KEGG; rno:316583; -.
DR UCSC; RGD:1310580; rat.
DR CTD; 93010; -.
DR RGD; 1310580; B3gnt7.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000157606; -.
DR HOGENOM; CLU_036849_5_1_1; -.
DR InParanoid; Q66H69; -.
DR OMA; YENHIYG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q66H69; -.
DR TreeFam; TF318639; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q66H69; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018267; Expressed in stomach and 19 other tissues.
DR Genevisible; Q66H69; RN.
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; ISS:UniProtKB.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IBA:GO_Central.
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 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_0000264620"
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..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"
SQ SEQUENCE 397 AA; 45447 MW; 522C0203FD5626D5 CRC64;
MSLWKKTLYK SVCLALALLV AVTVFQRSVT PGQFLQDPLP PTLGPPKTGS LVNPNSFWKS
SKDVVAPTPT VPRGPQVWDV VTTNCSINVN LTHQPWFQNL EPHFRQFLAY QHCRYFPMLL
NHPEKCAGDV YLLVVVKSVI TQHDRREVIR QTWGHEWESA GPDRGAVRTL FLLGTASKQE
ERTHYQQLLA YEDRLYGDIL QWDFLDSFFN LTLKEIHFLK WLDIYCPNVP FIFKGDDDVF
VNPTNLLEFL SDRQPQENLF VGDVLKHARP IRKKDNKYYI PAVMYSKATY PPYAGGGGFL
MSGSLARQLH HACDTLELFP IDDVFLGMCL EVLGVKPTGH EGFKTFGISR VRGSRMNKEP
CFYRSMLVVH KLLPAELLAM WDLVHSNLTC SLKFQVL
