B4GN3_MOUSE
ID B4GN3_MOUSE Reviewed; 986 AA.
AC Q6L8S8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase 3;
DE Short=Beta4GalNAc-T3;
DE Short=Beta4GalNAcT3;
DE EC=2.4.1.244;
DE AltName: Full=Beta-1,4-N-acetylgalactosaminyltransferase III;
DE AltName: Full=N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2;
DE Short=NGalNAc-T2;
GN Name=B4galnt3;
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].
RX PubMed=12966086; DOI=10.1074/jbc.m308857200;
RA Sato T., Gotoh M., Kiyohara K., Kameyama A., Kubota T., Kikuchi N.,
RA Ishizuka Y., Iwasaki H., Togayachi A., Kudo T., Ohkura T., Nakanishi H.,
RA Narimatsu H.;
RT "Molecular cloning and characterization of a novel human beta 1,4-N-
RT acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible for the
RT synthesis of N,N'-diacetyllactosediamine, galNAc beta 1-4GlcNAc.";
RL J. Biol. Chem. 278:47534-47544(2003).
CC -!- FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to
CC N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-
CC diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked
CC glycans and probably O-linked glycans. Mediates the N,N'-
CC diacetyllactosediamine formation on gastric mucosa (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-
CC alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-
CC acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:20493, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61631, ChEBI:CHEBI:67138, ChEBI:CHEBI:138027;
CC EC=2.4.1.244;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Localizes to apical Golgi.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta1,4-
CC N-acetylgalactosaminyltransferase III;
CC URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_507";
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DR EMBL; AB114826; BAD02450.1; -; mRNA.
DR CCDS; CCDS20480.1; -.
DR RefSeq; NP_942585.1; NM_198884.1.
DR AlphaFoldDB; Q6L8S8; -.
DR SMR; Q6L8S8; -.
DR STRING; 10090.ENSMUSP00000058253; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR iPTMnet; Q6L8S8; -.
DR PhosphoSitePlus; Q6L8S8; -.
DR PaxDb; Q6L8S8; -.
DR PRIDE; Q6L8S8; -.
DR ProteomicsDB; 277170; -.
DR Antibodypedia; 2483; 82 antibodies from 16 providers.
DR DNASU; 330406; -.
DR Ensembl; ENSMUST00000057283; ENSMUSP00000058253; ENSMUSG00000041372.
DR GeneID; 330406; -.
DR KEGG; mmu:330406; -.
DR UCSC; uc009dmy.1; mouse.
DR CTD; 283358; -.
DR MGI; MGI:3041155; B4galnt3.
DR VEuPathDB; HostDB:ENSMUSG00000041372; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_011195_0_0_1; -.
DR InParanoid; Q6L8S8; -.
DR OMA; VDPHLQF; -.
DR OrthoDB; 339331at2759; -.
DR PhylomeDB; Q6L8S8; -.
DR TreeFam; TF318303; -.
DR BioGRID-ORCS; 330406; 4 hits in 72 CRISPR screens.
DR ChiTaRS; B4galnt3; mouse.
DR PRO; PR:Q6L8S8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6L8S8; protein.
DR Bgee; ENSMUSG00000041372; Expressed in olfactory epithelium and 49 other tissues.
DR ExpressionAtlas; Q6L8S8; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0033842; F:N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF05679; CHGN; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51820; PA14; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..986
FT /note="Beta-1,4-N-acetylgalactosaminyltransferase 3"
FT /id="PRO_0000252369"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..986
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 109..278
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 113509 MW; D4CFB2B6B629A021 CRC64;
MGSPRAALLM LLLRPIKLLR RRFRLLLLLA VVSVGLWTLY LELVASAQAG GNPLNHRYGS
WRELAKALAS RNIPAVDPNL QFYRPQRLSL KDQEIARSRS RNSSYLKWNK PVPWLSEFRG
HANLHVFEDW CGSSIQQLRN NLHFPLYPHI RTTLRKLAVS PKWTNYGLRI FGYLHPFTDG
KIQFAIAADD NAEFWLSRDD QVSGLQLLAS VGKTGKEWTA PGEFGKFQSQ ISKPVSLSAS
LRYYFEVLHK QNDEGTDHVE VAWRRNDPGA KFTIIDSPFL SLFTNETILR MDEVGHIPQT
AASHVGSSNT PPRDEQPPAD MLRPDPRDTL FRVPLIAKSH LRHVLPDCPY KPSYLVDGLP
LQRYQGLRFV HLSFVYPNDY TRLSHMETHN KCFYQESAYD QDRSSFQEYI KMDKPEKHGP
EQPAGLEDGL LEESQYEDVP EEIPTSQDQN TGIQGRKQKT ISTPGLGVTD YHLRKLLARS
QSGPVAPLSK QNSTTAFPTR TSNIPVQRPE KSPVPSRDLS HSDQGARRNL PLIQRARPTG
DRPGKTLEQS QWLNQVESFI AEQRRGDRIE PPTPSRGWRP EEDVVIAADQ EGEVEEEEEG
EDEEEDMSEV FEYVPMFDPV VNWGQTFSAQ NLDFQALRTD WIDLNCNTSG NLLLPEQEAL
EVTRVFLRKL SQRTRGRYQL QRIVNVEKRQ DRLRGGRYFL ELELLDGQRL VRLSEYVSTR
GWRGGDHPGR EDTEARNLQG LVWSPRNRHR HVLNAQDPEP KLCWPQGFSW NHRAVVHFIV
PVKNQARWVQ QFIRDMESLS QVTGDAHFSI IITDYSSEDM DVEMALKRSR LRSYQYLKLS
GNFERSAGLQ AGIDLVKDPH SIIFLCDLHI HFPAGIIDTI RKHCVEGKMA FAPMVMRLHC
GATPQWPEGY WEVNGFGLLG IYKSDLDKIG GMNTKEFRDR WGGEDWELLD RILQAGLEVE
RLSLRNFFHH FHSKRGMWNR RQMKMP
