B4GN4_MOUSE
ID B4GN4_MOUSE Reviewed; 1034 AA.
AC Q766D5; Q8CHV2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1;
DE Short=NGalNAc-T1;
DE EC=2.4.1.244;
DE AltName: Full=Beta-1,4-N-acetylgalactosaminyltransferase IV;
DE Short=Beta4GalNAc-T4;
DE Short=Beta4GalNAcT4;
GN Name=B4galnt4;
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] (ISOFORM 1).
RX PubMed=15044014; DOI=10.1016/s0014-5793(04)00219-4;
RA Gotoh M., Sato T., Kiyohara K., Kameyama A., Kikuchi N., Kwon Y.-D.,
RA Ishizuka Y., Iwai T., Nakanishi H., Narimatsu H.;
RT "Molecular cloning and characterization of beta1,4-N-
RT acetylgalactosaminyltransferases IV synthesizing N,N'-
RT diacetyllactosediamine.";
RL FEBS Lett. 562:134-140(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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: 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. {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
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q766D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q766D5-2; Sequence=VSP_020917;
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 IV;
CC URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_508";
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DR EMBL; AB114827; BAD15101.1; -; mRNA.
DR EMBL; BC038881; AAH38881.1; -; mRNA.
DR CCDS; CCDS21998.1; -. [Q766D5-1]
DR RefSeq; NP_808565.2; NM_177897.3. [Q766D5-1]
DR AlphaFoldDB; Q766D5; -.
DR SMR; Q766D5; -.
DR STRING; 10090.ENSMUSP00000039758; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q766D5; 2 sites.
DR iPTMnet; Q766D5; -.
DR PhosphoSitePlus; Q766D5; -.
DR EPD; Q766D5; -.
DR MaxQB; Q766D5; -.
DR PaxDb; Q766D5; -.
DR PeptideAtlas; Q766D5; -.
DR PRIDE; Q766D5; -.
DR ProteomicsDB; 273524; -. [Q766D5-1]
DR ProteomicsDB; 273525; -. [Q766D5-2]
DR Antibodypedia; 64249; 5 antibodies from 5 providers.
DR DNASU; 330671; -.
DR Ensembl; ENSMUST00000048002; ENSMUSP00000039758; ENSMUSG00000055629. [Q766D5-1]
DR GeneID; 330671; -.
DR KEGG; mmu:330671; -.
DR UCSC; uc009kje.1; mouse. [Q766D5-1]
DR UCSC; uc009kjg.1; mouse. [Q766D5-2]
DR CTD; 338707; -.
DR MGI; MGI:2652891; B4galnt4.
DR VEuPathDB; HostDB:ENSMUSG00000055629; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_011195_0_0_1; -.
DR InParanoid; Q766D5; -.
DR OMA; LEPCTYA; -.
DR OrthoDB; 339331at2759; -.
DR PhylomeDB; Q766D5; -.
DR TreeFam; TF318303; -.
DR BioGRID-ORCS; 330671; 2 hits in 76 CRISPR screens.
DR ChiTaRS; B4galnt4; mouse.
DR PRO; PR:Q766D5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q766D5; protein.
DR Bgee; ENSMUSG00000055629; Expressed in embryonic brain and 157 other tissues.
DR ExpressionAtlas; Q766D5; baseline and differential.
DR Genevisible; Q766D5; MM.
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: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 Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1034
FT /note="N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000252371"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..1034
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 109..279
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REGION 51..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..817
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020917"
SQ SEQUENCE 1034 AA; 117373 MW; 2EF36F8710CA5B73 CRC64;
MPWFPVKKVR KQMKLLLLLL LLTCAAWLTY VHRSLVRPGR ALRQRLGYGR DGEKLTGVTD
SRGVRVPSST QRSEDSSESH EEEQAPEGRG PNMLFPGGPR KPPPLNLTHQ TPPWREEFKG
QVNLHVFEDW CGGAVGHLRR NLHFPLFPHT RTTVTKLAVS PKWKNYGLRI FGFIHPARDG
DIQFSVASDD NSEFWLSLDE SPAAAQLVAF VGKTGSEWTA PGEFTKFSSQ VSKPRRLMAS
RRYYFELLHK QDDKGSDHVE VGWRAFLPGL KFEIIDSAHI SLYTDESSLK MDHVAHVPQS
PASHIGGFPP QGEPSADMLH PDPRDTFFLT PRMEPLSLEN VLEPCAYAPT YILKDFPIAR
YQGLQFVYLS FIYPNDHTRL THMETDNKCF YRESPLYLER FGFYKYMKMD KEEGEEDEEE
EVQRRAFLFL NPDDFLDEED EQDLLDSLEP TDASVQQSHR TPTPAASTGT TASPTPPTTS
PLDEQTLRHS RALNWAPRPL PLFLGRAPPP RTVEKSPSKV YVTRVRPGQR ASPRALRDSP
WPPFPGVFLR PKPLPRVQLR VPPHPPRTQG YRTSGPKVTE LKPPVRAQTS QGGREGQLHG
QGLMVPTVDL NSSVETQPVT SFLSLSQVSR PQLPGEGEEG EEDGAPGDEA TSEDSEEEEE
PAAGRPLGRW REDAINWQRT FSVGAMDFEL LRSDWNDLRC NVSGNLQLPE AEAVDVVAQY
MERLNAKHGG RFSLLRIVNV EKRRDSARGS RFLLELELQE RGGSRQRLSE YVFLRLPGAR
VGDEDGESPE PPPAASIHPD SRPELCRPLH LAWRQDVMVH FIVPVKNQAR WVVQFLADMT
ALHVHTGDSY FNIILVDFES EDMDVERALR AAQLPRYQYL KRTGNFERSA GLQTGVDAVE
DPSSIVFLCD LHIHFPPNIL DSIRKHCVEG KLAFAPVVMR LGCGSSPWDP HGYWEVNGFG
LFGIYKSDFD RVGGMNTEEF RDQWGGEDWE LLDRVLQAGL EVERLRLRHF YHHYHSKRGM
WATRSRKGAR AQRS
