GLT18_MOUSE
ID GLT18_MOUSE Reviewed; 622 AA.
AC Q8K1B9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 18;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 18;
DE Short=GalNAc-T18;
DE AltName: Full=Polypeptide GalNAc transferase-like protein 4;
DE Short=GalNAc-T-like protein 4;
DE Short=pp-GaNTase-like protein 4;
DE AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 4;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 4;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4;
GN Name=Galnt18; Synonyms=Galntl4;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc)
CC residue from UDP-GalNAc to a serine or threonine residue on the protein
CC receptor. {ECO:0000250|UniProtKB:Q6P9A2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000250|UniProtKB:Q6P9A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957;
CC Evidence={ECO:0000250|UniProtKB:Q6P9A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000250|UniProtKB:Q6P9A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000250|UniProtKB:Q6P9A2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q6P9A2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC polypeptide N-acetylgalactosaminyltransferase-like protein 4;
CC URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_526";
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DR EMBL; BC024988; AAH24988.1; -; mRNA.
DR CCDS; CCDS21751.1; -.
DR RefSeq; NP_776100.2; NM_173739.3.
DR AlphaFoldDB; Q8K1B9; -.
DR SMR; Q8K1B9; -.
DR STRING; 10090.ENSMUSP00000043636; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8K1B9; 3 sites.
DR PhosphoSitePlus; Q8K1B9; -.
DR MaxQB; Q8K1B9; -.
DR PaxDb; Q8K1B9; -.
DR PRIDE; Q8K1B9; -.
DR ProteomicsDB; 271234; -.
DR Antibodypedia; 2327; 50 antibodies from 18 providers.
DR DNASU; 233733; -.
DR Ensembl; ENSMUST00000049430; ENSMUSP00000043636; ENSMUSG00000038296.
DR GeneID; 233733; -.
DR KEGG; mmu:233733; -.
DR UCSC; uc009jgc.1; mouse.
DR CTD; 374378; -.
DR MGI; MGI:2446239; Galnt18.
DR VEuPathDB; HostDB:ENSMUSG00000038296; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000155456; -.
DR HOGENOM; CLU_013477_4_0_1; -.
DR InParanoid; Q8K1B9; -.
DR OMA; NQHIHET; -.
DR OrthoDB; 273006at2759; -.
DR PhylomeDB; Q8K1B9; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 233733; 4 hits in 58 CRISPR screens.
DR ChiTaRS; Galnt18; mouse.
DR PRO; PR:Q8K1B9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K1B9; protein.
DR Bgee; ENSMUSG00000038296; Expressed in right lung and 209 other tissues.
DR ExpressionAtlas; Q8K1B9; baseline and differential.
DR Genevisible; Q8K1B9; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:MGI.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Polypeptide N-acetylgalactosaminyltransferase 18"
FT /id="PRO_0000059142"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..622
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 484..614
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 153..267
FT /note="Catalytic subdomain A"
FT REGION 324..400
FT /note="Catalytic subdomain B"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 383..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 497..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 545..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 586..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 622 AA; 71096 MW; 4FE9493795E3A561 CRC64;
MVCTRKTKTL VSTCVILSGM TNIICLLYVG WVTNYIASVY VRGQEPVPDK KLEEDKGDTL
KIIERLDHLE NVIKQHIQEA PAKPEEAEAE PFTDSSLFAH WGQELSPEGR RVALKQFQYY
GYNAYLSDRL PLDRPLPDLR PSGCRNLSFP DSLPEVSIVF IFVNEALSVL LRSIHSAMER
TPSHLLKEII LVDDNSSNEE LKEKLTEYVD KVNGQKPGFI KVVRHSKQEG LIRSRVSGWR
AATAPVVALF DAHVEFNVGW AEPVLTRIKE NRKRIISPSF DNIKYDNFEI EEYPLAAQGF
DWELWCRYLN PPKAWWKLEN STAPIRSPAL IGCFIVDRQY FEEIGLLDEG MEVYGGENVE
LGIRVSEISH TGLSSAPMMV WQCGGSVEVL PCSRIAHIER AHKPYTEDLT AHVRRNALRV
AEVWMDEFKS HVYMAWNIPQ EDSGIDIGDI TARKALRKQL QCKTFRWYLV SVYPEMRMYS
DIIAYGVLQN SLKTDLCLDQ GPDTENVPIV YICHGMTPQN VYYTSSQQIH VGILSPTVDD
DDNRCLVDVN SRPRLIECSY AKAKRMKLHW QFSQGGSIQN RKSKRCLELQ ENSDMEFGFQ
LVLQKCSGQH WTITNVLRSL VS
