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Polypeptide N-acetylgalactosaminyltransferase 18 (EC 2.4.1.41) (Polypeptide GalNAc transferase 18) (GalNAc-T18) (Polypeptide GalNAc transferase-like protein 4) (GalNAc-T-like protein 4) (pp-GaNTase-like protein 4) (Polypeptide N-acetylgalactosaminyltransferase-like protein 4) (Protein-UDP acetylgalactosaminyltransferase-like protein 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4)

 GLT18_HUMAN             Reviewed;         607 AA.
Q6P9A2; O95903; Q8NDY9;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 127.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 18;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 18;
Short=GalNAc-T18;
AltName: Full=Polypeptide GalNAc transferase-like protein 4;
Short=GalNAc-T-like protein 4;
Short=pp-GaNTase-like protein 4;
AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 4;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 4;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4;
Name=GALNT18; Synonyms=GALNTL4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Mei G., Yu W., Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=22186971; DOI=10.1093/glycob/cwr183;
Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.;
"UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
acetylgalactosaminyltransferases: completion of the family tree.";
Glycobiology 22:768-777(2012).
-!- FUNCTION: Catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. {ECO:0000269|PubMed:22186971}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6P9A2-1; Sequence=Displayed;
Name=2;
IsoId=Q6P9A2-2; Sequence=VSP_011234, VSP_011235;
Note=No experimental confirmation available.;
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD20062.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF131852; AAD20062.1; ALT_INIT; mRNA.
EMBL; BC060864; AAH60864.1; -; mRNA.
EMBL; BC037341; AAH37341.3; -; mRNA.
CCDS; CCDS7807.1; -. [Q6P9A2-1]
RefSeq; NP_940918.2; NM_198516.2. [Q6P9A2-1]
UniGene; Hs.655152; -.
UniGene; Hs.667788; -.
ProteinModelPortal; Q6P9A2; -.
SMR; Q6P9A2; -.
BioGrid; 131894; 18.
STRING; 9606.ENSP00000227756; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q6P9A2; -.
PhosphoSitePlus; Q6P9A2; -.
BioMuta; GALNT18; -.
DMDM; 116242498; -.
PaxDb; Q6P9A2; -.
PeptideAtlas; Q6P9A2; -.
PRIDE; Q6P9A2; -.
Ensembl; ENST00000227756; ENSP00000227756; ENSG00000110328. [Q6P9A2-1]
GeneID; 374378; -.
KEGG; hsa:374378; -.
UCSC; uc001mjo.3; human. [Q6P9A2-1]
CTD; 374378; -.
DisGeNET; 374378; -.
EuPathDB; HostDB:ENSG00000110328.5; -.
GeneCards; GALNT18; -.
HGNC; HGNC:30488; GALNT18.
HPA; HPA012955; -.
MIM; 615136; gene.
neXtProt; NX_Q6P9A2; -.
OpenTargets; ENSG00000110328; -.
PharmGKB; PA134950929; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00900000140827; -.
HOGENOM; HOG000038228; -.
HOVERGEN; HBG051699; -.
InParanoid; Q6P9A2; -.
KO; K00710; -.
OMA; SLFAHWG; -.
OrthoDB; EOG091G036M; -.
PhylomeDB; Q6P9A2; -.
TreeFam; TF313267; -.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
GenomeRNAi; 374378; -.
PRO; PR:Q6P9A2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110328; -.
CleanEx; HS_GALNTL4; -.
ExpressionAtlas; Q6P9A2; baseline and differential.
Genevisible; Q6P9A2; HS.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 607 Polypeptide N-
acetylgalactosaminyltransferase 18.
/FTId=PRO_0000059141.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 35 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 36 607 Lumenal. {ECO:0000255}.
DOMAIN 469 599 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 153 267 Catalytic subdomain A.
REGION 324 385 Catalytic subdomain B.
METAL 251 251 Manganese. {ECO:0000250}.
METAL 253 253 Manganese. {ECO:0000250}.
METAL 382 382 Manganese. {ECO:0000250}.
BINDING 194 194 Substrate. {ECO:0000250}.
BINDING 385 385 Substrate. {ECO:0000250}.
BINDING 390 390 Substrate. {ECO:0000250}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 144 377 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 368 447 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 482 498 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 530 543 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 571 591 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 79 91 EAPAKPEEAEAEP -> GYRRNFSLLNVSN (in
isoform 2). {ECO:0000303|Ref.1}.
/FTId=VSP_011234.
VAR_SEQ 92 607 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_011235.
CONFLICT 133 133 D -> G (in Ref. 2; AAH60864).
{ECO:0000305}.
CONFLICT 541 541 I -> T (in Ref. 2; AAH60864).
{ECO:0000305}.
SEQUENCE 607 AA; 69561 MW; 8FFA7BCB5016FF0C CRC64;
MVCTRKTKTL VSTCVILSGM TNIICLLYVG WVTNYIASVY VRGQEPAPDK KLEEDKGDTL
KIIERLDHLE NVIKQHIQEA PAKPEEAEAE PFTDSSLFAH WGQELSPEGR RVALKQFQYY
GYNAYLSDRL PLDRPLPDLR PSGCRNLSFP DSLPEVSIVF IFVNEALSVL LRSIHSAMER
TPPHLLKEII LVDDNSSNEE LKEKLTEYVD KVNSQKPGFI KVVRHSKQEG LIRSRVSGWR
AATAPVVALF DAHVEFNVGW AEPVLTRIKE NRKRIISPSF DNIKYDNFEI EEYPLAAQGF
DWELWCRYLN PPKAWWKLEN STAPIRSPAL IGCFIVDRQY FQEIGLLDEG MEVYGGENVE
LGIRVWQCGG SVEVLPCSRI AHIERAHKPY TEDLTAHVRR NALRVAEVWM DEFKSHVYMA
WNIPQEDSGI DIGDITARKA LRKQLQCKTF RWYLVSVYPE MRMYSDIIAY GVLQNSLKTD
LCLDQGPDTE NVPIMYICHG MTPQNVYYTS SQQIHVGILS PTVDDDDNRC LVDVNSRPRL
IECSYAKAKR MKLHWQFSQG GPIQNRKSKR CLELQENSDL EFGFQLVLQK CSGQHWSITN
VLRSLAS


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