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Polypeptide N-acetylgalactosaminyltransferase 6 (EC 2.4.1.41) (Polypeptide GalNAc transferase 6) (GalNAc-T6) (pp-GaNTase 6) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6)

 GALT6_HUMAN             Reviewed;         622 AA.
Q8NCL4; Q8IYH4; Q9H6G2; Q9UIV5;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
25-OCT-2017, entry version 131.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 6;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 6;
Short=GalNAc-T6;
Short=pp-GaNTase 6;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
Name=GALNT6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Gastric carcinoma;
PubMed=10464263; DOI=10.1074/jbc.274.36.25362;
Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N.,
Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.;
"Cloning and characterization of a close homologue of human UDP-N-
acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-
T3, designated GalNAc-T6. Evidence for genetic but not functional
redundancy.";
J. Biol. Chem. 274:25362-25370(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney epithelium, and Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
-!- 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. May participate in synthesis of oncofetal
fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin
peptides.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:10464263}.
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed in placenta and trachea. Weakly
expressed in brain and pancreas. Expressed in fibroblast. Weakly
or not expressed in lung, liver, muscle, kidney, spleen, thymus,
prostate, testis, ovary, intestine, colon, leukocyte, stomach,
thyroid, spinal cord, lymph node, trachea, adrenal gland and bone
marrow. {ECO:0000269|PubMed:10464263}.
-!- 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=BAB15297.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 6;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_488";
-----------------------------------------------------------------------
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EMBL; Y08565; CAA69876.1; -; mRNA.
EMBL; AK025961; BAB15297.1; ALT_INIT; mRNA.
EMBL; AK074658; BAC11118.1; -; mRNA.
EMBL; BC035822; AAH35822.2; -; mRNA.
CCDS; CCDS8813.1; -.
RefSeq; NP_009141.2; NM_007210.3.
RefSeq; XP_005268664.1; XM_005268607.1.
RefSeq; XP_006719277.1; XM_006719214.2.
RefSeq; XP_011536121.1; XM_011537819.2.
RefSeq; XP_011536124.1; XM_011537822.2.
RefSeq; XP_016874233.1; XM_017018744.1.
RefSeq; XP_016874234.1; XM_017018745.1.
UniGene; Hs.505575; -.
ProteinModelPortal; Q8NCL4; -.
SMR; Q8NCL4; -.
BioGrid; 116393; 26.
IntAct; Q8NCL4; 5.
MINT; MINT-5006466; -.
STRING; 9606.ENSP00000348668; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q8NCL4; -.
PhosphoSitePlus; Q8NCL4; -.
BioMuta; GALNT6; -.
DMDM; 51316028; -.
EPD; Q8NCL4; -.
MaxQB; Q8NCL4; -.
PaxDb; Q8NCL4; -.
PeptideAtlas; Q8NCL4; -.
PRIDE; Q8NCL4; -.
DNASU; 11226; -.
Ensembl; ENST00000356317; ENSP00000348668; ENSG00000139629.
Ensembl; ENST00000543196; ENSP00000444171; ENSG00000139629.
GeneID; 11226; -.
KEGG; hsa:11226; -.
UCSC; uc001ryk.3; human.
CTD; 11226; -.
DisGeNET; 11226; -.
EuPathDB; HostDB:ENSG00000139629.15; -.
GeneCards; GALNT6; -.
HGNC; HGNC:4128; GALNT6.
HPA; HPA011762; -.
HPA; HPA017086; -.
MIM; 605148; gene.
neXtProt; NX_Q8NCL4; -.
OpenTargets; ENSG00000139629; -.
PharmGKB; PA28541; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q8NCL4; -.
KO; K00710; -.
OMA; SYFEHIG; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q8NCL4; -.
TreeFam; TF313267; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; GALNT6; human.
GeneWiki; GALNT6; -.
GenomeRNAi; 11226; -.
PRO; PR:Q8NCL4; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139629; -.
CleanEx; HS_GALNT6; -.
ExpressionAtlas; Q8NCL4; baseline and differential.
Genevisible; Q8NCL4; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
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; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0006493; P:protein O-linked glycosylation; TAS:ProtInc.
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;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Polymorphism; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 622 Polypeptide N-
acetylgalactosaminyltransferase 6.
/FTId=PRO_0000059114.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 622 Lumenal. {ECO:0000255}.
DOMAIN 496 622 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 176 285 Catalytic subdomain A.
REGION 348 410 Catalytic subdomain B.
METAL 269 269 Manganese. {ECO:0000250}.
METAL 271 271 Manganese. {ECO:0000250}.
METAL 407 407 Manganese. {ECO:0000250}.
BINDING 217 217 Substrate. {ECO:0000250}.
BINDING 246 246 Substrate. {ECO:0000250}.
BINDING 379 379 Substrate. {ECO:0000250}.
BINDING 410 410 Substrate. {ECO:0000250}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 165 402 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 393 474 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 509 527 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 553 566 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 597 610 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VARIANT 423 423 V -> I (in dbSNP:rs747300).
/FTId=VAR_019580.
CONFLICT 362 362 S -> P (in Ref. 1; CAA69876).
{ECO:0000305}.
CONFLICT 454 454 A -> T (in Ref. 2; BAC11118).
{ECO:0000305}.
CONFLICT 551 551 Q -> R (in Ref. 2; BAC11118).
{ECO:0000305}.
SEQUENCE 622 AA; 71159 MW; 38E63FF2AFB486EF CRC64;
MRLLRRRHMP LRLAMVGCAF VLFLFLLHRD VSSREEATEK PWLKSLVSRK DHVLDLMLEA
MNNLRDSMPK LQIRAPEAQQ TLFSINQSCL PGFYTPAELK PFWERPPQDP NAPGADGKAF
QKSKWTPLET QEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLATTS
VIIVFHNEAW STLLRTVYSV LHTTPAILLK EIILVDDAST EEHLKEKLEQ YVKQLQVVRV
VRQEERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TVVVSPDIVT
IDLNTFEFAK PVQRGRVHSR GNFDWSLTFG WETLPPHEKQ RRKDETYPIK SPTFAGGLFS
ISKSYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
TSVIARNQVR LAEVWMDSYK KIFYRRNLQA AKMAQEKSFG DISERLQLRE QLHCHNFSWY
LHNVYPEMFV PDLTPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYSCHGL GGNQYFEYTT
QRDLRHNIAK QLCLHVSKGA LGLGSCHFTG KNSQVPKDEE WELAQDQLIR NSGSGTCLTS
QDKKPAMAPC NPSDPHQLWL FV


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