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Polypeptide N-acetylgalactosaminyltransferase 4 (EC 2.4.1.41) (Polypeptide GalNAc transferase 4) (GalNAc-T4) (pp-GaNTase 4) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4)

 GALT4_HUMAN             Reviewed;         578 AA.
Q8N4A0; B2R775; B4DMX6; O00208;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
25-OCT-2017, entry version 127.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 4;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 4;
Short=GalNAc-T4;
Short=pp-GaNTase 4;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 4;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4;
Name=GALNT4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANT ILE-506.
PubMed=9804815; DOI=10.1074/jbc.273.46.30472;
Bennett E.P., Hassan H., Mandel U., Mirgorodskaya E., Roepstorff P.,
Burchell J., Taylor-Papadimitriou J., Hollingsworth M.A., Merkx G.,
van Kessel A.G., Eiberg H., Steffensen R., Clausen H.;
"Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-
acetylgalactosaminyltransferase that complements other GalNAc-
transferases in complete O-glycosylation of the MUC1 tandem repeat.";
J. Biol. Chem. 273:30472-30481(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS THR-270 AND ILE-506.
TISSUE=Kidney, and Trachea;
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 GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLY-51.
TISSUE=Brain;
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).
[5]
DOMAIN, AND MUTAGENESIS OF ASP-459.
PubMed=10984485; DOI=10.1074/jbc.M005783200;
Hassan H., Reis C.A., Bennett E.P., Mirgorodskaya E., Roepstorff P.,
Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.;
"The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-
acetylgalactosaminyltransferase-T4 directs its glycopeptide
specificities.";
J. Biol. Chem. 275:38197-38205(2000).
-!- 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. Has a highest activity toward Muc7, EA2 and
Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of
SELPLG.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:9804815}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000305|PubMed:9804815}; Single-pass type II membrane protein
{ECO:0000305|PubMed:9804815}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N4A0-1; Sequence=Displayed;
Name=2;
IsoId=Q8N4A0-2; Sequence=VSP_045009, VSP_045010;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mucous cells.
{ECO:0000269|PubMed:9804815}.
-!- 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 directs the glycopeptide
specificity. It is required in the glycopeptide specificity of
enzyme activity but not for activity with naked peptide
substrates, suggesting that it triggers the catalytic domain to
act on GalNAc-glycopeptide substrates.
{ECO:0000269|PubMed:10984485}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 4;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_486";
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EMBL; Y08564; CAA69875.1; -; Genomic_DNA.
EMBL; AK297677; BAG60038.1; -; mRNA.
EMBL; AK312870; BAG35722.1; -; mRNA.
EMBL; AC010201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036390; AAH36390.1; -; mRNA.
CCDS; CCDS53817.1; -. [Q8N4A0-1]
RefSeq; NP_001186711.1; NM_001199782.1. [Q8N4A0-2]
RefSeq; NP_003765.2; NM_003774.4. [Q8N4A0-1]
UniGene; Hs.25130; -.
ProteinModelPortal; Q8N4A0; -.
SMR; Q8N4A0; -.
BioGrid; 114240; 9.
BioGrid; 1529357; 1.
STRING; 9606.ENSP00000436604; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q8N4A0; -.
PhosphoSitePlus; Q8N4A0; -.
SwissPalm; Q8N4A0; -.
BioMuta; GALNT4; -.
DMDM; 338817878; -.
EPD; Q8N4A0; -.
MaxQB; Q8N4A0; -.
PaxDb; Q8N4A0; -.
PeptideAtlas; Q8N4A0; -.
PRIDE; Q8N4A0; -.
DNASU; 8693; -.
Ensembl; ENST00000529983; ENSP00000436604; ENSG00000257594. [Q8N4A0-1]
GeneID; 100528030; -.
GeneID; 8693; -.
KEGG; hsa:100528030; -.
KEGG; hsa:8693; -.
UCSC; uc001tbd.4; human. [Q8N4A0-1]
CTD; 100528030; -.
CTD; 8693; -.
DisGeNET; 100528030; -.
DisGeNET; 8693; -.
EuPathDB; HostDB:ENSG00000257594.3; -.
GeneCards; GALNT4; -.
HGNC; HGNC:4126; GALNT4.
HPA; HPA076116; -.
MIM; 603565; gene.
neXtProt; NX_Q8N4A0; -.
OpenTargets; ENSG00000257594; -.
PharmGKB; PA28539; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q8N4A0; -.
KO; K00710; -.
OMA; ISLHRHI; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q8N4A0; -.
TreeFam; TF352660; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
PRO; PR:Q8N4A0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000257594; -.
CleanEx; HS_GALNT4; -.
Genevisible; Q8N4A0; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
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:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
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.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Polymorphism; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 578 Polypeptide N-
acetylgalactosaminyltransferase 4.
/FTId=PRO_0000059108.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 35 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 36 578 Lumenal. {ECO:0000255}.
DOMAIN 444 577 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 134 243 Catalytic subdomain A.
REGION 303 365 Catalytic subdomain B.
METAL 227 227 Manganese. {ECO:0000250}.
METAL 229 229 Manganese. {ECO:0000250}.
METAL 362 362 Manganese. {ECO:0000250}.
BINDING 175 175 Substrate. {ECO:0000250}.
BINDING 204 204 Substrate. {ECO:0000250}.
BINDING 334 334 Substrate. {ECO:0000250}.
BINDING 370 370 Substrate. {ECO:0000250}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 124 357 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 348 421 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 457 477 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 503 518 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 547 565 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 1 120 MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRA
RELGSRRLSDLQKNTEDLSRPLYKKPPADSRALGEWGKASK
LQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKR ->
MAWCVATADPAHTSRPLFTGLAVSRGSAGHAWSAGFDWAAV
VVVTGRRCRSGQTVPGAARSPLLPHPLPSPLRVPPPTGALG
RPLPRWPQPRRTPFWSVISKATKLRSPPWTSAPTASNL
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045009.
VAR_SEQ 121 292 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045010.
VARIANT 51 51 D -> G (in dbSNP:rs17853610).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_065257.
VARIANT 270 270 I -> T (in dbSNP:rs2230281).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_019576.
VARIANT 506 506 V -> I (in dbSNP:rs2230283).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9804815}.
/FTId=VAR_019577.
MUTAGEN 459 459 D->H: Affects the glycopeptide
specificity and abolishes ability to
glycosylate Muc1, Muc2 and Muc5AC.
{ECO:0000269|PubMed:10984485}.
CONFLICT 11 11 S -> T (in Ref. 1; CAA69875).
{ECO:0000305}.
CONFLICT 227 227 D -> Y (in Ref. 1; CAA69875).
{ECO:0000305}.
CONFLICT 247 247 D -> Y (in Ref. 1; CAA69875).
{ECO:0000305}.
SEQUENCE 578 AA; 66666 MW; 6EEEF502A40CBD2E CRC64;
MAVRWTWAGK SCLLLAFLTV AYIFVELLVS TFHASAGAGR ARELGSRRLS DLQKNTEDLS
RPLYKKPPAD SRALGEWGKA SKLQLNEDEL KQQEELIERY AINIYLSDRI SLHRHIEDKR
MYECKSQKFN YRTLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRV
YLKTQLETYI SNLDRVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNSGWLEPL
LERIGRDETA VVCPVIDTID WNTFEFYMQI GEPMIGGFDW RLTFQWHSVP KQERDRRISR
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV
GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDIS ERKLLRERLR
CKSFDWYLKN VFPNLHVPED RPGWHGAIRS RGISSECLDY NSPDNNPTGA NLSLFGCHGQ
GGNQFFEYTS NKEIRFNSVT ELCAEVPEQK NYVGMQNCPK DGFPVPANII WHFKEDGTIF
HPHSGLCLSA YRTPEGRPDV QMRTCDALDK NQIWSFEK


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