Q8N4A0 (GALT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 4
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 4
Short name=GalNAc-T4
Short name=pp-GaNTase 4
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4

Gene names

Name:

GALNT4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Probable Ref.1.
Tissue specificity	Ubiquitous. Highly expressed in mucous cells. Ref.1
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 By similarity. Ref.5 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. Ref.5
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay PubMed 12506059. Source: BHF-UCL
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N4A0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8N4A0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: MAVRWTWAGK...SLHRHIEDKR → MAWCVATADP...WTSAPTASNL
     121-292: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 578	578	Polypeptide N-acetylgalactosaminyltransferase 4		PRO_0000059108
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	36 – 578	543	Lumenal Potential
	Domain	444 – 577	134	Ricin B-type lectin
	Region	134 – 243	110	Catalytic subdomain A
	Region	303 – 365	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	471	1	N-linked (GlcNAc...) Potential
	Disulfide bond	457 ↔ 477		By similarity
	Disulfide bond	503 ↔ 518		By similarity
	Disulfide bond	547 ↔ 565		By similarity
Natural variations
	Alternative sequence	1 – 120	120	MAVRW…IEDKR → MAWCVATADPAHTSRPLFTG LAVSRGSAGHAWSAGFDWAA VVVVTGRRCRSGQTVPGAAR SPLLPHPLPSPLRVPPPTGA LGRPLPRWPQPRRTPFWSVI SKATKLRSPPWTSAPTASNL in isoform 2.		VSP_045009
	Alternative sequence	121 – 292	172	Missing in isoform 2.		VSP_045010
	Natural variant	51	1	D → G. Ref.4 Corresponds to variant rs17853610 [ dbSNP | Ensembl ].		VAR_065257
	Natural variant	270	1	I → T. Ref.2 Corresponds to variant rs2230281 [ dbSNP | Ensembl ].		VAR_019576
	Natural variant	506	1	V → I. Ref.1 Ref.2 Corresponds to variant rs2230283 [ dbSNP | Ensembl ].		VAR_019577
Experimental info
	Mutagenesis	459	1	D → H: Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC. Ref.5
	Sequence conflict	11	1	S → T in CAA69875. Ref.1
	Sequence conflict	227	1	D → Y in CAA69875. Ref.1
	Sequence conflict	247	1	D → Y in CAA69875. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 28, 2011. Version 2. Checksum: 6EEEF502A40CBD2E	FASTA	578	66,666
	10 20 30 40 50 60 MAVRWTWAGK SCLLLAFLTV AYIFVELLVS TFHASAGAGR ARELGSRRLS DLQKNTEDLS 70 80 90 100 110 120 RPLYKKPPAD SRALGEWGKA SKLQLNEDEL KQQEELIERY AINIYLSDRI SLHRHIEDKR 130 140 150 160 170 180 MYECKSQKFN YRTLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRV 190 200 210 220 230 240 YLKTQLETYI SNLDRVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNSGWLEPL 250 260 270 280 290 300 LERIGRDETA VVCPVIDTID WNTFEFYMQI GEPMIGGFDW RLTFQWHSVP KQERDRRISR 310 320 330 340 350 360 IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV 370 380 390 400 410 420 GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDIS ERKLLRERLR 430 440 450 460 470 480 CKSFDWYLKN VFPNLHVPED RPGWHGAIRS RGISSECLDY NSPDNNPTGA NLSLFGCHGQ 490 500 510 520 530 540 GGNQFFEYTS NKEIRFNSVT ELCAEVPEQK NYVGMQNCPK DGFPVPANII WHFKEDGTIF 550 560 570 HPHSGLCLSA YRTPEGRPDV QMRTCDALDK NQIWSFEK
	Isoform 2 [UniParc]. Checksum: EB89E46BF360847D	FASTA	406	45,702
	10 20 30 40 50 60 MAWCVATADP AHTSRPLFTG LAVSRGSAGH AWSAGFDWAA VVVVTGRRCR SGQTVPGAAR 70 80 90 100 110 120 SPLLPHPLPS PLRVPPPTGA LGRPLPRWPQ PRRTPFWSVI SKATKLRSPP WTSAPTASNL 130 140 150 160 170 180 ERDRRISRID PIRSPTMAGG LFAVSKKYFQ YLGTYDTGME VWGGENLELS FRVWQCGGKL 190 200 210 220 230 240 EIHPCSHVGH VFPKRAPYAR PNFLQNTARA AEVWMDEYKE HFYNRNPPAR KEAYGDISER 250 260 270 280 290 300 KLLRERLRCK SFDWYLKNVF PNLHVPEDRP GWHGAIRSRG ISSECLDYNS PDNNPTGANL 310 320 330 340 350 360 SLFGCHGQGG NQFFEYTSNK EIRFNSVTEL CAEVPEQKNY VGMQNCPKDG FPVPANIIWH 370 380 390 400 FKEDGTIFHP HSGLCLSAYR TPEGRPDVQM RTCDALDKNQ IWSFEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." 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. J. Biol. Chem. 273:30472-30481(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ILE-506.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS THR-270 AND ILE-506. Tissue: Kidney and Trachea.
[3]	"The finished DNA sequence of human chromosome 12." 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. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-51. Tissue: Brain.
[5]	"The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities." Hassan H., Reis C.A., Bennett E.P., Mirgorodskaya E., Roepstorff P., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H. J. Biol. Chem. 275:38197-38205(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF ASP-459.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 4

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08564 Genomic DNA. Translation: CAA69875.1. AK297677 mRNA. Translation: BAG60038.1. AK312870 mRNA. Translation: BAG35722.1. AC010201 Genomic DNA. No translation available. AC025034 Genomic DNA. No translation available. BC036390 mRNA. Translation: AAH36390.1.
IPI	IPI00339297. IPI00911074.
RefSeq	NP_001186711.1. NM_001199782.1. NP_003765.2. NM_003774.4.
UniGene	Hs.25130.
3D structure databases
ProteinModelPortal	Q8N4A0.
SMR	Q8N4A0. Positions 103-577.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q8N4A0.
Polymorphism databases
DMDM	51316025.
Proteomic databases
PeptideAtlas	Q8N4A0.
PRIDE	Q8N4A0.
Protocols and materials databases
DNASU	8693.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000529983; ENSP00000436604; ENSG00000257594.
GeneID	100528030. 8693.
KEGG	hsa:100528030. hsa:8693.
UCSC	uc001tbd.3. human.
Organism-specific databases
CTD	8693.
GeneCards	GC12M089913.
HGNC	HGNC:4126. GALNT4.
MIM	603565. gene.
neXtProt	NX_Q8N4A0.
PharmGKB	PA28539.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG051699.
KO	K00710.
OMA	NTFEFYM.
Enzyme and pathway databases
BRENDA	2.4.1.41. 2681.
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
CleanEx	HS_GALNT4.
Genevestigator	Q8N4A0.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	100528030.
NextBio	32603.
SOURCE	Search...

Entry information

Entry name

GALT4_HUMAN

Accession

Primary (citable) accession number: Q8N4A0
Secondary accession number(s): B2R775, B4DMX6, O00208

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.