O08832 (GALT4_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b.
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 By similarity.
Tissue specificity	Highly expressed in sublingual gland, stomach, colon, small intestine and cervix. Expressed at intermediate levels in kidney, ovary, lung and uterus. Weakly expressed in spleen, liver, heart and brain. Not expressed in submandibular and parotid glands, skeletal muscle and testis. 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. 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 By similarity.
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
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	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 578	578	Polypeptide N-acetylgalactosaminyltransferase 4		PRO_0000059109
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

Sequences

	Sequence		Length	Mass (Da)
	O08832 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 10ADC0D8B8B30835	FASTA	578	66,555
	10 20 30 40 50 60 MAVRWTWAGK SCLLLALLTL AYILVEFSVS TLYASPGAGG ARELGPRRLP DLDTREEDLS 70 80 90 100 110 120 QPLYIKPPAD SHALGEWGRA SKLQLNEGEL KQQEELIERY AINIYLSDRI SLHRHIEDKR 130 140 150 160 170 180 MYECKAKKFH YRSLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRI 190 200 210 220 230 240 YLKAQLETYI SNLERVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNTGWLEPL 250 260 270 280 290 300 LERISRDETA IVCPVIDTID WNTFEFYMQT GEPMIGGFDW RLTFQWHSVP KHERDRRTSR 310 320 330 340 350 360 IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV 370 380 390 400 410 420 GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDLS ERKLLRERLK 430 440 450 460 470 480 CKSFDWYLKN VFSNLHVPED RPGWHGAIRS MGISSECLDY NAPDNNPTGA NLSLFGCHGQ 490 500 510 520 530 540 GGNQFFEYTS NKEIRFNSVT ELCAEVPQQK DYVGMQNCPK DGLPVPVNII WHFKEDGTIF 550 560 570 HPHTRLCLSA YRTAEGRPSV HMKTCDALDK NQLWRFEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase." Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A. J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY. Tissue: Spleen.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow and Colon.
[3]	"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]. Strain: NMRI. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 4

Cross-references

Sequence databases
EMBL GenBank DDBJ	U73819 mRNA. Translation: AAB58301.1. AK033494 mRNA. Translation: BAC28317.1. AK148036 mRNA. Translation: BAE28303.1. AK153253 mRNA. Translation: BAE31844.1. BC057882 mRNA. Translation: AAH57882.1.
IPI	IPI00116332.
RefSeq	NP_056552.1. NM_015737.4.
UniGene	Mm.314.
3D structure databases
ProteinModelPortal	O08832.
SMR	O08832. Positions 75-577.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	O08832.
Proteomic databases
PRIDE	O08832.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000161240; ENSMUSP00000125315; ENSMUSG00000090035.
GeneID	14426.
KEGG	mmu:14426.
UCSC	uc007gxj.2. mouse.
Organism-specific databases
CTD	8693.
MGI	MGI:894692. Galnt4.
Phylogenomic databases
GeneTree	ENSGT00700000104138.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
KO	K00710.
OMA	NTFEFYM.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	O08832.
Genevestigator	O08832.
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
NextBio	286029.
SOURCE	Search...

Entry information

Entry name

GALT4_MOUSE

Accession

Primary (citable) accession number: O08832
Secondary accession number(s): Q3U681

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program