P70419 (GALT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 3
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 3
Short name=GalNAc-T3
Short name=pp-GaNTase 3
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3

Gene names

Name:

Galnt3

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	633 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 activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Glycosylates FGF23 By similarity. Probably glycosylates fibronectin in vivo. May be involved in phosphate homeostasis.
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 › Golgi stack membrane; Single-pass type II membrane protein By similarity. Note: Resides preferentially in the trans and medial parts of the Golgi stack By similarity.
Tissue specificity	Highly expressed in the reproductive tract, principally in the testis and uterus, and to a lesser degree in the cervix with only trace levels in the ovary. Also expressed at high level in sublingual gland, stomach and colon, with more moderate amounts present in the submandibular and parotid gland as well as the kidney. 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 binds to GalNAc and contributes to the glycopeptide specificity 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 O-linked glycosylation via serine Inferred from electronic annotation. Source: Compara protein O-linked glycosylation via threonine Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: Compara manganese ion binding Inferred from electronic annotation. Source: Compara 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 – 633	633	Polypeptide N-acetylgalactosaminyltransferase 3		PRO_0000059107
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 37	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	38 – 633	596	Lumenal Potential
	Domain	504 – 630	127	Ricin B-type lectin
	Region	184 – 293	110	Catalytic subdomain A
	Region	356 – 418	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	484	1	N-linked (GlcNAc...) Potential
	Disulfide bond	517 ↔ 535		By similarity
	Disulfide bond	561 ↔ 574		By similarity
	Disulfide bond	605 ↔ 618		By similarity
Experimental info
	Sequence conflict	324	1	S → N in AAH43331. Ref.5
	Sequence conflict	633	1	D → E in AAB09579. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P70419 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 8BEE7CDDBCF56428	FASTA	633	72,932
	10 20 30 40 50 60 MAHLKRLVKL HIKRHYHRKF WKLGAVIFFF LVVLILMQRE VSVQYSKEES KMERNLKNKN 70 80 90 100 110 120 KMLDFMLEAV NNIKDAMPKM QIGAPIKENI DVRERPCLQG YYTAAELKPV FDRPPQDSNA 130 140 150 160 170 180 PGASGKPFKI THLSPEEQKE KERGETKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR 190 200 210 220 230 240 CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDD YLHEKLEEYI 250 260 270 280 290 300 KQFSIVKIVR QQERKGLITA RLLGAAVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA 310 320 330 340 350 360 VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP 370 380 390 400 410 420 TFAGGLFSIS KKYFEHIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK 430 440 450 460 470 480 SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKSFGDL SKRFEIKKRL 490 500 510 520 530 540 QCKNFTWYLN TIYPEAYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL ILYTCHGLGG 550 560 570 580 590 600 NQYFEYSAQR EIRHNIQKEL CLHATQGVVQ LKACVYKGHR TIAPGEQIWE IRKDQLLYNP 610 620 630 LFKMCLSSNG EHPNLVPCDA TDLLQKWIFS QND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3." Zara J., Hagen F.K., Ten Hagen K.G., Van Wuyckhuyse B.C., Tabak L.A. Biochem. Biophys. Res. Commun. 228:38-44(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY. Strain: CD-1. Tissue: Testis.
[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: Muellerian duct.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 3

Cross-references

Sequence databases
EMBL GenBank DDBJ	U70538 mRNA. Translation: AAB09579.1. AK135489 mRNA. Translation: BAE22551.1. AL929230, AL928586 Genomic DNA. Translation: CAM20333.1. AL928586, AL929230 Genomic DNA. Translation: CAM21878.1. CH466519 Genomic DNA. Translation: EDL27008.1. BC043331 mRNA. Translation: AAH43331.1.
IPI	IPI00330383.
PIR	JC5247.
RefSeq	NP_056551.2. NM_015736.2.
UniGene	Mm.439760.
3D structure databases
ProteinModelPortal	P70419.
SMR	P70419. Positions 122-633.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000028378.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	P70419.
Proteomic databases
PaxDb	P70419.
PRIDE	P70419.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028378; ENSMUSP00000028378; ENSMUSG00000026994.
GeneID	14425.
KEGG	mmu:14425.
Organism-specific databases
CTD	2591.
MGI	MGI:894695. Galnt3.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104138.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q3UXL2.
KO	K00710.
OMA	QYFEYSA.
OrthoDB	EOG4GB75S.
Enzyme and pathway databases
BRENDA	2.4.1.41. 3474.
UniPathway	UPA00378.
Gene expression databases
Bgee	P70419.
Genevestigator	P70419.
GermOnline	ENSMUSG00000026994. Mus musculus.
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
ChiTaRS	GALNT3. mouse.
NextBio	286025.
SOURCE	Search...

Entry information

Entry name

GALT3_MOUSE

Accession

Primary (citable) accession number: P70419
Secondary accession number(s): Q3UXL2, Q80V55

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program