Reviewed, UniProtKB/Swiss-Prot Q8C102 (GALT5_MOUSE)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 5
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 5
      Short name=pp-GaNTase 5
      Short name=GalNAc-T5
    Protein-UDP acetylgalactosaminyltransferase 5
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5

Gene names

Name:

Galnt5

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	930 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates By similarity.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 By similarity.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Expressed at low level. Not expressed before E7.5 during embryogenesis. Expressed in dental mesenchyme and tongue. Accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 maxilla and mandible underlying the dental lamina. Ref.2
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
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 930	930	Polypeptide N-acetylgalactosaminyltransferase 5		PRO_0000059111
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Signal-anchor for type II membrane protein Potential
	Topological domain	36 – 930	895	Lumenal Potential
	Domain	794 – 925	132	Ricin B-type lectin
	Region	485 – 594	110	Catalytic subdomain A
	Region	654 – 716	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Glycosylation	283	1	N-linked (GlcNAc...) Potential
	Glycosylation	287	1	N-linked (GlcNAc...) Potential
	Glycosylation	309	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Glycosylation	387	1	N-linked (GlcNAc...) Potential
	Glycosylation	568	1	N-linked (GlcNAc...) Potential
	Glycosylation	766	1	N-linked (GlcNAc...) Potential
	Glycosylation	817	1	N-linked (GlcNAc...) Potential
	Glycosylation	835	1	N-linked (GlcNAc...) Potential
	Glycosylation	902	1	N-linked (GlcNAc...) Potential
	Disulfide bond	812 ↔ 825		By similarity
	Disulfide bond	848 ↔ 863		By similarity
	Disulfide bond	898 ↔ 913		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8C102-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: AC635A0A458B81B0	FASTA	930	105,780
	10 20 30 40 50 60 MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII RREHTGFRVE 70 80 90 100 110 120 PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN MDQVQRKGKM QNLLGRRKAV 130 140 150 160 170 180 PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS SQYMMSKWMT VLESEKTPFT ASRGVPLTKI 190 200 210 220 230 240 AGRTETFDKK QEAPQNYNVS SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP 250 260 270 280 290 300 PILKSEEVTV IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA 310 320 330 340 350 360 KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK QIPRNQSKTS 370 380 390 400 410 420 SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS HANIPENPGM HHVFRIDVTL 430 440 450 460 470 480 SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL 490 500 510 520 530 540 VHNDLPTTSI IMCFVDEVWS ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY 550 560 570 580 590 600 MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 610 620 630 640 650 660 KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK ETDIIRCPVM 670 680 690 700 710 720 AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG GEIELIPCSR VGHIFRNDNP 730 740 750 760 770 780 YSFPKDRMKT VERNLVRVAE VWLDDYRELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK 790 800 810 820 830 840 SFKWYLDNVF PDLKAPVVRA SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR 850 860 870 880 890 900 LIKHGEWCVA PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME 910 920 930 GNFSQKTLKL AACNPMELQQ KWKFEKYYEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head.
[2]	"Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development." Kingsley P.D., Hagen K.G., Maltby K.M., Zara J., Tabak L.A. Glycobiology 10:1317-1323(2000) [PubMed: 11159923] [Abstract] Cited for: TISSUE SPECIFICITY.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK029323 mRNA. Translation: BAC26396.1.
IPI	IPI00223910.
UniGene	Mm.68639
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8C102.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q8C102.
Genome annotation databases
Ensembl	ENSMUST00000028171; ENSMUSP00000028171; ENSMUSG00000026828; Mus musculus. [Genome view] ENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828; Mus musculus. [Genome view]
UCSC	uc008jsg.1. mouse.
Organism-specific databases
MGI	MGI:2179403. Galnt5.
Phylogenomic databases
HOGENOM	Q8C102.
HOVERGEN	Q8C102.
Enzyme and pathway databases
BRENDA	2.4.1.41. 244.
Gene expression databases
ArrayExpress	Q8C102.
Bgee	Q8C102.
Genevestigator	Q8C102.
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]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

GALT5_MOUSE

Accession

Primary (citable) accession number: Q8C102

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2003
Last modified:	October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)