Q8C102 (GALT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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=GalNAc-T5
Short name=pp-GaNTase 5
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5

Gene names

Name:

Galnt5

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	930 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 EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates By similarity.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-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.4
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 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 – 930	930	Polypeptide N-acetylgalactosaminyltransferase 5		PRO_0000059111
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Helical; 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
Experimental info
	Sequence conflict	705	1	I → L in BAC26396. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8C102 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: C5851F6E13CDF5D7	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 GEIEIIPCSR 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head.
[2]	"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.
[3]	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].
[4]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK029323 mRNA. Translation: BAC26396.1. AL928564, AL929144 Genomic DNA. Translation: CAM18783.1. AL929144, AL928564 Genomic DNA. Translation: CAM24473.1. CH466519 Genomic DNA. Translation: EDL26932.1.
IPI	IPI00223910.
RefSeq	NP_766443.2. NM_172855.3.
UniGene	Mm.484118.
3D structure databases
ProteinModelPortal	Q8C102.
SMR	Q8C102. Positions 429-925.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000028171.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q8C102.
Proteomic databases
PRIDE	Q8C102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828. ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
GeneID	241391.
KEGG	mmu:241391.
Organism-specific databases
CTD	11227.
MGI	MGI:2179403. Galnt5.
Phylogenomic databases
eggNOG	NOG307550.
GeneTree	ENSGT00680000099551.
HOGENOM	HOG000231869.
HOVERGEN	HBG051698.
InParanoid	A2AS75.
KO	K00710.
OMA	EGNFSQK.
OrthoDB	EOG41G33C.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
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]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	384997.
SOURCE	Search...

Entry information

Entry name

GALT5_MOUSE

Accession

Primary (citable) accession number: Q8C102
Secondary accession number(s): A2AS75

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program