Q6P9S7 (GLT10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 10
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 10
Short name=GalNAc-T10
Short name=pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10

Gene names

Name:

Galnt10

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	603 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 Muc5Ac and EA2 peptide 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.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Expressed at higher level than GALNT9. In the developing hindbrain region of E14.5 embryos it accumulates in the rapidly dividing, undifferentiated ventricular zone adjacent to the pons. It also accumulates in the regions immediately rostral and caudal to the dorsal rhombic lips differentiating into the cerebellum. Not expressed in the developing choroid plexus. 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.
Caution	According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.
Sequence caution	The sequence AAH16585.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD21405.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein O-linked glycosylation Inferred from direct assay Ref.4. Source: MGI
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.4. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 603	603	Polypeptide N-acetylgalactosaminyltransferase 10		PRO_0000059123
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 31	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	32 – 603	572	Lumenal Potential
	Domain	458 – 590	133	Ricin B-type lectin
	Region	144 – 253	110	Catalytic subdomain A
	Region	311 – 373	63	Catalytic subdomain B
	Region	373 – 384	12	Flexible loop By similarity
Sites
	Metal binding	237	1	Manganese By similarity
	Metal binding	239	1	Manganese By similarity
	Metal binding	370	1	Manganese By similarity
	Binding site	185	1	Substrate By similarity
	Binding site	237	1	Substrate By similarity
Amino acid modifications
	Glycosylation	124	1	N-linked (GlcNAc...) Potential
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	593	1	N-linked (GlcNAc...) Potential
	Disulfide bond	135 ↔ 365		By similarity
	Disulfide bond	356 ↔ 432		By similarity
	Disulfide bond	471 ↔ 488		By similarity
	Disulfide bond	523 ↔ 538		By similarity
	Disulfide bond	563 ↔ 578		By similarity
Experimental info
	Sequence conflict	233	1	V → I in BAD21405. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6P9S7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FF55FBA7E1DD7544	FASTA	603	69,116
	10 20 30 40 50 60 MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGLGAAVAPA AVQELHSRQK 70 80 90 100 110 120 KTFFLGAEQR LKDWHNKEAI RRDAQRVGYG EQGKPYPMTD AERVDQAYRE NGFNIYVSDK 130 140 150 160 170 180 ISLNRSLPDI RHPNCNSKLY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 190 200 210 220 230 240 VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASAATG DVVTFLDSHC 250 260 270 280 290 300 EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 310 320 330 340 350 360 PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM 370 380 390 400 410 420 EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV 430 440 450 460 470 480 VAQKKLRVSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CTDTKLGTLG 490 500 510 520 530 540 SPLRLETCIR GRGEAAWNSM QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS 550 560 570 580 590 600 MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRVFMNTCNP SSLTQQWLFE HTNSTVLENF NKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H. DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"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: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[3]	"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] OF 76-603. Strain: C57BL/6J. Tissue: Colon.
[4]	"Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9." Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K., Balys M.M., Beres T.M., Degand P., Tabak L.A. J. Biol. Chem. 276:17395-17404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK131155 mRNA. Translation: BAD21405.1. Different initiation. BC016585 mRNA. Translation: AAH16585.1. Different initiation. BC060617 mRNA. Translation: AAH60617.1. AK033515 mRNA. Translation: BAC28334.1.
IPI	IPI00314798.
RefSeq	NP_598950.2. NM_134189.2.
UniGene	Mm.271670.
3D structure databases
ProteinModelPortal	Q6P9S7.
SMR	Q6P9S7. Positions 69-603.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q6P9S7.
Proteomic databases
PRIDE	Q6P9S7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000066987; ENSMUSP00000065096; ENSMUSG00000020520.
GeneID	171212.
KEGG	mmu:171212.
UCSC	uc007jab.1. mouse.
Organism-specific databases
CTD	55568.
MGI	MGI:1890480. Galnt10.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00680000099551.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q6P9S7.
KO	K00710.
OMA	HSRQKKT.
OrthoDB	EOG4CC40V.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q6P9S7.
Bgee	Q6P9S7.
Genevestigator	Q6P9S7.
GermOnline	ENSMUSG00000020520. 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	GALNT10. mouse.
NextBio	370706.
SOURCE	Search...

Entry information

Entry name

GLT10_MOUSE

Accession

Primary (citable) accession number: Q6P9S7
Secondary accession number(s): Q6KAQ2, Q8BZU8, Q91YJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program