Reviewed, UniProtKB/Swiss-Prot Q86SR1 (GLT10_HUMAN)

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=pp-GaNTase 10
      Short name=GalNAc-T10
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10

Gene names

Name:

GALNT10

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-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	Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues. 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.
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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86SR1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q86SR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-251: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q86SR1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     354-366: WMCGGRMEDIPCS → SQLSRRPVLGTAS
     367-603: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q86SR1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-329: Missing.
     330-352: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ
     389-389: N → VRT

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 603

603

Polypeptide N-acetylgalactosaminyltransferase 10

PRO_0000059122

Regions

Topological domain

1 – 11

11

Cytoplasmic Potential

Transmembrane

12 – 31

20

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

Sites

Metal binding

237

1

Manganese

Metal binding

239

1

Manganese

Metal binding

370

1

Manganese

Binding site

185

1

Substrate

Binding site

237

1

Substrate

Amino acid modifications

Glycosylation

124

1

N-linked (GlcNAc...) Ref.7

Glycosylation

146

1

N-linked (GlcNAc...) Ref.7

Glycosylation

593

1

N-linked (GlcNAc...) Ref.7

Disulfide bond

135 ↔ 365

Ref.7

Disulfide bond

356 ↔ 432

Ref.7

Disulfide bond

471 ↔ 488

Ref.7

Disulfide bond

523 ↔ 538

Ref.7

Disulfide bond

563 ↔ 578

Ref.7

Natural variations

Alternative sequence

1 – 329

329

Missing in isoform 4.

VSP_011207

Alternative sequence

190 – 251

62

Missing in isoform 2.

VSP_011209

Alternative sequence

330 – 352

23

WELGG…EISFK → MLAWRDGELEAETSSSLFLL AMQ in isoform 4.

VSP_011208

Alternative sequence

354 – 366

13

WMCGG…DIPCS → SQLSRRPVLGTAS in isoform 3.

VSP_011212

Alternative sequence

367 – 603

237

Missing in isoform 3.

VSP_011213

Alternative sequence

389

1

N → VRT in isoform 4.

VSP_011214

Experimental info

Sequence conflict

518

1

H → Y in BAC56890. Ref.1

Sequence conflict

518

1

H → Y in BAB14676. Ref.3

Secondary structure

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603

Helix Strand Turn

Details...

Helix

77 – 84

8

Helix

91 – 93

3

Turn

100 – 103

4

Helix

106 – 109

4

Helix

115 – 119

5

Helix

133 – 136

4

Beta strand

140 – 143

4

Beta strand

147 – 155

9

Helix

158 – 171

14

Helix

174 – 176

3

Beta strand

177 – 184

8

Helix

190 – 192

3

Helix

194 – 200

7

Beta strand

206 – 210

5

Helix

217 – 227

11

Beta strand

230 – 235

6

Beta strand

238 – 242

5

Helix

248 – 256

9

Beta strand

260 – 269

10

Turn

271 – 273

3

Beta strand

285 – 288

4

Beta strand

294 – 297

4

Turn

301 – 303

3

Beta strand

319 – 325

7

Helix

326 – 331

6

Beta strand

341 – 344

4

Helix

345 – 355

11

Beta strand

359 – 370

12

Helix

386 – 397

12

Helix

399 – 401

3

Helix

402 – 406

5

Helix

410 – 412

3

Helix

421 – 430

10

Helix

435 – 441

7

Helix

446 – 449

4

Beta strand

458 – 465

8

Turn

466 – 468

3

Turn

478 – 480

3

Helix

495 – 497

3

Beta strand

503 – 505

3

Beta strand

511 – 514

4

Beta strand

528 – 532

5

Beta strand

540 – 543

4

Turn

558 – 560

3

Beta strand

563 – 566

4

Turn

568 – 570

3

Beta strand

573 – 576

4

Beta strand

587 – 591

5

Helix

594 – 597

4

Turn

598 – 601

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: EE176F6139B92573	FASTA	603	68,992
	10 20 30 40 50 60 MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA AGQGSHSRQK 70 80 90 100 110 120 KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD AERVDQAYRE NGFNIYVSDK 130 140 150 160 170 180 ISLNRSLPDI RHPNCNSKRY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 190 200 210 220 230 240 VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC 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 AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CADTKHGALG 490 500 510 520 530 540 SPLRLEGCVR GRGEAAWNNM QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS 550 560 570 580 590 600 MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF NRN
	Isoform 2. Checksum: 4216612D314EA82B	FASTA	541	61,947
	10 20 30 40 50 60 MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA AGQGSHSRQK 70 80 90 100 110 120 KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD AERVDQAYRE NGFNIYVSDK 130 140 150 160 170 180 ISLNRSLPDI RHPNCNSKRY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 190 200 210 220 230 240 VLVDDFSDRD RIARNRKTIV CPMIDVIDHD DFRYETQAGD AMRGAFDWEM YYKRIPIPPE 250 260 270 280 290 300 LQKADPSDPF ESPVMAGGLF AVDRKWFWEL GGYDPGLEIW GGEQYEISFK VWMCGGRMED 310 320 330 340 350 360 IPCSRVGHIY RKYVPYKVPA GVSLARNLKR VAEVWMDEYA EYIYQRRPEY RHLSAGDVAV 370 380 390 400 410 420 QKKLRSSLNC KSFKWFMTKI AWDLPKFYPP VEPPAAAWGE IRNVGTGLCA DTKHGALGSP 430 440 450 460 470 480 LRLEGCVRGR GEAAWNNMQV FTFTWREDIR PGDPQHTKKF CFDAISHTSP VTLYDCHSMK 490 500 510 520 530 540 GNQLWKYRKD KTLYHPVSGS CMDCSESDHR IFMNTCNPSS LTQQWLFEHT NSTVLEKFNR N
	Isoform 3. Checksum: 52AB23ABC6F797FE	FASTA	366	41,452
	10 20 30 40 50 60 MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA AGQGSHSRQK 70 80 90 100 110 120 KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD AERVDQAYRE NGFNIYVSDK 130 140 150 160 170 180 ISLNRSLPDI RHPNCNSKRY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI 190 200 210 220 230 240 VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC 250 260 270 280 290 300 EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 310 320 330 340 350 360 PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVSQLSRRP VLGTAS
	Isoform 4. Checksum: F357AFF828E57DC7	FASTA	276	31,833
	10 20 30 40 50 60 MLAWRDGELE AETSSSLFLL AMQVWMCGGR MEDIPCSRVG HIYRKYVPYK VPAGVSLARV 70 80 90 100 110 120 RTLKRVAEVW MDEYAEYIYQ RRPEYRHLSA GDVAVQKKLR SSLNCKSFKW FMTKIAWDLP 130 140 150 160 170 180 KFYPPVEPPA AAWGEIRNVG TGLCADTKHG ALGSPLRLEG CVRGRGEAAW NNMQVFTFTW 190 200 210 220 230 240 REDIRPGDPQ HTKKFCFDAI SHTSPVTLYD CHSMKGNQLW KYRKDKTLYH PVSGSCMDCS 250 260 270 ESDHRIFMNT CNPSSLTQQW LFEHTNSTVL EKFNRN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10." Cheng L., Tachibana K., Zhang Y., Guo J.-M., Tachibana K.K., Kameyama A., Wang H., Hiruma T., Iwasaki H., Togayachi A., Kudo T., Narimatsu H. FEBS Lett. 531:115-121(2002) [PubMed: 12417297] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY. Tissue: Colon cancer.
[2]	Bennett E.P. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-603 (ISOFORM 2). Tissue: Brain and Placenta.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterus.
[5]	"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones." Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O. DNA Res. 10:49-57(2003) [PubMed: 12693554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-366 (ISOFORM 3). Tissue: Spleen.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-603 (ISOFORM 1). Tissue: Kidney and Skin.
[7]	"Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)." Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R., Wakatsuki S., Narimatsu H. J. Mol. Biol. 359:708-727(2006) [PubMed: 16650853] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITH UDP-GALNAC AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES, GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB078145 mRNA. Translation: BAC56890.1.
AJ505950 mRNA. Translation: CAD44532.1.
AK023782 mRNA. Translation: BAB14676.1. Different initiation.
AK127135 mRNA. Translation: BAG54441.1.
AL096739 mRNA. Translation: CAB46378.1.
AK074132 mRNA. Translation: BAB84958.1.
BC007224 mRNA. Translation: AAH07224.2.
BC072450 mRNA. Translation: AAH72450.1.

IPI

IPI00303783.
IPI00375205.
IPI00456478.
IPI00456479.

PIR

T12552.

RefSeq

NP_060010.3.
NP_938080.1.

UniGene

Hs.651323
Hs.655011

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D7I	X-ray	2.50	A	40-603	[»]
2D7R	X-ray	2.80	A	40-603	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSite

Q86SR1.

Proteomic databases

PRIDE

Q86SR1.

Genome annotation databases

Ensembl

ENSG00000164574. Homo sapiens. [Contig view]

GeneID

55568.

KEGG

hsa:55568.

Organism-specific databases

GeneCards

GC05P153550.

H-InvDB

HIX0005339.

HGNC

HGNC:19873. GALNT10.

HPA

HPA007525.

MIM

608043. gene.

PharmGKB

PA134870832.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q86SR1.

OMA

Q86SR1. SHSRQKK.

Enzyme and pathway databases

BRENDA

2.4.1.41. 247.

Gene expression databases

ArrayExpress

Q86SR1.

Bgee

Q86SR1.

GermOnline

ENSG00000164574. Homo sapiens.

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

NextBio

60056.

SOURCE

Search...

Entry information

Entry name

GLT10_HUMAN

Accession

Primary (citable) accession number: Q86SR1
Secondary accession number(s): B3KXC9 , Q6IN56, Q86VP8, Q8IXJ2, Q8TEJ2, Q96IV2, Q9H8E1, Q9Y4M4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)