Q8N3T1 (GLT15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 15
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase-like protein 2
Short name=GalNAc-T-like protein 2
Short name=pp-GaNTase-like protein 2
Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Protein-UDP acetylgalactosaminyltransferase-like protein 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2

Gene names

Name:	GALNT15
Synonyms:	GALNTL2
ORF Names:	UNQ770/PRO1564

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate.
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 membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Widely expressed. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage. Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage. Ref.1 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.
Caution	Was originally (Ref.1) termed Galnt15/pp-GaNTase 15.
Sequence caution	The sequence CAD89983.1 differs from that shown. Reason: Frameshift at positions 169, 192, 206, 222 and 270.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
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	O-glycan processing Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW transport vesicle Inferred from direct assay. Source: LIFEdb
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 – 639	639	Polypeptide N-acetylgalactosaminyltransferase 15		PRO_0000059137
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 34	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	35 – 639	605	Lumenal Potential
	Domain	504 – 631	128	Ricin B-type lectin
	Region	190 – 299	110	Catalytic subdomain A
	Region	358 – 420	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	574	1	N-linked (GlcNAc...) Potential
	Disulfide bond	517 ↔ 536		By similarity
	Disulfide bond	562 ↔ 575		By similarity
	Disulfide bond	603 ↔ 620		By similarity
Natural variations
	Natural variant	68	1	V → G. Corresponds to variant rs36026882 [ dbSNP | Ensembl ].		VAR_049243
	Natural variant	151	1	P → L. Corresponds to variant rs11715981 [ dbSNP | Ensembl ].		VAR_049244
	Natural variant	324	1	P → A. Corresponds to variant rs12634179 [ dbSNP | Ensembl ].		VAR_049245
	Natural variant	432	1	A → T. Ref.5 Ref.7 Corresponds to variant rs17851238 [ dbSNP | Ensembl ].		VAR_049246
	Natural variant	510	1	H → Y. Corresponds to variant rs2271077 [ dbSNP | Ensembl ].		VAR_019593
Experimental info
	Sequence conflict	44	1	V → D in CAD38585. Ref.5
	Sequence conflict	326	1	K → R in CAD89983. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8N3T1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: F5DCA523AF4965DA	FASTA	639	73,063
	10 20 30 40 50 60 MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK HSPEARYRLD 70 80 90 100 110 120 FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA LPQARRNQSQ GRRGGSYRLI 130 140 150 160 170 180 KQPRRQDKEA PKRDWGADED GEVSEEEELT PFSLDPRGLQ EALSARIPLQ RALPEVRHPL 190 200 210 220 230 240 CLQQHPQDSL PTASVILCFH DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS 250 260 270 280 290 300 ALSEYVARLE GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 310 320 330 340 350 360 AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK ALQSPISPIR 370 380 390 400 410 420 SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA WLCGGSVEIL PCSRVGHIYQ 430 440 450 460 470 480 NQDSHSPLDQ EATLRNRVRI AETWLGSFKE TFYKHSPEAF SLSKAEKPDC MERLQLQRRL 490 500 510 520 530 540 GCRTFHWFLA NVYPELYPSE PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR 550 560 570 580 590 600 QQQYLQHTSR KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS 610 620 630 GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15." Cheng L., Tachibana K., Iwasaki H., Kameyama A., Zhang Y., Kubota T., Hiruma T., Tachibana K., Kudo T., Guo J.-M., Narimatsu H. FEBS Lett. 566:17-24(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
[2]	"Identification and initial characterization of 5000 expressed sequenced tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA libraries." Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J., Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M., Lark M.W. Osteoarthritis Cartilage 9:641-653(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY. Tissue: Osteoarthritic cartilage.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-432. Tissue: Adipose tissue and Spinal cord.
[6]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-432.
[8]	"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]. Tissue: Brain.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase-like protein 2

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB078149 mRNA. Translation: BAD29961.1. AY035399 mRNA. Translation: AAK63127.1. AY358443 mRNA. Translation: AAQ88808.1. AK312425 mRNA. Translation: BAG35335.1. AL831925 mRNA. Translation: CAD38585.1. AL832575 mRNA. Translation: CAD89983.1. Frameshift. AC087858 Genomic DNA. No translation available. CH471055 Genomic DNA. Translation: EAW64266.1. BC014789 mRNA. Translation: AAH14789.1.
IPI	IPI00384013.
RefSeq	NP_473451.3. NM_054110.4.
UniGene	Hs.411308.
3D structure databases
ProteinModelPortal	Q8N3T1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N3T1. 1 interaction.
MINT	MINT-4724072.
STRING	9606.ENSP00000344260.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q8N3T1.
Polymorphism databases
DMDM	51316023.
Proteomic databases
PaxDb	Q8N3T1.
PRIDE	Q8N3T1.
Protocols and materials databases
DNASU	117248.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339732; ENSP00000344260; ENSG00000131386.
GeneID	117248.
KEGG	hsa:117248.
UCSC	uc003caq.4. human.
Organism-specific databases
CTD	117248.
GeneCards	GC03P016193.
HGNC	HGNC:21531. GALNT15.
HPA	HPA017076.
neXtProt	NX_Q8N3T1.
PharmGKB	PA134936170.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG282033.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q8N3T1.
KO	K00710.
OMA	ETWLGSF.
OrthoDB	EOG4W9J3Z.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8N3T1.
Bgee	Q8N3T1.
CleanEx	HS_GALNTL2.
Genevestigator	Q8N3T1.
GermOnline	ENSG00000131386. 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]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	117248.
NextBio	80182.

Entry information

Entry name

GLT15_HUMAN

Accession

Primary (citable) accession number: Q8N3T1
Secondary accession number(s): A6NMN1 , B2R638, F1LIP6, Q86T60, Q96C46, Q96DJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 29, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.