Q8N428 (GLT16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 16
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase-like protein 1
Short name=GalNAc-T-like protein 1
Short name=pp-GaNTase-like protein 1
Polypeptide N-acetylgalactosaminyltransferase-like protein 1
Protein-UDP acetylgalactosaminyltransferase-like protein 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1

Gene names

Name:	GALNT16
Synonyms:	GALNTL1, KIAA1130

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	558 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May catalyze 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 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.
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.
Sequence caution	The sequence BAA86444.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N428-1)

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: Q8N428-2)

The sequence of this isoform differs from the canonical sequence as follows:
     514-558: KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT → VSLLASGPEAQQPEGPCLRVADLGRRAPD

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Polypeptide N-acetylgalactosaminyltransferase 16		PRO_0000059135
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 26	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 558	532	Lumenal Potential
	Domain	428 – 555	128	Ricin B-type lectin
	Region	122 – 227	106	Catalytic subdomain A
	Region	286 – 348	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	441 ↔ 460		By similarity
	Disulfide bond	486 ↔ 506		By similarity
	Disulfide bond	530 ↔ 543		By similarity
Natural variations
	Alternative sequence	514 – 558	45	KWRRK…LLPHT → VSLLASGPEAQQPEGPCLRV ADLGRRAPD in isoform 2.		VSP_011231
	Natural variant	201	1	V → M. Ref.2 Ref.3 Corresponds to variant rs12879377 [ dbSNP | Ensembl ].		VAR_055848
	Natural variant	497	1	P → S. Corresponds to variant rs59840366 [ dbSNP | Ensembl ].		VAR_061195

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: FF35C5606B5291B8	FASTA	558	63,074
	10 20 30 40 50 60 MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL REDRTIPLIV 70 80 90 100 110 120 TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS PDRPIRDTRH YSCPSVSYSS 130 140 150 160 170 180 DLPATSVIIT FHNEARSTLL RTVKSVLNRT PANLIQEIIL VDDFSSDPED CLLLTRIPKV 190 200 210 220 230 240 KCLRNDRREG LIRSRVRGAD VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII 250 260 270 280 290 300 DVISLDNFAY LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID 310 320 330 340 350 360 KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR HPYNFPEGNA 370 380 390 400 410 420 LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR IEQRKKMNCK SFRWYLENVY 430 440 450 460 470 480 PELTVPVKEA LPGIIKQGVN CLESQGQNTA GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI 490 500 510 520 530 540 QQQGKCLAAT STLMSSPGSP VILQMCNPRE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT 550 SKCQADAQAQ QWQLLPHT
	Isoform 2 [UniParc]. Checksum: 1E517B517B2568A9	FASTA	542	60,972
	10 20 30 40 50 60 MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL REDRTIPLIV 70 80 90 100 110 120 TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS PDRPIRDTRH YSCPSVSYSS 130 140 150 160 170 180 DLPATSVIIT FHNEARSTLL RTVKSVLNRT PANLIQEIIL VDDFSSDPED CLLLTRIPKV 190 200 210 220 230 240 KCLRNDRREG LIRSRVRGAD VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII 250 260 270 280 290 300 DVISLDNFAY LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID 310 320 330 340 350 360 KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR HPYNFPEGNA 370 380 390 400 410 420 LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR IEQRKKMNCK SFRWYLENVY 430 440 450 460 470 480 PELTVPVKEA LPGIIKQGVN CLESQGQNTA GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI 490 500 510 520 530 540 QQQGKCLAAT STLMSSPGSP VILQMCNPRE GKQVSLLASG PEAQQPEGPC LRVADLGRRA PD

References

[1]	"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain." Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O. DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[2]	"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] (ISOFORM 1), VARIANT MET-201. Tissue: Brain.
[3]	"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] (ISOFORM 1), VARIANT MET-201. Tissue: Brain and Chondrosarcoma.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB032956 mRNA. Translation: BAA86444.1. Different initiation. AK289745 mRNA. Translation: BAF82434.1. BC036812 mRNA. Translation: AAH36812.2. BC098578 mRNA. Translation: AAH98578.1.
IPI	IPI00166613. IPI00456715.
RefSeq	NP_001161840.1. NM_001168368.1. NP_065743.2. NM_020692.2.
UniGene	Hs.21035.
3D structure databases
ProteinModelPortal	Q8N428.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000336729.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q8N428.
Polymorphism databases
DMDM	51316024.
Proteomic databases
PaxDb	Q8N428.
PRIDE	Q8N428.
Protocols and materials databases
DNASU	57452.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000337827; ENSP00000336729; ENSG00000100626. ENST00000448469; ENSP00000402970; ENSG00000100626. ENST00000553471; ENSP00000451420; ENSG00000100626. ENST00000553669; ENSP00000451200; ENSG00000100626.
GeneID	57452.
KEGG	hsa:57452.
UCSC	uc001xlb.2. human.
Organism-specific databases
CTD	57452.
GeneCards	GC14P069726.
HGNC	HGNC:23233. GALNT16.
neXtProt	NX_Q8N428.
PharmGKB	PA134991608.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG239675.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q8N428.
KO	K00710.
OMA	PEDCQLL.
OrthoDB	EOG4DZ1V4.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8N428.
Bgee	Q8N428.
CleanEx	HS_GALNTL1.
Genevestigator	Q8N428.
GermOnline	ENSG00000100626. Homo sapiens.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2_met. IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF02709. Glyco_transf_7C. 1 hit. 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	57452.
NextBio	63624.

Entry information

Entry name

GLT16_HUMAN

Accession

Primary (citable) accession number: Q8N428
Secondary accession number(s): Q4KMG3, Q9ULT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 99 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.