Q49A17 (GLTL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase-like 6
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 17
Short name=GalNAc-T17
Short name=pp-GaNTase 17
Protein-UDP acetylgalactosaminyltransferase 17
Putative polypeptide N-acetylgalactosaminyltransferase 17
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17

Gene names

Name:	GALNTL6
Synonyms:	GALNT17

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	601 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 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
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 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	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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: Q49A17-1)

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: Q49A17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQ → MRAKFRAGAGHQRNPSISADHGVHELVY

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 601	601	Polypeptide N-acetylgalactosaminyltransferase-like 6		PRO_0000325774
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	29 – 601	573	Lumenal Potential
	Domain	453 – 585	133	Ricin B-type lectin
	Region	139 – 248	110	Catalytic subdomain A
	Region	306 – 368	63	Catalytic subdomain B
Sites
	Metal binding	232	1	Manganese By similarity
	Metal binding	234	1	Manganese By similarity
	Metal binding	365	1	Manganese By similarity
Amino acid modifications
	Glycosylation	141	1	N-linked (GlcNAc...) Potential
	Glycosylation	588	1	N-linked (GlcNAc...) Potential
	Disulfide bond	130 ↔ 360		By similarity
	Disulfide bond	351 ↔ 427		By similarity
	Disulfide bond	466 ↔ 483		By similarity
	Disulfide bond	518 ↔ 533		By similarity
	Disulfide bond	558 ↔ 573		By similarity
Natural variations
	Alternative sequence	1 – 45	45	MKRKQ…EPGEQ → MRAKFRAGAGHQRNPSISAD HGVHELVY in isoform 2.		VSP_032402
Experimental info
	Sequence conflict	83	1	G → R in AAH47551. Ref.3
	Sequence conflict	250	1	A → P in AAH47551. Ref.3
	Sequence conflict	563	1	P → H in AAH47551. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: DEFBE2E41DD2FC1D	FASTA	601	69,788
	10 20 30 40 50 60 MKRKQKRFLQ MTLLFTVALI FLPNVGLWSL YKDKHLVKSA EPGEQQTFPL GLGDGQFYSW 70 80 90 100 110 120 TDGLRRKDWH DYESIQKEAM RSGKGEHGKP YPLTEEDHDD SAYRENGFNI FVSNNIALER 130 140 150 160 170 180 SLPDIRHANC KHKMYLERLP NTSIIIPFHN EGWTSLLRTI HSIINRTPGS LIAEIILVDD 190 200 210 220 230 240 FSEREHLKDK LEEYMARFSK VRIVRTKKRE GLIRTRLLGA SMARGEVLTF LDSHCEVNVN 250 260 270 280 290 300 WLPPLLNQIA LNHKTIVCPM IDVIDHNHFG YEAQAGDAMR GAFDWEMYYK RIPIPPELQR 310 320 330 340 350 360 ADPSDPFESP VMAGGLFAVD RKWFWELGGY DPGLEIWGGE QYEISFKVWM CGGEMFDVPC 370 380 390 400 410 420 SRVGHIYRKY VPYKVPSGTS LARNLKRVAE TWMDEFAEYI YQRRPEYRHL STGDISAQKE 430 440 450 460 470 480 LRKQLKCKDF KWFMAAVAWD VPKYYPPVEP PPAAWGEIRN VAANLCVDSK HGATGTELRL 490 500 510 520 530 540 DICVKDGSER TWSHEQLFTF GWREDIRPGE PLHTRKFCFD AISHNSPVTL YDCHGMKGNQ 550 560 570 580 590 600 LWGYRKDRTL FHPVSNSCMD CNPAEKKIFM ARCDPLSETQ QWIFEHINMT VLEKFNHHAN S
	Isoform 2 [UniParc]. Checksum: 5A97ED40D9AB1E8F	FASTA	584	67,589
	10 20 30 40 50 60 MRAKFRAGAG HQRNPSISAD HGVHELVYQT FPLGLGDGQF YSWTDGLRRK DWHDYESIQK 70 80 90 100 110 120 EAMRSGKGEH GKPYPLTEED HDDSAYRENG FNIFVSNNIA LERSLPDIRH ANCKHKMYLE 130 140 150 160 170 180 RLPNTSIIIP FHNEGWTSLL RTIHSIINRT PGSLIAEIIL VDDFSEREHL KDKLEEYMAR 190 200 210 220 230 240 FSKVRIVRTK KREGLIRTRL LGASMARGEV LTFLDSHCEV NVNWLPPLLN QIALNHKTIV 250 260 270 280 290 300 CPMIDVIDHN HFGYEAQAGD AMRGAFDWEM YYKRIPIPPE LQRADPSDPF ESPVMAGGLF 310 320 330 340 350 360 AVDRKWFWEL GGYDPGLEIW GGEQYEISFK VWMCGGEMFD VPCSRVGHIY RKYVPYKVPS 370 380 390 400 410 420 GTSLARNLKR VAETWMDEFA EYIYQRRPEY RHLSTGDISA QKELRKQLKC KDFKWFMAAV 430 440 450 460 470 480 AWDVPKYYPP VEPPPAAWGE IRNVAANLCV DSKHGATGTE LRLDICVKDG SERTWSHEQL 490 500 510 520 530 540 FTFGWREDIR PGEPLHTRKF CFDAISHNSP VTLYDCHGMK GNQLWGYRKD RTLFHPVSNS 550 560 570 580 CMDCNPAEKK IFMARCDPLS ETQQWIFEHI NMTVLEKFNH HANS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The GalNAc-transferase gene family." Bennett E.P. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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). Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ626725 mRNA. Translation: CAF25036.1. AC024706 Genomic DNA. No translation available. AC025561 Genomic DNA. No translation available. AC025821 Genomic DNA. No translation available. AC093803 Genomic DNA. No translation available. AC095045 Genomic DNA. No translation available. AC095063 Genomic DNA. No translation available. AC097496 Genomic DNA. No translation available. AC105285 Genomic DNA. No translation available. AC108064 Genomic DNA. No translation available. AC109520 Genomic DNA. No translation available. AC110776 Genomic DNA. No translation available. AC131952 Genomic DNA. No translation available. BC047551 mRNA. Translation: AAH47551.1.
IPI	IPI00454894. IPI00888755.
RefSeq	NP_001030017.2. NM_001034845.2.
UniGene	Hs.386236.
3D structure databases
HSSP	HSSP built from PDB template 2FFV based on UniProtKB Q10471.
ProteinModelPortal	Q49A17.
SMR	Q49A17. Positions 63-598.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000385382.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Polymorphism databases
DMDM	296434516.
Proteomic databases
PaxDb	Q49A17.
PRIDE	Q49A17.
Protocols and materials databases
DNASU	442117.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000506823; ENSP00000423313; ENSG00000174473. ENST00000508122; ENSP00000423827; ENSG00000174473.
GeneID	442117.
KEGG	hsa:442117.
UCSC	uc003isv.3. human.
Organism-specific databases
CTD	442117.
GeneCards	GC04P172735.
HGNC	HGNC:33844. GALNTL6.
HPA	HPA031019.
neXtProt	NX_Q49A17.
PharmGKB	PA164720162.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG239675.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q49A17.
KO	K00710.
OMA	FAVNRKW.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q49A17.
Bgee	Q49A17.
CleanEx	HS_GALNTL6.
Genevestigator	Q49A17.
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	442117.
NextBio	110727.

Entry information

Entry name

GLTL6_HUMAN

Accession

Primary (citable) accession number: Q49A17
Secondary accession number(s): Q2L4S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	May 18, 2010
Last modified:	April 3, 2013
This is version 68 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.