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Q49A17 (GLTL6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Polypeptide N-acetylgalactosaminyltransferase-like 6
PRO_0000325774

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 601573Lumenal Potential
Domain453 – 585133Ricin B-type lectin
Region139 – 248110Catalytic subdomain A
Region306 – 36863Catalytic subdomain B

Sites

Metal binding2321Manganese By similarity
Metal binding2341Manganese By similarity
Metal binding3651Manganese By similarity
Binding site1801Substrate By similarity
Binding site2091Substrate By similarity
Binding site2331Substrate By similarity
Binding site3371Substrate By similarity
Binding site3681Substrate By similarity
Binding site3731Substrate By similarity

Amino acid modifications

Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Disulfide bond130 ↔ 360 By similarity
Disulfide bond351 ↔ 427 By similarity
Disulfide bond466 ↔ 483 By similarity
Disulfide bond518 ↔ 533 By similarity
Disulfide bond558 ↔ 573 By similarity

Natural variations

Alternative sequence1 – 4545MKRKQ…EPGEQ → MRAKFRAGAGHQRNPSISAD HGVHELVY in isoform 2.
VSP_032402

Experimental info

Sequence conflict831G → R in AAH47551. Ref.3
Sequence conflict2501A → P in AAH47551. Ref.3
Sequence conflict5631P → H in AAH47551. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: DEFBE2E41DD2FC1D

FASTA60169,788
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5A97ED40D9AB1E8F
Show »

FASTA58467,589

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_001030017.2. NM_001034845.2.
UniGeneHs.386236.

3D structure databases

ProteinModelPortalQ49A17.
SMRQ49A17. Positions 63-598.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000385382.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Polymorphism databases

DMDM296434516.

Proteomic databases

PaxDbQ49A17.
PRIDEQ49A17.

Protocols and materials databases

DNASU442117.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000506823; ENSP00000423313; ENSG00000174473. [Q49A17-1]
ENST00000508122; ENSP00000423827; ENSG00000174473. [Q49A17-2]
GeneID442117.
KEGGhsa:442117.
UCSCuc003isv.3. human. [Q49A17-1]

Organism-specific databases

CTD442117.
GeneCardsGC04P172735.
HGNCHGNC:33844. GALNTL6.
HPAHPA031019.
neXtProtNX_Q49A17.
PharmGKBPA164720162.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ49A17.
KOK00710.
OMAFAVNRKW.
OrthoDBEOG7J9VP2.
PhylomeDBQ49A17.
TreeFamTF313267.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ49A17.
BgeeQ49A17.
CleanExHS_GALNTL6.
GenevestigatorQ49A17.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi442117.
NextBio110727.
PROQ49A17.

Entry information

Entry nameGLTL6_HUMAN
AccessionPrimary (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 16, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM