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Q7TT15 (GLTL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase-like protein 3
Short name=GalNAc-T-like protein 3
Short name=pp-GaNTase-like protein 3
Protein-UDP acetylgalactosaminyltransferase-like protein 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
Williams-Beuren syndrome chromosomal region 17 protein homolog
Gene names
Name:Wbscr17
Synonyms:Galntl3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7TT15-1)

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: Q7TT15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     194-196: SDE → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
PRO_0000059140

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 598571Lumenal Potential
Domain465 – 594130Ricin B-type lectin
Region151 – 262112Catalytic subdomain A
Region319 – 38163Catalytic subdomain B

Sites

Metal binding2461Manganese By similarity
Metal binding2481Manganese By similarity
Metal binding3781Manganese By similarity
Binding site1921Substrate By similarity
Binding site2231Substrate By similarity
Binding site3811Substrate By similarity
Binding site3861Substrate By similarity

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Disulfide bond142 ↔ 373 By similarity
Disulfide bond364 ↔ 443 By similarity
Disulfide bond478 ↔ 494 By similarity
Disulfide bond526 ↔ 541 By similarity
Disulfide bond568 ↔ 586 By similarity

Natural variations

Alternative sequence194 – 1963SDE → R in isoform 2.
VSP_011232

Experimental info

Sequence conflict741V → D in BAC33446. Ref.3
Sequence conflict2241E → D in BAC33446. Ref.3
Sequence conflict2641Q → K in BAC33446. Ref.3

Sequences

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

Last modified October 1, 2003. Version 1.
Checksum: 66F91B355EF571F5

FASTA59867,691
        10         20         30         40         50         60 
MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ 

        70         80         90        100        110        120 
DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPSEEEK AKGPHEKYGY 

       130        140        150        160        170        180 
NSYLSEKISL DRSIPDYRPT KCKELKYSKE LPQISIIFIF VNEALSVILR SVHSAVNHTP 

       190        200        210        220        230        240 
THLLKEIILV DDNSDEEELK APLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKAATGQ 

       250        260        270        280        290        300 
VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW 

       310        320        330        340        350        360 
CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK 

       370        380        390        400        410        420 
VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP 

       430        440        450        460        470        480 
LENPGIDIGD VSERKALRKS LKCKNFQWYL DHVYPEMRRY NNTIAYGELR NNKAKDVCLD 

       490        500        510        520        530        540 
QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD 

       550        560        570        580        590 
CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WAIKNPIK 

« Hide

Isoform 2 [UniParc].

Checksum: 2907521731EFC58D
Show »

FASTA59667,516

References

« Hide 'large scale' references
[1]"Identification of additional transcripts in the Williams-Beuren syndrome critical region."
Merla G., Ucla C., Guipponi M., Reymond A.
Hum. Genet. 110:429-438(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"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).
Strain: C57BL/6.
Tissue: Brain.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-455 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Cerebellum and Embryonic spinal ganglion.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 128-143, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF467979 mRNA. Translation: AAM62404.1.
AK035817 mRNA. Translation: BAC29197.1.
AK048758 mRNA. Translation: BAC33446.2.
AK051281 mRNA. Translation: BAC34591.2.
BC052469 mRNA. Translation: AAH52469.1.
CCDSCCDS39296.1. [Q7TT15-1]
RefSeqNP_660253.2. NM_145218.3. [Q7TT15-1]
UniGeneMm.299204.

3D structure databases

ProteinModelPortalQ7TT15.
SMRQ7TT15. Positions 93-595.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

PhosphoSiteQ7TT15.

Proteomic databases

PaxDbQ7TT15.
PRIDEQ7TT15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040. [Q7TT15-1]
GeneID212996.
KEGGmmu:212996.
UCSCuc008zuq.1. mouse. [Q7TT15-1]

Organism-specific databases

CTD64409.
MGIMGI:2137594. Wbscr17.

Phylogenomic databases

eggNOGNOG259711.
GeneTreeENSGT00670000097647.
HOGENOMHOG000038228.
HOVERGENHBG051699.
InParanoidQ7TT15.
KOK00710.
OMARYENSGH.
OrthoDBEOG7JX33Q.
PhylomeDBQ7TT15.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ7TT15.
GenevestigatorQ7TT15.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373790.
PROQ7TT15.
SOURCESearch...

Entry information

Entry nameGLTL3_MOUSE
AccessionPrimary (citable) accession number: Q7TT15
Secondary accession number(s): Q8BKN7 expand/collapse secondary AC list , Q8BUY1, Q8BX73, Q8BZC8, Q8K483
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot