Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7TT15

- GLTL3_MOUSE

UniProt

Q7TT15 - GLTL3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Gene

Wbscr17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactori

Manganese.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921SubstrateBy similarity
Binding sitei223 – 2231SubstrateBy similarity
Metal bindingi246 – 2461ManganeseBy similarity
Metal bindingi248 – 2481ManganeseBy similarity
Metal bindingi378 – 3781ManganeseBy similarity
Binding sitei381 – 3811SubstrateBy similarity
Binding sitei386 – 3861SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Wbscr17
Synonyms:Galntl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2137594. Wbscr17.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3PRO_0000059140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi142 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 443PROSITE-ProRule annotation
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi478 ↔ 494PROSITE-ProRule annotation
Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi526 ↔ 541PROSITE-ProRule annotation
Disulfide bondi568 ↔ 586PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ7TT15.
PaxDbiQ7TT15.
PRIDEiQ7TT15.

PTM databases

PhosphoSiteiQ7TT15.

Expressioni

Gene expression databases

BgeeiQ7TT15.
ExpressionAtlasiQ7TT15. baseline and differential.
GenevestigatoriQ7TT15.

Structurei

3D structure databases

ProteinModelPortaliQ7TT15.
SMRiQ7TT15. Positions 93-591.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini28 – 598571LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini465 – 594130Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 262112Catalytic subdomain AAdd
BLAST
Regioni319 – 38163Catalytic subdomain BAdd
BLAST

Domaini

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 similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG259711.
GeneTreeiENSGT00670000097647.
HOGENOMiHOG000038228.
HOVERGENiHBG051699.
InParanoidiQ7TT15.
KOiK00710.
OMAiRYENSGH.
OrthoDBiEOG7JX33Q.
PhylomeDBiQ7TT15.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7TT15-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN
60 70 80 90 100
LSAHSASPIQ DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP
110 120 130 140 150
ATLSPSEEEK AKGPHEKYGY NSYLSEKISL DRSIPDYRPT KCKELKYSKE
160 170 180 190 200
LPQISIIFIF VNEALSVILR SVHSAVNHTP THLLKEIILV DDNSDEEELK
210 220 230 240 250
APLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKAATGQ VTGFFDAHVE
260 270 280 290 300
FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW
310 320 330 340 350
CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY
360 370 380 390 400
GGENIELGIK VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR
410 420 430 440 450
VAEVWMDDYK SHVYIAWNLP LENPGIDIGD VSERKALRKS LKCKNFQWYL
460 470 480 490 500
DHVYPEMRRY NNTIAYGELR NNKAKDVCLD QGPLENHTAI LYPCHGWGPQ
510 520 530 540 550
LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD CDKVKSSLYK
560 570 580 590
RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WAIKNPIK
Length:598
Mass (Da):67,691
Last modified:October 1, 2003 - v1
Checksum:i66F91B355EF571F5
GO
Isoform 2 (identifier: Q7TT15-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:596
Mass (Da):67,516
Checksum:i2907521731EFC58D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741V → D in BAC33446. (PubMed:16141072)Curated
Sequence conflicti224 – 2241E → D in BAC33446. (PubMed:16141072)Curated
Sequence conflicti264 – 2641Q → K in BAC33446. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei194 – 1963SDE → R in isoform 2. 1 PublicationVSP_011232

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS39296.1. [Q7TT15-1]
RefSeqiNP_660253.2. NM_145218.3. [Q7TT15-1]
UniGeneiMm.299204.

Genome annotation databases

EnsembliENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040. [Q7TT15-1]
GeneIDi212996.
KEGGimmu:212996.
UCSCiuc008zuq.1. mouse. [Q7TT15-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS39296.1. [Q7TT15-1 ]
RefSeqi NP_660253.2. NM_145218.3. [Q7TT15-1 ]
UniGenei Mm.299204.

3D structure databases

ProteinModelPortali Q7TT15.
SMRi Q7TT15. Positions 93-591.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSitei Q7TT15.

Proteomic databases

MaxQBi Q7TT15.
PaxDbi Q7TT15.
PRIDEi Q7TT15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000086023 ; ENSMUSP00000083187 ; ENSMUSG00000034040 . [Q7TT15-1 ]
GeneIDi 212996.
KEGGi mmu:212996.
UCSCi uc008zuq.1. mouse. [Q7TT15-1 ]

Organism-specific databases

CTDi 64409.
MGIi MGI:2137594. Wbscr17.

Phylogenomic databases

eggNOGi NOG259711.
GeneTreei ENSGT00670000097647.
HOGENOMi HOG000038228.
HOVERGENi HBG051699.
InParanoidi Q7TT15.
KOi K00710.
OMAi RYENSGH.
OrthoDBi EOG7JX33Q.
PhylomeDBi Q7TT15.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

NextBioi 373790.
PROi Q7TT15.
SOURCEi Search...

Gene expression databases

Bgeei Q7TT15.
ExpressionAtlasi Q7TT15. baseline and differential.
Genevestigatori Q7TT15.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGLTL3_MOUSE
AccessioniPrimary (citable) accession number: Q7TT15
Secondary accession number(s): Q8BKN7
, Q8BUY1, Q8BX73, Q8BZC8, Q8K483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3