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Protein

N-acetylgalactosaminyltransferase 7

Gene

Galnt7

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

Functioni

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified (By similarity).By similarity

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity
Metal bindingi301 – 3011ManganeseBy similarity
Metal bindingi303 – 3031ManganeseBy similarity
Binding sitei412 – 4121SubstrateBy similarity
Metal bindingi440 – 4401ManganeseBy similarity
Binding sitei443 – 4431SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • protein O-linked glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylgalactosaminyltransferase 7 (EC:2.4.1.-)
Alternative name(s):
Polypeptide GalNAc transferase 7
Short name:
GalNAc-T7
Short name:
pp-GaNTase 7
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Gene namesi
Name:Galnt7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1349449. Galnt7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 657628LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657N-acetylgalactosaminyltransferase 7PRO_0000059117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi197 ↔ 435PROSITE-ProRule annotation
Disulfide bondi426 ↔ 507PROSITE-ProRule annotation
Disulfide bondi545 ↔ 562PROSITE-ProRule annotation
Disulfide bondi585 ↔ 600PROSITE-ProRule annotation
Disulfide bondi625 ↔ 640PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ80VA0.
MaxQBiQ80VA0.
PaxDbiQ80VA0.
PeptideAtlasiQ80VA0.
PRIDEiQ80VA0.

PTM databases

iPTMnetiQ80VA0.
PhosphoSiteiQ80VA0.

Expressioni

Tissue specificityi

Highly expressed in sublingual gland. Expressed at lower level in stomach, small intestiine and colon.1 Publication

Gene expression databases

BgeeiQ80VA0.
GenevisibleiQ80VA0. MM.

Interactioni

Protein-protein interaction databases

IntActiQ80VA0. 1 interaction.
MINTiMINT-4095546.
STRINGi10090.ENSMUSP00000034021.

Structurei

3D structure databases

ProteinModelPortaliQ80VA0.
SMRiQ80VA0. Positions 148-656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 652121Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 317112Catalytic subdomain AAdd
BLAST
Regioni381 – 44363Catalytic 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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ80VA0.
KOiK00710.
OMAiIQRQYLT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ80VA0.
TreeFamiTF352176.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80VA0-1) [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
MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDQSPLSR MREDRDVNNP
60 70 80 90 100
LPNRGGNGLA PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG
110 120 130 140 150
GDSQRDVMQR QYLTFKPQTF TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG
160 170 180 190 200
EKAKPLVLGP EYKQAVQASI KEFGFNMVAS DMISLDRSVN DLRQEECKYW
210 220 230 240 250
HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA EIVLIDDFSN
260 270 280 290 300
KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
310 320 330 340 350
DAHCEVAVNW YAPLVAPISK DRTICTVPII DVISGNTYEI IPQGGGDEDG
360 370 380 390 400
YARGAWDWSM LWKRVPLTSR EKRLRKTKTE PYRSPAMAGG LFAIEKDFFF
410 420 430 440 450
ELGLYDPGLQ IWGGENFEIS YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN
460 470 480 490 500
PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF YASRPESKAL PYGDISELKK
510 520 530 540 550
FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL ETAYCIDSMG
560 570 580 590 600
KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC
610 620 630 640 650
NLNEFKEWQY FKSLHRFTHI TSGKCLDRSE VLHQVFISTC DSSKMTQKWE

MNNIHSV
Length:657
Mass (Da):75,419
Last modified:August 16, 2004 - v2
Checksum:i51B6F3B17E77E703
GO
Isoform 2 (identifier: Q80VA0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     323-377: TICTVPIIDV...TSREKRLRKT → ATCTVPLIDY...SHKEKAKRKH

Show »
Length:657
Mass (Da):75,500
Checksum:i0943CAEF352AF3F1
GO
Isoform 3 (identifier: Q80VA0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     323-377: TICTVPIIDV...TSREKRLRKT → ATCTVPLIDY...SHKEKAKRKH
     384-657: Missing.

Note: No experimental confirmation available.
Show »
Length:383
Mass (Da):43,781
Checksum:i8D858DA7EDFEF62D
GO

Sequence cautioni

The sequence AAH07484.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti316 – 3161A → P in BAC28284 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei323 – 37755TICTV…RLRKT → ATCTVPLIDYIDGNDYSIEP QQGGDEDGFARGAWDWSMLW KRIPLSHKEKAKRKH in isoform 2 and isoform 3. 1 PublicationVSP_011204Add
BLAST
Alternative sequencei384 – 657274Missing in isoform 3. 1 PublicationVSP_011205Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF349573 mRNA. Translation: AAK37549.1.
AK033427 mRNA. Translation: BAC28284.1.
AK036523 mRNA. Translation: BAC29461.1.
AK041791 mRNA. Translation: BAC31068.1.
BC007484 mRNA. Translation: AAH07484.1. Different initiation.
BC049907 mRNA. Translation: AAH49907.1.
BC052461 mRNA. Translation: AAH52461.1.
CCDSiCCDS22317.1. [Q80VA0-1]
CCDS52552.1. [Q80VA0-2]
RefSeqiNP_001161453.1. NM_001167981.1. [Q80VA0-2]
NP_653332.3. NM_144731.4. [Q80VA0-1]
UniGeneiMm.62886.

Genome annotation databases

EnsembliENSMUST00000034021; ENSMUSP00000034021; ENSMUSG00000031608. [Q80VA0-1]
ENSMUST00000110316; ENSMUSP00000105945; ENSMUSG00000031608. [Q80VA0-2]
GeneIDi108150.
KEGGimmu:108150.
UCSCiuc009lsy.2. mouse. [Q80VA0-1]
uc009lsz.2. mouse. [Q80VA0-2]
uc009lta.2. mouse. [Q80VA0-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

N-acetylgalactosaminyltransferase 7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF349573 mRNA. Translation: AAK37549.1.
AK033427 mRNA. Translation: BAC28284.1.
AK036523 mRNA. Translation: BAC29461.1.
AK041791 mRNA. Translation: BAC31068.1.
BC007484 mRNA. Translation: AAH07484.1. Different initiation.
BC049907 mRNA. Translation: AAH49907.1.
BC052461 mRNA. Translation: AAH52461.1.
CCDSiCCDS22317.1. [Q80VA0-1]
CCDS52552.1. [Q80VA0-2]
RefSeqiNP_001161453.1. NM_001167981.1. [Q80VA0-2]
NP_653332.3. NM_144731.4. [Q80VA0-1]
UniGeneiMm.62886.

3D structure databases

ProteinModelPortaliQ80VA0.
SMRiQ80VA0. Positions 148-656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80VA0. 1 interaction.
MINTiMINT-4095546.
STRINGi10090.ENSMUSP00000034021.

Protein family/group databases

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

PTM databases

iPTMnetiQ80VA0.
PhosphoSiteiQ80VA0.

Proteomic databases

EPDiQ80VA0.
MaxQBiQ80VA0.
PaxDbiQ80VA0.
PeptideAtlasiQ80VA0.
PRIDEiQ80VA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034021; ENSMUSP00000034021; ENSMUSG00000031608. [Q80VA0-1]
ENSMUST00000110316; ENSMUSP00000105945; ENSMUSG00000031608. [Q80VA0-2]
GeneIDi108150.
KEGGimmu:108150.
UCSCiuc009lsy.2. mouse. [Q80VA0-1]
uc009lsz.2. mouse. [Q80VA0-2]
uc009lta.2. mouse. [Q80VA0-3]

Organism-specific databases

CTDi51809.
MGIiMGI:1349449. Galnt7.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ80VA0.
KOiK00710.
OMAiIQRQYLT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ80VA0.
TreeFamiTF352176.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGalnt7. mouse.
PROiQ80VA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ80VA0.
GenevisibleiQ80VA0. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and acceptor specificity of the murine UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T7."
    Kanoh A., Miyahara N., Irimura T.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  2. "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] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Bone, Colon and Thymus.
  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).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary tumor.
  4. "Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity."
    Ten Hagen K.G., Tetaert D., Hagen F.K., Richet C., Beres T.B., Gagnon J., Balys M.M., VanWuyckhuyse B., Bedi G.S., Degand P., Tabak L.A.
    J. Biol. Chem. 274:27867-27874(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas.

Entry informationi

Entry nameiGALT7_MOUSE
AccessioniPrimary (citable) accession number: Q80VA0
Secondary accession number(s): Q8BY62
, Q8BZ70, Q8BZW0, Q91VW6, Q99MD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.