Q80VA0 (GALT7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Galnt7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
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.
Tissue specificity	Highly expressed in sublingual gland. Expressed at lower level in stomach, small intestiine and colon. Ref.4
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.
Sequence caution	The sequence AAH07484.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein O-linked glycosylation Inferred from direct assay PubMed 11278534. Source: MGI
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay PubMed 11278534. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q80VA0-1)

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: Q80VA0-2)

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

Isoform 3 (identifier: Q80VA0-3)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	N-acetylgalactosaminyltransferase 7		PRO_0000059117
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 657	628	Lumenal Potential
	Domain	532 – 652	121	Ricin B-type lectin
	Region	206 – 317	112	Catalytic subdomain A
	Region	381 – 443	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	545 ↔ 562		By similarity
	Disulfide bond	585 ↔ 600		By similarity
	Disulfide bond	625 ↔ 640		By similarity
Natural variations
	Alternative sequence	323 – 377	55	TICTV…RLRKT → ATCTVPLIDYIDGNDYSIEP QQGGDEDGFARGAWDWSMLW KRIPLSHKEKAKRKH in isoform 2 and isoform 3.		VSP_011204
	Alternative sequence	384 – 657	274	Missing in isoform 3.		VSP_011205
Experimental info
	Sequence conflict	316	1	A → P in BAC28284. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 51B6F3B17E77E703	FASTA	657	75,419
	10 20 30 40 50 60 MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDQSPLSR MREDRDVNNP LPNRGGNGLA 70 80 90 100 110 120 PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG GDSQRDVMQR QYLTFKPQTF 130 140 150 160 170 180 TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG EKAKPLVLGP EYKQAVQASI KEFGFNMVAS 190 200 210 220 230 240 DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA 250 260 270 280 290 300 EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL 310 320 330 340 350 360 DAHCEVAVNW YAPLVAPISK DRTICTVPII DVISGNTYEI IPQGGGDEDG YARGAWDWSM 370 380 390 400 410 420 LWKRVPLTSR EKRLRKTKTE PYRSPAMAGG LFAIEKDFFF ELGLYDPGLQ IWGGENFEIS 430 440 450 460 470 480 YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF 490 500 510 520 530 540 YASRPESKAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL 550 560 570 580 590 600 ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC 610 620 630 640 650 NLNEFKEWQY FKSLHRFTHI TSGKCLDRSE VLHQVFISTC DSSKMTQKWE MNNIHSV
	Isoform 2 [UniParc]. Checksum: 0943CAEF352AF3F1	FASTA	657	75,500
	10 20 30 40 50 60 MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDQSPLSR MREDRDVNNP LPNRGGNGLA 70 80 90 100 110 120 PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG GDSQRDVMQR QYLTFKPQTF 130 140 150 160 170 180 TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG EKAKPLVLGP EYKQAVQASI KEFGFNMVAS 190 200 210 220 230 240 DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA 250 260 270 280 290 300 EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL 310 320 330 340 350 360 DAHCEVAVNW YAPLVAPISK DRATCTVPLI DYIDGNDYSI EPQQGGDEDG FARGAWDWSM 370 380 390 400 410 420 LWKRIPLSHK EKAKRKHKTE PYRSPAMAGG LFAIEKDFFF ELGLYDPGLQ IWGGENFEIS 430 440 450 460 470 480 YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF 490 500 510 520 530 540 YASRPESKAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL 550 560 570 580 590 600 ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC 610 620 630 640 650 NLNEFKEWQY FKSLHRFTHI TSGKCLDRSE VLHQVFISTC DSSKMTQKWE MNNIHSV
	Isoform 3 [UniParc]. Checksum: 8D858DA7EDFEF62D	FASTA	383	43,781
	10 20 30 40 50 60 MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDQSPLSR MREDRDVNNP LPNRGGNGLA 70 80 90 100 110 120 PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG GDSQRDVMQR QYLTFKPQTF 130 140 150 160 170 180 TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG EKAKPLVLGP EYKQAVQASI KEFGFNMVAS 190 200 210 220 230 240 DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA 250 260 270 280 290 300 EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL 310 320 330 340 350 360 DAHCEVAVNW YAPLVAPISK DRATCTVPLI DYIDGNDYSI EPQQGGDEDG FARGAWDWSM 370 380 LWKRIPLSHK EKAKRKHKTE PYR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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/6 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.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

N-acetylgalactosaminyltransferase 7

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00117611. IPI00227374. IPI00457459.
RefSeq	NP_001161453.1. NM_001167981.1. NP_653332.3. NM_144731.4.
UniGene	Mm.62886.
3D structure databases
ProteinModelPortal	Q80VA0.
SMR	Q80VA0. Positions 148-656.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q80VA0.
Proteomic databases
PaxDb	Q80VA0.
PRIDE	Q80VA0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034021; ENSMUSP00000034021; ENSMUSG00000031608. ENSMUST00000110316; ENSMUSP00000105945; ENSMUSG00000031608.
GeneID	108150.
KEGG	mmu:108150.
UCSC	uc009lsy.2. mouse. uc009lsz.2. mouse. uc009lta.2. mouse.
Organism-specific databases
CTD	51809.
MGI	MGI:1349449. Galnt7.
Phylogenomic databases
eggNOG	NOG248127.
GeneTree	ENSGT00680000099551.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
KO	K00710.
OMA	NIEWGEI.
OrthoDB	EOG44MXRP.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q80VA0.
Bgee	Q80VA0.
Genevestigator	Q80VA0.
GermOnline	ENSMUSG00000031608. Mus musculus.
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
ChiTaRS	GALNT7. mouse.
NextBio	360166.
SOURCE	Search...

Entry information

Entry name

GALT7_MOUSE

Accession

Primary (citable) accession number: Q80VA0
Secondary accession number(s): Q8BY62 , Q8BZ70, Q8BZW0, Q91VW6, Q99MD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program