GALT7_MOUSE
ID GALT7_MOUSE Reviewed; 657 AA.
AC Q80VA0; Q8BY62; Q8BZ70; Q8BZW0; Q91VW6; Q99MD7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=N-acetylgalactosaminyltransferase 7;
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q86SF2};
DE AltName: Full=Polypeptide GalNAc transferase 7;
DE Short=GalNAc-T7;
DE Short=pp-GaNTase 7;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7;
GN Name=Galnt7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Kanoh A., Miyahara N., Irimura T.;
RT "Molecular cloning and acceptor specificity of the murine UDP-GalNAc:
RT polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T7.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Bone, Colon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10488133; DOI=10.1074/jbc.274.39.27867;
RA Ten Hagen K.G., Tetaert D., Hagen F.K., Richet C., Beres T.B., Gagnon J.,
RA Balys M.M., VanWuyckhuyse B., Bedi G.S., Degand P., Tabak L.A.;
RT "Characterization of a UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase that displays glycopeptide N-
RT acetylgalactosaminyltransferase activity.";
RL J. Biol. Chem. 274:27867-27874(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide
CC biosynthesis, which catalyzes the transfer of an N-acetyl-D-
CC galactosamine residue to an already glycosylated peptide. In contrast
CC to other proteins of the family, it does not act as a peptide
CC transferase that transfers GalNAc onto serine or threonine residue on
CC the protein receptor, but instead requires the prior addition of a
CC GalNAc on a peptide before adding additional GalNAc moieties. Some
CC peptide transferase activity is however not excluded, considering that
CC its appropriate peptide substrate may remain unidentified (By
CC similarity). {ECO:0000250|UniProtKB:Q86SF2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000250|UniProtKB:Q86SF2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000250|UniProtKB:Q86SF2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q86SF2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80VA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80VA0-2; Sequence=VSP_011204;
CC Name=3;
CC IsoId=Q80VA0-3; Sequence=VSP_011204, VSP_011205;
CC -!- TISSUE SPECIFICITY: Highly expressed in sublingual gland. Expressed at
CC lower level in stomach, small intestiine and colon.
CC {ECO:0000269|PubMed:10488133}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07484.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=N-
CC acetylgalactosaminyltransferase 7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_516";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF349573; AAK37549.1; -; mRNA.
DR EMBL; AK033427; BAC28284.1; -; mRNA.
DR EMBL; AK036523; BAC29461.1; -; mRNA.
DR EMBL; AK041791; BAC31068.1; -; mRNA.
DR EMBL; BC007484; AAH07484.1; ALT_INIT; mRNA.
DR EMBL; BC049907; AAH49907.1; -; mRNA.
DR EMBL; BC052461; AAH52461.1; -; mRNA.
DR CCDS; CCDS22317.1; -. [Q80VA0-1]
DR CCDS; CCDS52552.1; -. [Q80VA0-2]
DR RefSeq; NP_001161453.1; NM_001167981.1. [Q80VA0-2]
DR RefSeq; NP_653332.3; NM_144731.4. [Q80VA0-1]
DR AlphaFoldDB; Q80VA0; -.
DR SMR; Q80VA0; -.
DR BioGRID; 223866; 2.
DR IntAct; Q80VA0; 1.
DR STRING; 10090.ENSMUSP00000034021; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; Q80VA0; -.
DR PhosphoSitePlus; Q80VA0; -.
DR EPD; Q80VA0; -.
DR MaxQB; Q80VA0; -.
DR PaxDb; Q80VA0; -.
DR PeptideAtlas; Q80VA0; -.
DR PRIDE; Q80VA0; -.
DR ProteomicsDB; 267555; -. [Q80VA0-1]
DR ProteomicsDB; 267556; -. [Q80VA0-2]
DR ProteomicsDB; 267557; -. [Q80VA0-3]
DR Antibodypedia; 28517; 111 antibodies from 23 providers.
DR DNASU; 108150; -.
DR Ensembl; ENSMUST00000034021; ENSMUSP00000034021; ENSMUSG00000031608. [Q80VA0-1]
DR Ensembl; ENSMUST00000110316; ENSMUSP00000105945; ENSMUSG00000031608. [Q80VA0-2]
DR GeneID; 108150; -.
DR KEGG; mmu:108150; -.
DR UCSC; uc009lsy.2; mouse. [Q80VA0-1]
DR UCSC; uc009lsz.2; mouse. [Q80VA0-2]
DR UCSC; uc009lta.2; mouse. [Q80VA0-3]
DR CTD; 51809; -.
DR MGI; MGI:1349449; Galnt7.
DR VEuPathDB; HostDB:ENSMUSG00000031608; -.
DR eggNOG; KOG3737; Eukaryota.
DR GeneTree; ENSGT00940000158105; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q80VA0; -.
DR OMA; CAYDHYK; -.
DR PhylomeDB; Q80VA0; -.
DR TreeFam; TF352176; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 108150; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Galnt7; mouse.
DR PRO; PR:Q80VA0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80VA0; protein.
DR Bgee; ENSMUSG00000031608; Expressed in epithelium of stomach and 250 other tissues.
DR Genevisible; Q80VA0; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Lectin; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..657
FT /note="N-acetylgalactosaminyltransferase 7"
FT /id="PRO_0000059117"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..657
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 532..652
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..317
FT /note="Catalytic subdomain A"
FT REGION 381..443
FT /note="Catalytic subdomain B"
FT COMPBIAS 83..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 197..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 426..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 545..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 585..600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 625..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 323..377
FT /note="TICTVPIIDVISGNTYEIIPQGGGDEDGYARGAWDWSMLWKRVPLTSREKRL
FT RKT -> ATCTVPLIDYIDGNDYSIEPQQGGDEDGFARGAWDWSMLWKRIPLSHKEKAK
FT RKH (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011204"
FT VAR_SEQ 384..657
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011205"
FT CONFLICT 316
FT /note="A -> P (in Ref. 2; BAC28284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 75419 MW; 51B6F3B17E77E703 CRC64;
MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDQSPLSR MREDRDVNNP LPNRGGNGLA
PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG GDSQRDVMQR QYLTFKPQTF
TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG EKAKPLVLGP EYKQAVQASI KEFGFNMVAS
DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA
EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
DAHCEVAVNW YAPLVAPISK DRTICTVPII DVISGNTYEI IPQGGGDEDG YARGAWDWSM
LWKRVPLTSR EKRLRKTKTE PYRSPAMAGG LFAIEKDFFF ELGLYDPGLQ IWGGENFEIS
YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF
YASRPESKAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL
ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC
NLNEFKEWQY FKSLHRFTHI TSGKCLDRSE VLHQVFISTC DSSKMTQKWE MNNIHSV
