GALT7_HUMAN
ID GALT7_HUMAN Reviewed; 657 AA.
AC Q86SF2; B3KQU3; Q7Z5W7; Q9UJ28;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=N-acetylgalactosaminyltransferase 7;
DE EC=2.4.1.41 {ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=10544240; DOI=10.1016/s0014-5793(99)01268-5;
RA Bennett E.P., Hassan H., Hollingsworth M.A., Clausen H.;
RT "A novel human UDP-N-acetyl-D-galactosamine;polypeptide N-
RT acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial
RT GalNAc-glycosylated acceptor substrates.";
RL FEBS Lett. 460:226-230(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Testis;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11925450; DOI=10.1074/jbc.m202684200;
RA Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A.,
RA Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R.,
RA Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A.,
RA Clausen H.;
RT "Functional conservation of subfamilies of putative UDP-N-
RT acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
RT Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of
RT l(2)35Aa is essential in Drosophila.";
RL J. Biol. Chem. 277:22623-22638(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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.
CC {ECO:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450}.
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:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
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:0000269|PubMed:10544240, ECO:0000269|PubMed:11925450};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:10544240, ECO:0000305|PubMed:11925450}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in uterus, retina,
CC kidney, small intestine, omentum, stomach and CNS.
CC {ECO:0000269|PubMed:10544240}.
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 -!- 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_hum_489";
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DR EMBL; AJ002744; CAB60270.1; -; mRNA.
DR EMBL; AK075488; BAG52155.1; -; mRNA.
DR EMBL; CH471056; EAX04761.1; -; Genomic_DNA.
DR EMBL; BC035303; AAH35303.1; -; mRNA.
DR EMBL; BC046129; AAH46129.1; -; mRNA.
DR EMBL; BC047468; AAH47468.1; -; mRNA.
DR CCDS; CCDS3815.1; -.
DR RefSeq; NP_059119.2; NM_017423.2.
DR PDB; 6IWQ; X-ray; 2.95 A; A/B/C/D/E/F=61-657.
DR PDB; 6IWR; X-ray; 2.60 A; A/B/C/D/E/F=61-657.
DR PDBsum; 6IWQ; -.
DR PDBsum; 6IWR; -.
DR AlphaFoldDB; Q86SF2; -.
DR SMR; Q86SF2; -.
DR BioGRID; 119735; 54.
DR IntAct; Q86SF2; 21.
DR MINT; Q86SF2; -.
DR STRING; 9606.ENSP00000265000; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR UniLectin; Q86SF2; -.
DR iPTMnet; Q86SF2; -.
DR PhosphoSitePlus; Q86SF2; -.
DR BioMuta; GALNT7; -.
DR DMDM; 51315961; -.
DR EPD; Q86SF2; -.
DR jPOST; Q86SF2; -.
DR MassIVE; Q86SF2; -.
DR MaxQB; Q86SF2; -.
DR PaxDb; Q86SF2; -.
DR PeptideAtlas; Q86SF2; -.
DR PRIDE; Q86SF2; -.
DR ProteomicsDB; 69579; -.
DR Antibodypedia; 28517; 111 antibodies from 23 providers.
DR DNASU; 51809; -.
DR Ensembl; ENST00000265000.9; ENSP00000265000.4; ENSG00000109586.12.
DR GeneID; 51809; -.
DR KEGG; hsa:51809; -.
DR MANE-Select; ENST00000265000.9; ENSP00000265000.4; NM_017423.3; NP_059119.2.
DR UCSC; uc003isz.4; human.
DR CTD; 51809; -.
DR DisGeNET; 51809; -.
DR GeneCards; GALNT7; -.
DR HGNC; HGNC:4129; GALNT7.
DR HPA; ENSG00000109586; Low tissue specificity.
DR MIM; 605005; gene.
DR neXtProt; NX_Q86SF2; -.
DR OpenTargets; ENSG00000109586; -.
DR PharmGKB; PA28542; -.
DR VEuPathDB; HostDB:ENSG00000109586; -.
DR eggNOG; KOG3737; Eukaryota.
DR GeneTree; ENSGT00940000158105; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q86SF2; -.
DR OMA; EMNNIHT; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q86SF2; -.
DR TreeFam; TF352176; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q86SF2; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q86SF2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 51809; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; GALNT7; human.
DR GenomeRNAi; 51809; -.
DR Pharos; Q86SF2; Tbio.
DR PRO; PR:Q86SF2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86SF2; protein.
DR Bgee; ENSG00000109586; Expressed in mucosa of sigmoid colon and 199 other tissues.
DR ExpressionAtlas; Q86SF2; baseline and differential.
DR Genevisible; Q86SF2; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 3D-structure; Disulfide bond; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..657
FT /note="N-acetylgalactosaminyltransferase 7"
FT /id="PRO_0000059116"
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 31..65
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 36..50
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 CONFLICT 188
FT /note="S -> N (in Ref. 1; CAB60270)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="F -> C (in Ref. 1; CAB60270)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="G -> S (in Ref. 1; CAB60270)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="K -> Q (in Ref. 1; CAB60270)"
FT /evidence="ECO:0000305"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 324..334
FT /evidence="ECO:0007829|PDB:6IWR"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 429..442
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 477..483
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 496..504
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 510..516
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:6IWR"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:6IWR"
FT TURN 612..615
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:6IWR"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:6IWR"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:6IWR"
SQ SEQUENCE 657 AA; 75389 MW; D78CB5CBDA4B02FA CRC64;
MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP MPNRGGNGLA
PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG GDSQKDIMQR QYLTFKPQTF
TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG EKAKPLVLGP EFKQAIQASI KEFGFNMVAS
DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA
EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG YARGAWDWSM
LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF ELGLYDPGLQ IWGGENFEIS
YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF
YASRPESQAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF
ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC
NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE MNNIHSV
