GALT4_HUMAN
ID GALT4_HUMAN Reviewed; 578 AA.
AC Q8N4A0; B2R775; B4DMX6; O00208;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 4;
DE EC=2.4.1.41 {ECO:0000269|PubMed:10984485, ECO:0000269|PubMed:29208955, ECO:0000269|PubMed:9804815};
DE AltName: Full=Polypeptide GalNAc transferase 4;
DE Short=GalNAc-T4 {ECO:0000303|PubMed:9804815};
DE Short=pp-GaNTase 4;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 4;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4;
GN Name=GALNT4;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT ILE-506.
RX PubMed=9804815; DOI=10.1074/jbc.273.46.30472;
RA Bennett E.P., Hassan H., Mandel U., Mirgorodskaya E., Roepstorff P.,
RA Burchell J., Taylor-Papadimitriou J., Hollingsworth M.A., Merkx G.,
RA van Kessel A.G., Eiberg H., Steffensen R., Clausen H.;
RT "Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-
RT acetylgalactosaminyltransferase that complements other GalNAc-transferases
RT in complete O-glycosylation of the MUC1 tandem repeat.";
RL J. Biol. Chem. 273:30472-30481(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP THR-270 AND ILE-506.
RC TISSUE=Kidney, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-51.
RC TISSUE=Brain;
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, DOMAIN, PATHWAY, AND MUTAGENESIS OF ASP-459.
RX PubMed=10984485; DOI=10.1074/jbc.m005783200;
RA Hassan H., Reis C.A., Bennett E.P., Mirgorodskaya E., Roepstorff P.,
RA Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.;
RT "The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-
RT acetylgalactosaminyltransferase-T4 directs its glycopeptide
RT specificities.";
RL J. Biol. Chem. 275:38197-38205(2000).
RN [6] {ECO:0007744|PDB:5NQA}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP DOMAIN, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, COFACTOR, AND DISULFIDE
RP BONDS.
RX PubMed=29208955; DOI=10.1038/s41467-017-02006-0;
RA de Las Rivas M., Lira-Navarrete E., Daniel E.J.P., Companon I., Coelho H.,
RA Diniz A., Jimenez-Barbero J., Peregrina J.M., Clausen H., Corzana F.,
RA Marcelo F., Jimenez-Oses G., Gerken T.A., Hurtado-Guerrero R.;
RT "The interdomain flexible linker of the polypeptide GalNAc transferases
RT dictates their long-range glycosylation preferences.";
RL Nat. Commun. 8:1959-1959(2017).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has a highest
CC activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2.
CC Glycosylates 'Thr-57' of SELPLG. {ECO:0000269|PubMed:10984485,
CC ECO:0000269|PubMed:29208955, ECO:0000269|PubMed:9804815}.
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:10984485, ECO:0000269|PubMed:29208955,
CC ECO:0000269|PubMed:9804815};
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:10984485, ECO:0000269|PubMed:29208955,
CC ECO:0000269|PubMed:9804815};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:29208955};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10984485, ECO:0000269|PubMed:29208955,
CC ECO:0000269|PubMed:9804815}.
CC -!- INTERACTION:
CC Q8N4A0; P42858: HTT; NbExp=12; IntAct=EBI-21555925, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:9804815}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9804815}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N4A0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N4A0-2; Sequence=VSP_045009, VSP_045010;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mucous cells.
CC {ECO:0000269|PubMed:9804815}.
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 directs the glycopeptide
CC specificity. It is required in the glycopeptide specificity of enzyme
CC activity but not for activity with naked peptide substrates, suggesting
CC that it triggers the catalytic domain to act on GalNAc-glycopeptide
CC substrates. {ECO:0000269|PubMed:10984485, ECO:0000269|PubMed:29208955}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 4;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_486";
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DR EMBL; Y08564; CAA69875.1; -; Genomic_DNA.
DR EMBL; AK297677; BAG60038.1; -; mRNA.
DR EMBL; AK312870; BAG35722.1; -; mRNA.
DR EMBL; AC010201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036390; AAH36390.1; -; mRNA.
DR CCDS; CCDS53817.1; -. [Q8N4A0-1]
DR RefSeq; NP_001186711.1; NM_001199782.1. [Q8N4A0-2]
DR RefSeq; NP_003765.2; NM_003774.4. [Q8N4A0-1]
DR PDB; 5NQA; X-ray; 1.90 A; A/B=1-578.
DR PDB; 6H0B; X-ray; 1.80 A; A/B=1-578.
DR PDBsum; 5NQA; -.
DR PDBsum; 6H0B; -.
DR AlphaFoldDB; Q8N4A0; -.
DR SMR; Q8N4A0; -.
DR BioGRID; 114240; 12.
DR BioGRID; 1529357; 1.
DR IntAct; Q8N4A0; 9.
DR STRING; 9606.ENSP00000436604; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR UniLectin; Q8N4A0; -.
DR GlyGen; Q8N4A0; 2 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q8N4A0; -.
DR PhosphoSitePlus; Q8N4A0; -.
DR SwissPalm; Q8N4A0; -.
DR BioMuta; GALNT4; -.
DR DMDM; 338817878; -.
DR EPD; Q8N4A0; -.
DR jPOST; Q8N4A0; -.
DR MassIVE; Q8N4A0; -.
DR MaxQB; Q8N4A0; -.
DR PaxDb; Q8N4A0; -.
DR PeptideAtlas; Q8N4A0; -.
DR PRIDE; Q8N4A0; -.
DR ProteomicsDB; 71900; -. [Q8N4A0-1]
DR Antibodypedia; 53055; 155 antibodies from 25 providers.
DR DNASU; 8693; -.
DR Ensembl; ENST00000529983.3; ENSP00000436604.2; ENSG00000257594.4. [Q8N4A0-1]
DR GeneID; 100528030; -.
DR GeneID; 8693; -.
DR KEGG; hsa:100528030; -.
DR KEGG; hsa:8693; -.
DR MANE-Select; ENST00000529983.3; ENSP00000436604.2; NM_003774.5; NP_003765.2.
DR UCSC; uc001tbd.4; human. [Q8N4A0-1]
DR CTD; 100528030; -.
DR CTD; 8693; -.
DR DisGeNET; 100528030; -.
DR DisGeNET; 8693; -.
DR GeneCards; GALNT4; -.
DR HGNC; HGNC:4126; GALNT4.
DR HPA; ENSG00000257594; Tissue enhanced (stomach).
DR MalaCards; GALNT4; -.
DR MIM; 603565; gene.
DR neXtProt; NX_Q8N4A0; -.
DR OpenTargets; ENSG00000257594; -.
DR PharmGKB; PA28539; -.
DR VEuPathDB; HostDB:ENSG00000257594; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000163607; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8N4A0; -.
DR OMA; WHSVPKH; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8N4A0; -.
DR TreeFam; TF352660; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q8N4A0; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8N4A0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 100528030; 32 hits in 956 CRISPR screens.
DR BioGRID-ORCS; 8693; 8 hits in 1064 CRISPR screens.
DR Pharos; Q8N4A0; Tbio.
DR PRO; PR:Q8N4A0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N4A0; protein.
DR Bgee; ENSG00000257594; Expressed in endometrium and 101 other tissues.
DR Genevisible; Q8N4A0; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB.
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; Alternative splicing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="Polypeptide N-acetylgalactosaminyltransferase 4"
FT /id="PRO_0000059108"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..578
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 444..577
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 134..243
FT /note="Catalytic subdomain A"
FT REGION 303..365
FT /note="Catalytic subdomain B"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT SITE 459
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000269|PubMed:29208955"
FT SITE 478
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000269|PubMed:29208955"
FT SITE 483
FT /note="Interaction with glycopeptide substrate"
FT /evidence="ECO:0000269|PubMed:29208955"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:29208955, ECO:0007744|PDB:5NQA"
FT DISULFID 348..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:29208955, ECO:0007744|PDB:5NQA"
FT DISULFID 457..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:29208955, ECO:0007744|PDB:5NQA"
FT DISULFID 503..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:29208955, ECO:0007744|PDB:5NQA"
FT DISULFID 547..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:29208955, ECO:0007744|PDB:5NQA"
FT VAR_SEQ 1..120
FT /note="MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSDL
FT QKNTEDLSRPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRIS
FT LHRHIEDKR -> MAWCVATADPAHTSRPLFTGLAVSRGSAGHAWSAGFDWAAVVVVTG
FT RRCRSGQTVPGAARSPLLPHPLPSPLRVPPPTGALGRPLPRWPQPRRTPFWSVISKATK
FT LRSPPWTSAPTASNL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045009"
FT VAR_SEQ 121..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045010"
FT VARIANT 51
FT /note="D -> G (in dbSNP:rs17853610)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_065257"
FT VARIANT 270
FT /note="I -> T (in dbSNP:rs2230281)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_019576"
FT VARIANT 506
FT /note="V -> I (in dbSNP:rs2230283)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9804815"
FT /id="VAR_019577"
FT MUTAGEN 459
FT /note="D->H: Affects the glycopeptide specificity and
FT abolishes ability to glycosylate Muc1, Muc2 and Muc5AC."
FT /evidence="ECO:0000269|PubMed:10984485"
FT CONFLICT 11
FT /note="S -> T (in Ref. 1; CAA69875)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> Y (in Ref. 1; CAA69875)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="D -> Y (in Ref. 1; CAA69875)"
FT /evidence="ECO:0000305"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6H0B"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:6H0B"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:6H0B"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5NQA"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 351..363
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 410..418
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 444..451
FT /evidence="ECO:0007829|PDB:6H0B"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:5NQA"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6H0B"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:6H0B"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:6H0B"
SQ SEQUENCE 578 AA; 66666 MW; 6EEEF502A40CBD2E CRC64;
MAVRWTWAGK SCLLLAFLTV AYIFVELLVS TFHASAGAGR ARELGSRRLS DLQKNTEDLS
RPLYKKPPAD SRALGEWGKA SKLQLNEDEL KQQEELIERY AINIYLSDRI SLHRHIEDKR
MYECKSQKFN YRTLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRV
YLKTQLETYI SNLDRVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNSGWLEPL
LERIGRDETA VVCPVIDTID WNTFEFYMQI GEPMIGGFDW RLTFQWHSVP KQERDRRISR
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV
GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDIS ERKLLRERLR
CKSFDWYLKN VFPNLHVPED RPGWHGAIRS RGISSECLDY NSPDNNPTGA NLSLFGCHGQ
GGNQFFEYTS NKEIRFNSVT ELCAEVPEQK NYVGMQNCPK DGFPVPANII WHFKEDGTIF
HPHSGLCLSA YRTPEGRPDV QMRTCDALDK NQIWSFEK
