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 02-OCT-2024, entry version 166. 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; Q13790: APOF; NbExp=2; IntAct=EBI-21555925, EBI-21895464; 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"; 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; 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; 15. DR BioGRID; 1529357; 2. DR IntAct; Q8N4A0; 11. DR STRING; 9606.ENSP00000436604; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GT27; Glycosyltransferase Family 27. DR UniLectin; Q8N4A0; -. DR GlyCosmos; Q8N4A0; 2 sites, 2 glycans. 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 jPOST; Q8N4A0; -. DR MassIVE; Q8N4A0; -. DR PaxDb; 9606-ENSP00000436604; -. DR PeptideAtlas; Q8N4A0; -. DR Antibodypedia; 53055; 168 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 AGR; HGNC:4126; -. DR AGR; HGNC:42957; -. 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 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; DWNNFEF; -. DR OrthoDB; 202750at2759; -. 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; 33 hits in 1000 CRISPR screens. DR BioGRID-ORCS; 8693; 8 hits in 1140 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 102 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. 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; 2.80.10.50; -; 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 PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR11675:SF7; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 4; 1. DR Pfam; PF00535; Glycos_transf_2; 1. DR Pfam; PF00652; Ricin_B_lectin; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 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; Proteomics identification; Reference proteome; KW Signal-anchor; Transferase; 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 //