ID GALT2_HUMAN Reviewed; 571 AA. AC Q10471; A8K1Y3; B7Z8V8; C5HU00; Q9NPY4; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2; DE EC=2.4.1.41 {ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:25939779, ECO:0000269|PubMed:7592619}; DE AltName: Full=Polypeptide GalNAc transferase 2; DE Short=GalNAc-T2; DE Short=pp-GaNTase 2; DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 2; DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2; DE Contains: DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2 soluble form; GN Name=GALNT2; 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] (ISOFORM 1), PROTEIN SEQUENCE OF 52-93; 104-120; RP 170-182; 193-218; 303-323; 421-424 AND 510-546, FUNCTION, COFACTOR, RP CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY. RC TISSUE=Gastric carcinoma; RX PubMed=7592619; DOI=10.1074/jbc.270.41.24156; RA White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.; RT "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D- RT galactosamine:polypeptide N-acetylgalactosaminyltransferase."; RL J. Biol. Chem. 270:24156-24165(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP MET-554. RC TISSUE=Hippocampus, 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 [7] RP FUNCTION. RX PubMed=9295285; DOI=10.1074/jbc.272.38.23503; RA Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., RA Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., RA Taylor-Papadimitriou J., Clausen H.; RT "Substrate specificities of three members of the human UDP-N-acetyl-alpha- RT D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, RT GalNAc-T1, -T2, and -T3."; RL J. Biol. Chem. 272:23503-23514(1997). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=9394011; DOI=10.1242/jcs.111.1.45; RA Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., RA Whitehouse C., Berger E.G., Clausen H., Nilsson T.; RT "Localization of three human polypeptide GalNAc-transferases in HeLa cells RT suggests initiation of O-linked glycosylation throughout the Golgi RT apparatus."; RL J. Cell Sci. 111:45-60(1998). RN [9] RP FUNCTION. RX PubMed=12438318; DOI=10.1074/jbc.m211097200; RA Iwasaki H., Zhang Y., Tachibana K., Gotoh M., Kikuchi N., Kwon Y.-D., RA Togayachi A., Kudo T., Kubota T., Narimatsu H.; RT "Initiation of O-glycan synthesis in IgA1 hinge region is determined by a RT single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- RT acetylgalactosaminyltransferase 2."; RL J. Biol. Chem. 278:5613-5621(2003). RN [10] 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). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-29. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 75-571 IN COMPLEX WITH UDP; RP PEPTIDE SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP PATHWAY, AND DISULFIDE BONDS. RX PubMed=16434399; DOI=10.1074/jbc.m513590200; RA Fritz T.A., Raman J., Tabak L.A.; RT "Dynamic association between the catalytic and lectin domains of human UDP- RT GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2."; RL J. Biol. Chem. 281:8613-8619(2006). RN [16] {ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS RP AND MANGANESE, COFACTOR, AND DISULFIDE BONDS. RX PubMed=24954443; DOI=10.1002/anie.201402781; RA Lira-Navarrete E., Iglesias-Fernandez J., Zandberg W.F., Companon I., RA Kong Y., Corzana F., Pinto B.M., Clausen H., Peregrina J.M., Vocadlo D.J., RA Rovira C., Hurtado-Guerrero R.; RT "Substrate-guided front-face reaction revealed by combined structural RT snapshots and metadynamics for the polypeptide N- RT acetylgalactosaminyltransferase2."; RL Angew. Chem. Int. Ed. Engl. 53:8206-8210(2014). RN [17] {ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP} RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MANGANESE AND RP SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, MUTAGENESIS OF RP TRP-282 AND PHE-361, AND DISULFIDE BONDS. RX PubMed=25939779; DOI=10.1038/ncomms7937; RA Lira-Navarrete E., de Las Rivas M., Companon I., Pallares M.C., Kong Y., RA Iglesias-Fernandez J., Bernardes G.J., Peregrina J.M., Rovira C., RA Bernado P., Bruscolini P., Clausen H., Lostao A., Corzana F., RA Hurtado-Guerrero R.; RT "Dynamic interplay between catalytic and lectin domains of GalNAc- RT transferases modulates protein O-glycosylation."; RL Nat. Commun. 6:6937-6937(2015). RN [18] RP VARIANTS CDG2T SER-104 AND 289-GLN--GLN-571 DEL, CHARACTERIZATION OF RP VARIANTS CDG2T SER-104 AND 289-GLN--GLN-571 DEL, INVOLVEMENT IN CDG2T, AND RP FUNCTION. RX PubMed=27508872; DOI=10.1016/j.cmet.2016.07.012; RG Myocardial Infarction Exome Sequencing Study; RA Khetarpal S.A., Schjoldager K.T., Christoffersen C., Raghavan A., RA Edmondson A.C., Reutter H.M., Ahmed B., Ouazzani R., Peloso G.M., RA Vitali C., Zhao W., Somasundara A.V., Millar J.S., Park Y., Fernando G., RA Livanov V., Choi S., Noe E., Patel P., Ho S.P., Kirchgessner T.G., RA Wandall H.H., Hansen L., Bennett E.P., Vakhrushev S.Y., Saleheen D., RA Kathiresan S., Brown C.D., Abou Jamra R., LeGuern E., Clausen H., RA Rader D.J.; RT "Loss of function of GALNT2 lowers high-density lipoproteins in humans, RT nonhuman primates, and rodents."; RL Cell Metab. 24:234-245(2016). RN [19] RP VARIANTS CDG2T 200-ARG--GLN-571 DEL; PRO-210 AND 289-GLN--GLN-571 DEL, RP CHARACTERIZATION OF VARIANTS CDG2T 200-ARG--GLN-571 DEL; PRO-210 AND RP 289-GLN--GLN-571 DEL, VARIANTS ARG-271 AND VAL-493, CHARACTERIZATION OF RP VARIANTS ARG-271 AND VAL-493, AND FUNCTION. RX PubMed=32293671; DOI=10.1093/brain/awaa063; RA Zilmer M., Edmondson A.C., Khetarpal S.A., Alesi V., Zaki M.S., Rostasy K., RA Madsen C.G., Lepri F.R., Sinibaldi L., Cusmai R., Novelli A., Issa M.Y., RA Fenger C.D., Abou Jamra R., Reutter H., Briuglia S., Agolini E., Hansen L., RA Petaejae-Repo U.E., Hintze J., Raymond K.M., Liedtke K., Stanley V., RA Musaev D., Gleeson J.G., Vitali C., O'Brien W.T., Gardella E., Rubboli G., RA Rader D.J., Schjoldager K.T., Moeller R.S.; RT "Novel congenital disorder of O-linked glycosylation caused by GALNT2 loss RT of function."; RL Brain 143:1114-1126(2020). 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 broad CC spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. CC Probably involved in O-linked glycosylation of the immunoglobulin A1 CC (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, CC ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism CC (PubMed:27508872, PubMed:32293671). {ECO:0000269|PubMed:12438318, CC ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:25939779, CC ECO:0000269|PubMed:27508872, ECO:0000269|PubMed:32293671, CC ECO:0000269|PubMed:7592619, ECO:0000269|PubMed:9295285}. 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:16434399, ECO:0000269|PubMed:25939779, CC ECO:0000269|PubMed:7592619}; 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:16434399, ECO:0000269|PubMed:25939779, CC ECO:0000269|PubMed:7592619}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, CC ECO:0000269|PubMed:25939779, ECO:0000269|PubMed:7592619}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:25939779, CC ECO:0000269|PubMed:7592619}. CC -!- INTERACTION: CC Q10471; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-10226985, EBI-747430; CC Q10471; O75208: COQ9; NbExp=3; IntAct=EBI-10226985, EBI-724524; CC Q10471; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-10226985, EBI-749265; CC Q10471; Q9HC36: MRM3; NbExp=3; IntAct=EBI-10226985, EBI-1045440; CC Q10471; Q9HC29: NOD2; NbExp=2; IntAct=EBI-10226985, EBI-7445625; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:9394011}. Secreted {ECO:0000269|PubMed:37453717, CC ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans CC and medial parts of the Golgi stack. A secreted form also exists. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q10471-1; Sequence=Displayed; CC Name=2; CC IsoId=Q10471-2; Sequence=VSP_056491, VSP_056492, VSP_056493; CC -!- TISSUE SPECIFICITY: Detected in urine (at protein level) CC (PubMed:37453717). Widely expressed. {ECO:0000269|PubMed:37453717, CC ECO:0000269|PubMed:7592619}. 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 -!- DISEASE: Congenital disorder of glycosylation 2T (CDG2T) [MIM:618885]: CC A form of congenital disorder of glycosylation, a genetically CC heterogeneous group of multisystem disorders caused by a defect in CC glycoprotein biosynthesis and characterized by under-glycosylated serum CC glycoproteins. Congenital disorders of glycosylation result in a wide CC variety of clinical features, such as defects in the nervous system CC development, psychomotor retardation, dysmorphic features, hypotonia, CC coagulation disorders, and immunodeficiency. The broad spectrum of CC features reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CDG2T CC is an autosomal recessive form characterized by global developmental CC delay, intellectual disability with language deficit, autistic CC features, behavioral abnormalities, epilepsy, chronic insomnia, white CC matter changes on brain imaging, dysmorphic features, decreased CC stature, and decreased high density lipoprotein cholesterol levels. CC {ECO:0000269|PubMed:27508872, ECO:0000269|PubMed:32293671}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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 2; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_484"; 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; X85019; CAA59381.1; -; mRNA. DR EMBL; AK290048; BAF82737.1; -; mRNA. DR EMBL; AK304029; BAH14094.1; -; mRNA. DR EMBL; AL592228; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL078646; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL117349; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FJ515852; ACS13744.1; -; Genomic_DNA. DR EMBL; CH471098; EAW69911.1; -; Genomic_DNA. DR EMBL; BC041120; AAH41120.1; -; mRNA. DR CCDS; CCDS1582.1; -. [Q10471-1] DR PIR; I37405; I37405. DR RefSeq; NP_001278795.1; NM_001291866.1. DR RefSeq; NP_004472.1; NM_004481.4. [Q10471-1] DR PDB; 2FFU; X-ray; 1.64 A; A=75-571. DR PDB; 2FFV; X-ray; 2.75 A; A/B=75-571. DR PDB; 4D0T; X-ray; 2.45 A; A/B/C/D/E/F=1-571. DR PDB; 4D0Z; X-ray; 2.20 A; A/B/C/D/E/F=1-571. DR PDB; 4D11; X-ray; 2.85 A; A/B/C/D/E/F=1-571. DR PDB; 5AJN; X-ray; 1.67 A; A=1-571. DR PDB; 5AJO; X-ray; 1.48 A; A=1-571. DR PDB; 5AJP; X-ray; 1.65 A; A=1-571. DR PDB; 5FV9; X-ray; 2.07 A; A/B/C/D/E/F=1-571. DR PDB; 5NDF; X-ray; 2.30 A; A/B/C/D/E/F=1-571. DR PDB; 6E7I; X-ray; 1.80 A; A=74-571. DR PDB; 6EGS; X-ray; 2.70 A; A/B=75-571. DR PDB; 6NQT; X-ray; 3.05 A; A/B/C/D/E/F=1-571. DR PDBsum; 2FFU; -. DR PDBsum; 2FFV; -. DR PDBsum; 4D0T; -. DR PDBsum; 4D0Z; -. DR PDBsum; 4D11; -. DR PDBsum; 5AJN; -. DR PDBsum; 5AJO; -. DR PDBsum; 5AJP; -. DR PDBsum; 5FV9; -. DR PDBsum; 5NDF; -. DR PDBsum; 6E7I; -. DR PDBsum; 6EGS; -. DR PDBsum; 6NQT; -. DR AlphaFoldDB; Q10471; -. DR SMR; Q10471; -. DR BioGRID; 108862; 117. DR IntAct; Q10471; 31. DR MINT; Q10471; -. DR STRING; 9606.ENSP00000355632; -. DR BindingDB; Q10471; -. DR ChEMBL; CHEMBL3713355; -. DR CAZy; CBM13; Carbohydrate-Binding Module Family 13. DR CAZy; GT27; Glycosyltransferase Family 27. DR UniLectin; Q10471; -. DR GlyCosmos; Q10471; 1 site, 1 glycan. DR GlyGen; Q10471; 6 sites, 3 O-linked glycans (6 sites). DR iPTMnet; Q10471; -. DR PhosphoSitePlus; Q10471; -. DR SwissPalm; Q10471; -. DR BioMuta; GALNT2; -. DR DMDM; 51315838; -. DR EPD; Q10471; -. DR jPOST; Q10471; -. DR MassIVE; Q10471; -. DR MaxQB; Q10471; -. DR PaxDb; 9606-ENSP00000355632; -. DR PeptideAtlas; Q10471; -. DR ProteomicsDB; 58854; -. [Q10471-1] DR ProteomicsDB; 6986; -. DR Pumba; Q10471; -. DR Antibodypedia; 2493; 187 antibodies from 28 providers. DR DNASU; 2590; -. DR Ensembl; ENST00000366672.5; ENSP00000355632.4; ENSG00000143641.10. [Q10471-1] DR GeneID; 2590; -. DR KEGG; hsa:2590; -. DR MANE-Select; ENST00000366672.5; ENSP00000355632.4; NM_004481.5; NP_004472.1. DR UCSC; uc010pwa.2; human. [Q10471-1] DR AGR; HGNC:4124; -. DR CTD; 2590; -. DR DisGeNET; 2590; -. DR GeneCards; GALNT2; -. DR HGNC; HGNC:4124; GALNT2. DR HPA; ENSG00000143641; Low tissue specificity. DR MalaCards; GALNT2; -. DR MIM; 602274; gene. DR MIM; 618885; phenotype. DR neXtProt; NX_Q10471; -. DR OpenTargets; ENSG00000143641; -. DR PharmGKB; PA28537; -. DR VEuPathDB; HostDB:ENSG00000143641; -. DR eggNOG; KOG3738; Eukaryota. DR GeneTree; ENSGT00940000156958; -. DR HOGENOM; CLU_013477_0_2_1; -. DR InParanoid; Q10471; -. DR OMA; QEWAFSK; -. DR OrthoDB; 202750at2759; -. DR PhylomeDB; Q10471; -. DR TreeFam; TF313267; -. DR BRENDA; 2.4.1.41; 2681. DR PathwayCommons; Q10471; -. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-913709; O-linked glycosylation of mucins. DR SignaLink; Q10471; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 2590; 18 hits in 1160 CRISPR screens. DR ChiTaRS; GALNT2; human. DR EvolutionaryTrace; Q10471; -. DR GeneWiki; GALNT2; -. DR GenomeRNAi; 2590; -. DR Pharos; Q10471; Tchem. DR PRO; PR:Q10471; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q10471; Protein. DR Bgee; ENSG00000143641; Expressed in descending thoracic aorta and 197 other cell types or tissues. DR ExpressionAtlas; Q10471; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005795; C:Golgi stack; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. 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; IDA:GO_Central. DR GO; GO:0051604; P:protein maturation; IDA:BHF-UCL. DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB. DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:BHF-UCL. DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:BHF-UCL. 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:SF119; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 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. DR Genevisible; Q10471; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Congenital disorder of glycosylation; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane; KW Metal-binding; Phosphoprotein; Proteoglycan; Reference proteome; Secreted; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..571 FT /note="Polypeptide N-acetylgalactosaminyltransferase 2" FT /id="PRO_0000223391" FT CHAIN 52..571 FT /note="Polypeptide N-acetylgalactosaminyltransferase 2 FT soluble form" FT /id="PRO_0000012265" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..24 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 25..571 FT /note="Lumenal" FT /evidence="ECO:0000255" FT DOMAIN 443..566 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REGION 53..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 135..240 FT /note="Catalytic subdomain A" FT REGION 300..362 FT /note="Catalytic subdomain B" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 176 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 201 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 224 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, FT ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJP, FT ECO:0007744|PDB:5FV9" FT BINDING 225 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 226 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, FT ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJP, FT ECO:0007744|PDB:5FV9" FT BINDING 331 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 359 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, FT ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJP, FT ECO:0007744|PDB:5FV9" FT BINDING 362 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9" FT BINDING 367 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:16434399, FT ECO:0000269|PubMed:24954443, ECO:0000269|PubMed:25939779, FT ECO:0007744|PDB:2FFU, ECO:0007744|PDB:2FFV, FT ECO:0007744|PDB:4D0T, ECO:0007744|PDB:4D0Z, FT ECO:0007744|PDB:4D11, ECO:0007744|PDB:5AJN, FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP, FT ECO:0007744|PDB:5FV9, ECO:0007744|PDB:5NDF, FT ECO:0007744|PDB:6EGS" FT SITE 516 FT /note="Not glycosylated" FT MOD_RES 536 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 29 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:37453717" FT DISULFID 126..354 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, FT ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, FT ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, FT ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, FT ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS" FT DISULFID 345..423 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, FT ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, FT ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, FT ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, FT ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS" FT DISULFID 456..473 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, FT ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, FT ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, FT ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, FT ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS" FT DISULFID 496..513 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, FT ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, FT ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, FT ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, FT ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS" FT DISULFID 539..555 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174, FT ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:24954443, FT ECO:0000269|PubMed:25939779, ECO:0007744|PDB:2FFU, FT ECO:0007744|PDB:2FFV, ECO:0007744|PDB:4D0T, FT ECO:0007744|PDB:4D0Z, ECO:0007744|PDB:4D11, FT ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, FT ECO:0007744|PDB:5AJP, ECO:0007744|PDB:5FV9, FT ECO:0007744|PDB:5NDF, ECO:0007744|PDB:6EGS" FT VAR_SEQ 1..90 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056491" FT VAR_SEQ 303..355 FT /note="TPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPC FT S -> DLVPRVAVWWQPGDHPVQPCGTRVPEAAPLHVPGWQWHCLCPKHPPGSRGLDG FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056492" FT VAR_SEQ 356..571 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056493" FT VARIANT 104 FT /note="F -> S (in CDG2T; loss-of-funtion variant resulting FT in lack of ApoC-III and IgA1 glycosylation; FT dbSNP:rs1663960324)" FT /evidence="ECO:0000269|PubMed:27508872" FT /id="VAR_084283" FT VARIANT 200..571 FT /note="Missing (in CDG2T; loss of ApoC-III glycosylation)" FT /evidence="ECO:0000269|PubMed:32293671" FT /id="VAR_084284" FT VARIANT 210 FT /note="R -> P (in CDG2T; loss of ApoC-III glycosylation)" FT /evidence="ECO:0000269|PubMed:32293671" FT /id="VAR_084285" FT VARIANT 245 FT /note="R -> H (in dbSNP:rs1923950)" FT /id="VAR_049240" FT VARIANT 271 FT /note="K -> R (found in a patient with multiple FT abnormalities including neonatal hypotonia, psychomotor FT delay, feeding difficulty and dysmorphic features; likely FT benign; does not affect ApoC-III glycosylation)" FT /evidence="ECO:0000269|PubMed:32293671" FT /id="VAR_084286" FT VARIANT 289..571 FT /note="Missing (in CDG2T; loss-of-funtion variant resulting FT in lack of ApoC-III glycosylation)" FT /evidence="ECO:0000269|PubMed:27508872, FT ECO:0000269|PubMed:32293671" FT /id="VAR_084287" FT VARIANT 493 FT /note="M -> V (found in a patient with multiple FT abnormalities including neonatal hypotonia, psychomotor FT delay, feeding difficulty and dysmorphic features; likely FT benign; does not affect ApoC-III glycosylation; FT dbSNP:rs774570005)" FT /evidence="ECO:0000269|PubMed:32293671" FT /id="VAR_084288" FT VARIANT 554 FT /note="V -> M (in dbSNP:rs2273970)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_019575" FT MUTAGEN 282 FT /note="W->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25939779" FT MUTAGEN 361 FT /note="F->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25939779" FT CONFLICT 70 FT /note="T -> G (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 78 FT /note="W -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 93 FT /note="R -> G (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="R -> W (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 290..291 FT /note="RR -> SC (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="R -> Q (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="P -> H (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 522 FT /note="W -> A (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="H -> M (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 83..87 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:5AJO" FT TURN 98..102 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 106..111 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 124..128 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 168..175 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 186..189 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 193..197 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 204..214 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 217..223 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 235..243 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 247..256 FT /evidence="ECO:0007829|PDB:5AJO" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 280..284 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 287..295 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 308..314 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 315..320 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 336..344 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 348..360 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:5AJO" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:6EGS" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 378..388 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 393..399 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 412..420 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 426..432 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 445..452 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:5AJO" FT TURN 463..465 FT /evidence="ECO:0007829|PDB:6EGS" FT STRAND 469..472 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 478..480 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 495..498 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 509..512 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 518..520 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 522..525 FT /evidence="ECO:0007829|PDB:5AJO" FT TURN 526..529 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 530..533 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 536..541 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 545..547 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 551..554 FT /evidence="ECO:0007829|PDB:5AJO" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:5AJO" FT STRAND 564..568 FT /evidence="ECO:0007829|PDB:5AJO" SQ SEQUENCE 571 AA; 64733 MW; D9A0F5D17C55BAF2 CRC64; MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP IKKKDLHHSN GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA RNKFNQVESD KLRMDRAIPD TRHDQCQRKQ WRVDLPATSV VITFHNEARS ALLRTVVSVL KKSPPHLIKE IILVDDYSND PEDGALLGKI EKVRVLRNDR REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER VAEDRTRVVS PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE IIPCSRVGHV FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV PSARNVPYGN IQSRLELRKK LSCKPFKWYL ENVYPELRVP DHQDIAFGAL QQGTNCLDTL GHFADGVVGV YECHNAGGNQ EWALTKEKSV KHMDLCLTVV DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL DSRTAKSGGL SVEVCGPALS QQWKFTLNLQ Q //