GALT2_HUMAN
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 03-AUG-2022, entry version 196.
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.270.41.24166;
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 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 [15] {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 [16] {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 [17]
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 [18]
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:9394011}.
CC Note=Resides preferentially in the trans and medial parts of the Golgi
CC 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: Widely expressed. {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";
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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; 105.
DR IntAct; Q10471; 29.
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 GlyGen; Q10471; 1 site, 1 O-linked glycan (1 site).
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; Q10471; -.
DR PeptideAtlas; Q10471; -.
DR PRIDE; Q10471; -.
DR ProteomicsDB; 58854; -. [Q10471-1]
DR ProteomicsDB; 6986; -.
DR Antibodypedia; 2493; 177 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 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; 606683at2759; -.
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; 16 hits in 1084 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 195 other tissues.
DR ExpressionAtlas; Q10471; baseline and differential.
DR Genevisible; Q10471; HS.
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:0030173; C:integral component of Golgi membrane; NAS: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; 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; Congenital disorder of glycosylation;
KW Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Secreted; Signal-anchor;
KW 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 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 /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 (likely benign variant; does not affect ApoC-
FT 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; b)"
FT /evidence="ECO:0000269|PubMed:27508872,
FT ECO:0000269|PubMed:32293671"
FT /id="VAR_084287"
FT VARIANT 493
FT /note="M -> V (likely benign variant; does not affect ApoC-
FT III glycosylation; 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
