ID   GLT11_HUMAN             Reviewed;         608 AA.
AC   Q8NCW6; B3KWF4; Q6PCD1; Q9H6C2; Q9H6Z5; Q9UDR8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 11;
DE            EC=2.4.1.41;
DE   AltName: Full=Polypeptide GalNAc transferase 11;
DE            Short=GalNAc-T11;
DE            Short=pp-GaNTase 11;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 11;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11;
GN   Name=GALNT11;
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), FUNCTION, ENZYME ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11925450; DOI=10.1074/jbc.m202684200;
RA   Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A.,
RA   Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R.,
RA   Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A.,
RA   Clausen H.;
RT   "Functional conservation of subfamilies of putative UDP-N-
RT   acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in
RT   Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of
RT   l(2)35Aa is essential in Drosophila.";
RL   J. Biol. Chem. 277:22623-22638(2002).
RN   [2]
RP   SEQUENCE REVISION TO 14-15; 119; 295; 310; 365 AND 369.
RA   Bennett E.P.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, Kidney epithelium, and Subthalamic nucleus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
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   [6]
RP   POSSIBLE INVOLVEMENT IN HETEROTAXY.
RX   PubMed=21282601; DOI=10.1073/pnas.1019645108;
RA   Fakhro K.A., Choi M., Ware S.M., Belmont J.W., Towbin J.A., Lifton R.P.,
RA   Khokha M.K., Brueckner M.;
RT   "Rare copy number variations in congenital heart disease patients identify
RT   unique genes in left-right patterning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2915-2920(2011).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF HIS-247, AND INTERACTION WITH NOTCH1.
RX   PubMed=24226769; DOI=10.1038/nature12723;
RA   Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H.,
RA   Brueckner M., Khokha M.K.;
RT   "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type
RT   and laterality.";
RL   Nature 504:456-459(2013).
RN   [8]
RP   VARIANT TYR-197.
RX   PubMed=20547088; DOI=10.1016/j.legalmed.2010.04.001;
RA   Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S., Fukumori Y.,
RA   Saitou N., Jin F., Chattopadhyay P.K., Henke L., Henke J.;
RT   "A Japanese-specific allele in the GALNT11 gene.";
RL   Leg. Med. 12:208-211(2010).
CC   -!- FUNCTION: Polypeptide N-acetylgalactosaminyltransferase that catalyzes
CC       the initiation of protein O-linked glycosylation and is involved in
CC       left/right asymmetry by mediating O-glycosylation of NOTCH1. O-
CC       glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the
CC       balance between motile and immotile (sensory) cilia at the left-right
CC       organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases
CC       catalyze the transfer of an N-acetyl-D-galactosamine residue to a
CC       serine or threonine residue on the protein receptor. Displays the same
CC       enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in
CC       glycosylation of erythropoietin (EPO). {ECO:0000269|PubMed:11925450,
CC       ECO:0000269|PubMed:24226769}.
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:11925450};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC         O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC         Evidence={ECO:0000269|PubMed:11925450};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Interacts with NOTCH1. {ECO:0000269|PubMed:24226769}.
CC   -!- INTERACTION:
CC       Q8NCW6-2; O15499: GSC2; NbExp=3; IntAct=EBI-13364322, EBI-19954058;
CC       Q8NCW6-2; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-13364322, EBI-744081;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:11925450}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:11925450}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NCW6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NCW6-2; Sequence=VSP_011215, VSP_011216;
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney. Expressed at
CC       intermediate level in brain, heart and skeletal muscle. Weakly
CC       expressed other tissues. In kidney, it is strongly expressed in tubules
CC       but not expressed in glomeruli. {ECO:0000269|PubMed:11925450}.
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: Note=Defects in GALNT11 may be a cause of heterotaxy, a
CC       congenital heart disease resulting from abnormalities in left-right
CC       (LR) body patterning. {ECO:0000269|PubMed:21282601}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Polypeptide N-acetylgalactosaminyltransferase 11;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_494";
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; Y12434; CAC79625.3; -; mRNA.
DR   EMBL; AK025287; BAB15105.1; -; mRNA.
DR   EMBL; AK026056; BAB15338.1; ALT_INIT; mRNA.
DR   EMBL; AK124934; BAG54116.1; -; mRNA.
DR   EMBL; AC006017; AAD45821.1; -; Genomic_DNA.
DR   EMBL; BC059377; AAH59377.1; -; mRNA.
DR   CCDS; CCDS5930.1; -. [Q8NCW6-1]
DR   CCDS; CCDS94237.1; -. [Q8NCW6-2]
DR   RefSeq; NP_071370.2; NM_022087.3. [Q8NCW6-1]
DR   RefSeq; XP_006716145.1; XM_006716082.2.
DR   RefSeq; XP_006716146.1; XM_006716083.2. [Q8NCW6-1]
DR   RefSeq; XP_006716147.1; XM_006716084.2. [Q8NCW6-1]
DR   RefSeq; XP_016867989.1; XM_017012500.1.
DR   AlphaFoldDB; Q8NCW6; -.
DR   SMR; Q8NCW6; -.
DR   BioGRID; 121988; 32.
DR   IntAct; Q8NCW6; 16.
DR   STRING; 9606.ENSP00000416787; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q8NCW6; 2 sites, 1 glycan.
DR   GlyGen; Q8NCW6; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8NCW6; -.
DR   PhosphoSitePlus; Q8NCW6; -.
DR   BioMuta; GALNT11; -.
DR   DMDM; 51316030; -.
DR   EPD; Q8NCW6; -.
DR   jPOST; Q8NCW6; -.
DR   MassIVE; Q8NCW6; -.
DR   MaxQB; Q8NCW6; -.
DR   PaxDb; 9606-ENSP00000416787; -.
DR   PeptideAtlas; Q8NCW6; -.
DR   ProteomicsDB; 72960; -. [Q8NCW6-1]
DR   ProteomicsDB; 72961; -. [Q8NCW6-2]
DR   Antibodypedia; 52579; 139 antibodies from 18 providers.
DR   DNASU; 63917; -.
DR   Ensembl; ENST00000415421.5; ENSP00000410093.1; ENSG00000178234.13. [Q8NCW6-2]
DR   Ensembl; ENST00000422997.6; ENSP00000389449.3; ENSG00000178234.13. [Q8NCW6-2]
DR   Ensembl; ENST00000430044.7; ENSP00000395122.2; ENSG00000178234.13. [Q8NCW6-1]
DR   Ensembl; ENST00000434507.5; ENSP00000416787.1; ENSG00000178234.13. [Q8NCW6-1]
DR   GeneID; 63917; -.
DR   KEGG; hsa:63917; -.
DR   MANE-Select; ENST00000430044.7; ENSP00000395122.2; NM_022087.4; NP_071370.2.
DR   UCSC; uc003wku.3; human. [Q8NCW6-1]
DR   AGR; HGNC:19875; -.
DR   CTD; 63917; -.
DR   DisGeNET; 63917; -.
DR   GeneCards; GALNT11; -.
DR   HGNC; HGNC:19875; GALNT11.
DR   HPA; ENSG00000178234; Group enriched (choroid plexus, kidney).
DR   MIM; 615130; gene.
DR   neXtProt; NX_Q8NCW6; -.
DR   OpenTargets; ENSG00000178234; -.
DR   PharmGKB; PA134911149; -.
DR   VEuPathDB; HostDB:ENSG00000178234; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000158227; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q8NCW6; -.
DR   OMA; PVFQPWH; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q8NCW6; -.
DR   TreeFam; TF313267; -.
DR   BRENDA; 2.4.1.41; 2681.
DR   PathwayCommons; Q8NCW6; -.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   SABIO-RK; Q8NCW6; -.
DR   SignaLink; Q8NCW6; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 63917; 10 hits in 1165 CRISPR screens.
DR   ChiTaRS; GALNT11; human.
DR   GenomeRNAi; 63917; -.
DR   Pharos; Q8NCW6; Tbio.
DR   PRO; PR:Q8NCW6; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8NCW6; Protein.
DR   Bgee; ENSG00000178234; Expressed in choroid plexus epithelium and 210 other cell types or tissues.
DR   ExpressionAtlas; Q8NCW6; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005112; F:Notch binding; IDA:UniProtKB.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR   GO; GO:0007220; P:Notch receptor processing; ISS:UniProtKB.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; ISS: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:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; ISS: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:SF10; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 11; 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; Q8NCW6; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Heterotaxy; Lectin; Manganese; Membrane; Metal-binding;
KW   Notch signaling pathway; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..608
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 11"
FT                   /id="PRO_0000059125"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..608
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          476..607
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          150..261
FT                   /note="Catalytic subdomain A"
FT   REGION          319..381
FT                   /note="Catalytic subdomain B"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         378
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q921L8"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        364..441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        493..512
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        536..553
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        578..596
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   VAR_SEQ         196..202
FT                   /note="DDLKGEL -> GKECCTW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011215"
FT   VAR_SEQ         203..608
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011216"
FT   VARIANT         151
FT                   /note="P -> S (in dbSNP:rs6464201)"
FT                   /id="VAR_019589"
FT   VARIANT         197
FT                   /note="D -> Y (in dbSNP:rs3778922)"
FT                   /evidence="ECO:0000269|PubMed:20547088"
FT                   /id="VAR_019590"
FT   MUTAGEN         247
FT                   /note="H->A: Abolishes glycosyltransferase activity and
FT                   ability to rescue left-right patterning defects induced by
FT                   galnt11 knockdown in X.tropicalis."
FT                   /evidence="ECO:0000269|PubMed:24226769"
FT   CONFLICT        94
FT                   /note="F -> L (in Ref. 3; BAG54116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="M -> V (in Ref. 3; BAB15105)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        577
FT                   /note="Q -> L (in Ref. 3; BAB15105)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   608 AA;  68919 MW;  075D7B839A8D5607 CRC64;
     MGSVTVRYFC YGCLFTSATW TVLLFVYFNF SEVTQPLKNV PVKGSGPHGP SPKKFYPRFT
     RGPSRVLEPQ FKANKIDDVI DSRVEDPEEG HLKFSSELGM IFNERDQELR DLGYQKHAFN
     MLISDRLGYH RDVPDTRNAA CKEKFYPPDL PAASVVICFY NEAFSALLRT VHSVIDRTPA
     HLLHEIILVD DDSDFDDLKG ELDEYVQKYL PGKIKVIRNT KREGLIRGRM IGAAHATGEV
     LVFLDSHCEV NVMWLQPLLA AIREDRHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
     KWDLVPLSEL GRAEGATAPI KSPTMAGGLF AMNRQYFHEL GQYDSGMDIW GGENLEISFR
     IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD
     LKTKSYGNIS ERVELRKKLG CKSFKWYLDN VYPEMQISGS HAKPQQPIFV NRGPKRPKVL
     QRGRLYHLQT NKCLVAQGRP SQKGGLVVLK ACDYSDPNQI WIYNEEHELV LNSLLCLDMS
     ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR AVDPLGQKGS VAMAICDGSS
     SQQWHLEG
//