GLT11_HUMAN
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 03-AUG-2022, entry version 164.
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";
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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 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; 30.
DR IntAct; Q8NCW6; 16.
DR STRING; 9606.ENSP00000416787; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
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; Q8NCW6; -.
DR PeptideAtlas; Q8NCW6; -.
DR PRIDE; Q8NCW6; -.
DR ProteomicsDB; 72960; -. [Q8NCW6-1]
DR ProteomicsDB; 72961; -. [Q8NCW6-2]
DR Antibodypedia; 52579; 124 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 CTD; 63917; -.
DR DisGeNET; 63917; -.
DR GeneCards; GALNT11; -.
DR HGNC; HGNC:19875; GALNT11.
DR HPA; ENSG00000178234; Tissue enhanced (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; FQPWHSR; -.
DR OrthoDB; 606683at2759; -.
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; 8 hits in 1087 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 208 other tissues.
DR ExpressionAtlas; Q8NCW6; baseline and differential.
DR Genevisible; Q8NCW6; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 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
