ID   GLT11_XENTR             Reviewed;         601 AA.
AC   Q6DJR8;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   03-AUG-2022, entry version 91.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, 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).
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.
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   -!- 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Interacts with notch1. {ECO:0000269|PubMed:24226769}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
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   -!- DISRUPTION PHENOTYPE: Aberrant left-right patterning resulting in
CC       abnormal cardiac loops, including leftward and symmetric/midline loops.
CC       {ECO:0000269|PubMed:24226769}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH75106.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC075106; AAH75106.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001006904.1; NM_001006903.1.
DR   AlphaFoldDB; Q6DJR8; -.
DR   SMR; Q6DJR8; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   DNASU; 448751; -.
DR   GeneID; 448751; -.
DR   KEGG; xtr:448751; -.
DR   CTD; 63917; -.
DR   Xenbase; XB-GENE-981830; galnt11.
DR   OrthoDB; 606683at2759; -.
DR   Reactome; R-XTR-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000040522; Expressed in mesonephros and 12 other tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005112; F:Notch binding; IDA:UniProtKB.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
DR   GO; GO:0007220; P:Notch receptor processing; IMP:UniProtKB.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IMP:UniProtKB.
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; IMP: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   Calcium; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Lectin; Manganese; Membrane; Notch signaling pathway;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..601
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 11"
FT                   /id="PRO_0000425208"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..601
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          469..600
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          143..254
FT                   /note="Catalytic subdomain A"
FT                   /evidence="ECO:0000250"
FT   REGION          312..374
FT                   /note="Catalytic subdomain B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        486..505
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        529..546
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        571..589
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ   SEQUENCE   601 AA;  68383 MW;  1FA0294A3CEEA236 CRC64;
     MGSAALRCFC YGCLFTSVTW TLLLFIYFNF SEESQGFRHV PVKGLEPYKP LPKKIYPRFS
     RDSMGQHSDP RKGHNGNQLE TEANADLSPE LGMIFNEQDQ DVRDVGYQKH AFNLLISNRL
     GYHRDVPDTR DSKCAKKTYP PDLPMASIVI CFYNEAFSAL LRTVHSVLDR TPAQLLHEII
     LVDDNSELDD LKKDLDGYMQ ENLSKKVKLV RNKQREGLIR GRMVGASHAT GDVLVFLDSH
     CEVNEMWLQP LLAPIKENPR TVVCPVIDII SADTLIYSSS PVVRGGFNWG LHFKWDPVPL
     AELGGPEGFS APFRSPTMAG GLFAMDREYF NMLGQYDSGM DIWGGENLEI SFRIWMCGGS
     LLIVPCSRVG HIFRKRRPYG SPGGHDTMAH NSLRLAHVWM DEYKDQYFAL RPELRNRDFG
     DIRERLALRR RLNCKSFKWY LDNIYPEMQV SGPNAKPQPP VFMNKGQKRP KILQRGRLIN
     MQTNRCLVAQ GHPSQKGGLV VAKECDYNDS EQVWSYNEEH ELILSNLLCL DMSETRSSDP
     PRLMKCHGSG GSQQWVFGKS NRLYQVSVGQ CLKLVDPMSR KGYVSMAICD GSPSQQWHLE
     N