ID   GLT11_MOUSE             Reviewed;         608 AA.
AC   Q921L8; Q3TT83; Q8BU26; Q8K032;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 161.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Shimoji S., Reynolds P.R., Ten Hagen K.G., Tabak L.A.;
RT   "Characterization of a novel mouse UDP-GalNAc:polypeptide N-
RT   acetylgalactosaminyltransferase.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Ovary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   DEVELOPMENTAL STAGE.
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. Displays the same
CC       enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in
CC       glycosylation of erythropoietin (EPO) (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Interacts with NOTCH1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in kidney. Weakly expressed in
CC       other tissues. {ECO:0000269|PubMed:11925450}.
CC   -!- DEVELOPMENTAL STAGE: At 8.0 dpc, present in the left-right organiser
CC       (LRO) node, with enrichment in crown cells compared to pit cells (at
CC       protein level). {ECO:0000269|PubMed:24226769}.
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   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH34184.1; Type=Erroneous termination; Note=Truncated C-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_mou_519";
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DR   EMBL; Y12435; CAC79626.1; -; mRNA.
DR   EMBL; AF495528; AAQ06668.1; -; mRNA.
DR   EMBL; AK088014; BAC40096.1; -; mRNA.
DR   EMBL; AK161524; BAE36442.1; -; mRNA.
DR   EMBL; BC011428; AAH11428.1; -; mRNA.
DR   EMBL; BC021504; AAH21504.1; -; mRNA.
DR   EMBL; BC034184; AAH34184.1; ALT_SEQ; mRNA.
DR   EMBL; BC034185; AAH34185.1; -; mRNA.
DR   EMBL; BC036143; AAH36143.1; -; mRNA.
DR   EMBL; BC036145; AAH36145.1; -; mRNA.
DR   CCDS; CCDS19133.1; -.
DR   RefSeq; NP_659157.1; NM_144908.3.
DR   RefSeq; XP_006535744.1; XM_006535681.3.
DR   RefSeq; XP_011248066.1; XM_011249764.2.
DR   AlphaFoldDB; Q921L8; -.
DR   SMR; Q921L8; -.
DR   STRING; 10090.ENSMUSP00000036240; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q921L8; 2 sites, No reported glycans.
DR   GlyGen; Q921L8; 2 sites.
DR   iPTMnet; Q921L8; -.
DR   PhosphoSitePlus; Q921L8; -.
DR   EPD; Q921L8; -.
DR   jPOST; Q921L8; -.
DR   MaxQB; Q921L8; -.
DR   PaxDb; 10090-ENSMUSP00000036240; -.
DR   ProteomicsDB; 271230; -.
DR   Antibodypedia; 52579; 139 antibodies from 18 providers.
DR   DNASU; 231050; -.
DR   Ensembl; ENSMUST00000045737.14; ENSMUSP00000036240.8; ENSMUSG00000038072.15.
DR   Ensembl; ENSMUST00000114950.2; ENSMUSP00000110600.2; ENSMUSG00000038072.15.
DR   Ensembl; ENSMUST00000114952.8; ENSMUSP00000110602.2; ENSMUSG00000038072.15.
DR   GeneID; 231050; -.
DR   KEGG; mmu:231050; -.
DR   UCSC; uc008wss.1; mouse.
DR   AGR; MGI:2444392; -.
DR   CTD; 63917; -.
DR   MGI; MGI:2444392; Galnt11.
DR   VEuPathDB; HostDB:ENSMUSG00000038072; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000158227; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q921L8; -.
DR   OMA; PVFQPWH; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q921L8; -.
DR   TreeFam; TF313267; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 231050; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Galnt11; mouse.
DR   PRO; PR:Q921L8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q921L8; Protein.
DR   Bgee; ENSMUSG00000038072; Expressed in right kidney and 261 other cell types or tissues.
DR   ExpressionAtlas; Q921L8; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISS: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:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISS: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; Q921L8; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW   Manganese; Membrane; Metal-binding; Notch signaling pathway;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..608
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 11"
FT                   /id="PRO_0000059126"
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:0007744|PubMed:21183079"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   CONFLICT        545
FT                   /note="S -> L (in Ref. 3; BAC40096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   608 AA;  69201 MW;  0E452FDA1CA5668B CRC64;
     MGSITVRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP FPKKFYPRFT
     RGPGRVLDPQ FKANRIDRLM NNHIEDPDKG LSKSSSELGM IFNERDQELR DLGYQKHAFN
     MLISNRLGYH RDVPDTRNAE CRRKSYPTDL PTASIVICFY NEAFSALLRT VHSVVDRTPA
     HLLHEIILVD DSSDFDDLKG ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV
     LVFLDSHCEV NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
     KWDLVPVSEL GGPDGATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW GGENLEISFR
     IWMCGGKLFI LPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD
     LKNKSFGNIS ERVELRKKLG CQSFKWYLDN IYPEMQIPGP NAKPQQPVLI NRGPKRPRVL
     QRGRLYHLQT NKCLVAQGRS SQKGGLVLLK TCDYGDPTQV WIYNEDHELI LNNLLCLDMS
     ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VMDLMDQKGY VGMAICDGSS
     SQQWRLEG
//