GLT11_MOUSE
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 03-AUG-2022, entry version 154.
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 GlyGen; Q921L8; 2 sites.
DR iPTMnet; Q921L8; -.
DR PhosphoSitePlus; Q921L8; -.
DR EPD; Q921L8; -.
DR jPOST; Q921L8; -.
DR MaxQB; Q921L8; -.
DR PaxDb; Q921L8; -.
DR PRIDE; Q921L8; -.
DR ProteomicsDB; 271230; -.
DR Antibodypedia; 52579; 124 antibodies from 18 providers.
DR DNASU; 231050; -.
DR Ensembl; ENSMUST00000045737; ENSMUSP00000036240; ENSMUSG00000038072.
DR Ensembl; ENSMUST00000114950; ENSMUSP00000110600; ENSMUSG00000038072.
DR Ensembl; ENSMUST00000114952; ENSMUSP00000110602; ENSMUSG00000038072.
DR GeneID; 231050; -.
DR KEGG; mmu:231050; -.
DR UCSC; uc008wss.1; mouse.
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; FQPWHSR; -.
DR OrthoDB; 606683at2759; -.
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 71 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 257 other tissues.
DR ExpressionAtlas; Q921L8; baseline and differential.
DR Genevisible; Q921L8; MM.
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: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; 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 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
