GLT13_MOUSE
ID GLT13_MOUSE Reviewed; 556 AA.
AC Q8CF93; Q8BLE4; Q8BYT3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 13;
DE EC=2.4.1.41 {ECO:0000305|PubMed:27629416, ECO:0000305|PubMed:8618846};
DE AltName: Full=Polypeptide GalNAc transferase 13;
DE Short=GalNAc-T13;
DE Short=pp-GaNTase 13;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 13;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13;
GN Name=Galnt13;
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] (ISOFORM 1), FUNCTION, PATHWAY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12407114; DOI=10.1074/jbc.m203094200;
RA Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T.,
RA Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT GalNAc alpha-serine/threonine antigen.";
RL J. Biol. Chem. 278:573-584(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Hypothalamus;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=8618846; DOI=10.1073/pnas.92.26.12070;
RA Hennet T., Hagen F.K., Tabak L.A., Marth J.D.;
RT "T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-
RT transferase gene by site-directed recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12070-12074(1995).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12651884; DOI=10.1093/glycob/cwg062;
RA Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.;
RT "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
RT isoforms in murine tissues determined by real-time PCR: a new view of a
RT large family.";
RL Glycobiology 13:549-557(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27629416; DOI=10.1074/jbc.m116.743955;
RA Xu Y., Pang W., Lu J., Shan A., Zhang Y.;
RT "Polypeptide N-Acetylgalactosaminyltransferase 13 Contributes to
RT Neurogenesis via Stabilizing the Mucin-type O-Glycoprotein Podoplanin.";
RL J. Biol. Chem. 291:23477-23488(2016).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc)
CC residue from UDP-GalNAc to a serine or threonine residue on the protein
CC receptor (PubMed:12407114, PubMed:8618846, PubMed:27629416). Generates
CC GalNAc-O-Ser/Thr structure also known as Tn antigen, which itself is
CC immunogenic but also serves as a precursor for the synthesis of
CC different mucin-type O-glycan core structures (PubMed:12407114).
CC Contributes to the synthesis of O-linked glycans on mucins and
CC proteoglycans of the central nervous system (PubMed:12407114,
CC PubMed:27629416). Can glycosylate both unmodified peptides and
CC glycopeptides that already contain an O-linked GalNAc sugar. Transfers
CC GalNAc to Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC.
CC Transfers GalNAc to three consecutive serine/threonine residues on SDC3
CC forming a triplet-Tn epitope expressed in Purkinje cells of the
CC developing brain (By similarity). May promote neurogenesis through
CC glycosylation and stabilization of PDPN (PubMed:27629416).
CC {ECO:0000250|UniProtKB:Q8IUC8, ECO:0000269|PubMed:12407114,
CC ECO:0000269|PubMed:27629416, ECO:0000269|PubMed:8618846}.
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:0000305|PubMed:27629416, ECO:0000305|PubMed:8618846};
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:0000305|PubMed:27629416, ECO:0000305|PubMed:8618846};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:12407114}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CF93-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CF93-2; Sequence=VSP_011220;
CC -!- TISSUE SPECIFICITY: Specifically expressed in neuronal cells. Not
CC expressed in glial cells such as astrocytes. Expressed at low level.
CC {ECO:0000269|PubMed:12407114, ECO:0000269|PubMed:12651884}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in the developing brain,
CC reaching a peak at 17.5 dpc, followed by a decrease at 19.5 dpc. Highly
CC expressed during the postnatal period. Expressed in cortical neural
CC precursor cells at 17.5 dpc. {ECO:0000269|PubMed:27629416}.
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: No visible phenotype. It however abolishes Tn
CC antigen in neuronal cells. {ECO:0000269|PubMed:8618846}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially wrongly assigned as Galnt8. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 13;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_521";
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DR EMBL; AB082928; BAC54546.1; -; mRNA.
DR EMBL; AK038387; BAC29981.1; -; mRNA.
DR EMBL; AK045417; BAC32353.1; -; mRNA.
DR CCDS; CCDS16041.1; -. [Q8CF93-1]
DR RefSeq; NP_766618.2; NM_173030.2. [Q8CF93-1]
DR RefSeq; XP_006498154.1; XM_006498091.2. [Q8CF93-1]
DR RefSeq; XP_006498155.1; XM_006498092.2. [Q8CF93-1]
DR AlphaFoldDB; Q8CF93; -.
DR SMR; Q8CF93; -.
DR STRING; 10090.ENSMUSP00000108253; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8CF93; 3 sites.
DR iPTMnet; Q8CF93; -.
DR PhosphoSitePlus; Q8CF93; -.
DR MaxQB; Q8CF93; -.
DR PaxDb; Q8CF93; -.
DR PRIDE; Q8CF93; -.
DR ProteomicsDB; 271019; -. [Q8CF93-1]
DR ProteomicsDB; 271020; -. [Q8CF93-2]
DR Antibodypedia; 33696; 156 antibodies from 20 providers.
DR DNASU; 271786; -.
DR Ensembl; ENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
DR Ensembl; ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
DR Ensembl; ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
DR Ensembl; ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
DR GeneID; 271786; -.
DR KEGG; mmu:271786; -.
DR UCSC; uc008jrq.1; mouse. [Q8CF93-1]
DR UCSC; uc012bvm.1; mouse. [Q8CF93-2]
DR CTD; 114805; -.
DR MGI; MGI:2139447; Galnt13.
DR VEuPathDB; HostDB:ENSMUSG00000060988; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000158904; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8CF93; -.
DR OMA; NSNQCLA; -.
DR OrthoDB; 606683at2759; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 271786; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Galnt13; mouse.
DR PRO; PR:Q8CF93; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CF93; protein.
DR Bgee; ENSMUSG00000060988; Expressed in cerebellum lobe and 100 other tissues.
DR ExpressionAtlas; Q8CF93; baseline and differential.
DR Genevisible; Q8CF93; 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:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:MGI.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO:MGI.
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; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..556
FT /note="Polypeptide N-acetylgalactosaminyltransferase 13"
FT /id="PRO_0000059131"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 428..550
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 114..224
FT /note="Catalytic subdomain A"
FT REGION 284..346
FT /note="Catalytic subdomain B"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 343
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10471"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 329..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 441..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 481..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 522..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 466
FT /note="V -> VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011220"
FT CONFLICT 457
FT /note="N -> K (in Ref. 2; BAC32353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 63983 MW; 593934CFD0AED148 CRC64;
MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII
RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI
SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV
INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD
SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL
CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS
GSRSQQWLLR NMTLGT
