ID GLT10_MOUSE Reviewed; 603 AA.
AC Q6P9S7; Q6KAQ2; Q8BZU8; Q91YJ6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 149.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 10;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 10;
DE Short=GalNAc-T10;
DE Short=pp-GaNTase 10;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 10;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10;
GN Name=Galnt10;
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 [LARGE SCALE MRNA].
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-603.
RC STRAIN=C57BL/6J; TISSUE=Colon;
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 TISSUE SPECIFICITY.
RX PubMed=11278534; DOI=10.1074/jbc.m009638200;
RA Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K.,
RA Balys M.M., Beres T.M., Degand P., Tabak L.A.;
RT "Cloning and characterization of a ninth member of the UDP-
RT GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-
RT T9.";
RL J. Biol. Chem. 276:17395-17404(2001).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward Muc5Ac and EA2 peptide substrates (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at higher level than GALNT9. In the
CC developing hindbrain region of 14.5 dpc embryos it accumulates in the
CC rapidly dividing, undifferentiated ventricular zone adjacent to the
CC pons. It also accumulates in the regions immediately rostral and caudal
CC to the dorsal rhombic lips differentiating into the cerebellum. Not
CC expressed in the developing choroid plexus.
CC {ECO:0000269|PubMed:11278534}.
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 -!- CAUTION: According to experiments made in rat, this enzyme is unable to
CC transfer GalNAc onto serine or threonine residue on the protein
CC receptor, but instead requires the prior addition of a GalNAc on a
CC peptide before adding additional GalNAc moieties, thereby acting as a
CC glycopeptide transferase. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD21405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 10;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_518";
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DR EMBL; AK131155; BAD21405.1; ALT_INIT; mRNA.
DR EMBL; BC016585; AAH16585.1; ALT_INIT; mRNA.
DR EMBL; BC060617; AAH60617.1; -; mRNA.
DR EMBL; AK033515; BAC28334.1; -; mRNA.
DR CCDS; CCDS24719.1; -.
DR RefSeq; NP_598950.2; NM_134189.2.
DR AlphaFoldDB; Q6P9S7; -.
DR SMR; Q6P9S7; -.
DR STRING; 10090.ENSMUSP00000065096; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyCosmos; Q6P9S7; 3 sites, No reported glycans.
DR GlyGen; Q6P9S7; 3 sites.
DR PhosphoSitePlus; Q6P9S7; -.
DR SwissPalm; Q6P9S7; -.
DR MaxQB; Q6P9S7; -.
DR PaxDb; 10090-ENSMUSP00000065096; -.
DR ProteomicsDB; 270999; -.
DR Pumba; Q6P9S7; -.
DR Antibodypedia; 2029; 190 antibodies from 25 providers.
DR DNASU; 171212; -.
DR Ensembl; ENSMUST00000066987.14; ENSMUSP00000065096.8; ENSMUSG00000020520.15.
DR GeneID; 171212; -.
DR KEGG; mmu:171212; -.
DR UCSC; uc007jab.1; mouse.
DR AGR; MGI:1890480; -.
DR CTD; 55568; -.
DR MGI; MGI:1890480; Galnt10.
DR VEuPathDB; HostDB:ENSMUSG00000020520; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156690; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q6P9S7; -.
DR OMA; DHSNFNY; -.
DR OrthoDB; 202750at2759; -.
DR PhylomeDB; Q6P9S7; -.
DR TreeFam; TF313267; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 171212; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Galnt10; mouse.
DR PRO; PR:Q6P9S7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6P9S7; Protein.
DR Bgee; ENSMUSG00000020520; Expressed in spermatocyte and 228 other cell types or tissues.
DR ExpressionAtlas; Q6P9S7; baseline and differential.
DR Genevisible; Q6P9S7; MM.
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:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0016266; P:O-glycan processing; ISO:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
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:SF41; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 10; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..603
FT /note="Polypeptide N-acetylgalactosaminyltransferase 10"
FT /id="PRO_0000059123"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..603
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 458..590
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 144..253
FT /note="Catalytic subdomain A"
FT REGION 311..373
FT /note="Catalytic subdomain B"
FT REGION 373..384
FT /note="Flexible loop"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 356..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 471..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 523..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 563..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT CONFLICT 233
FT /note="V -> I (in Ref. 1; BAD21405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 69116 MW; FF55FBA7E1DD7544 CRC64;
MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGLGAAVAPA AVQELHSRQK
KTFFLGAEQR LKDWHNKEAI RRDAQRVGYG EQGKPYPMTD AERVDQAYRE NGFNIYVSDK
ISLNRSLPDI RHPNCNSKLY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI
VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASAATG DVVTFLDSHC
EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM
EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV
VAQKKLRVSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CTDTKLGTLG
SPLRLETCIR GRGEAAWNSM QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS
MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRVFMNTCNP SSLTQQWLFE HTNSTVLENF
NKN
//
