GLT10_RAT
ID GLT10_RAT Reviewed; 603 AA.
AC Q925R7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Sublingual gland;
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.
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:0000269|PubMed:11278534};
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:0000269|PubMed:11278534};
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: Highly expressed in the sublingual gland, testis,
CC small intestine, colon and ovary. Expressed at intermediate level in
CC heart, brain, spleen, lung, stomach, cervix and uterus.
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 PubMed:11278534, 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 -!- CAUTION: Was originally termed Galnt9/pp-GaNTase 9.
CC {ECO:0000305|PubMed:11278534}.
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DR EMBL; AF241241; AAK54498.1; -; mRNA.
DR RefSeq; NP_570098.1; NM_130742.1.
DR AlphaFoldDB; Q925R7; -.
DR SMR; Q925R7; -.
DR STRING; 10116.ENSRNOP00000003447; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q925R7; 3 sites.
DR PhosphoSitePlus; Q925R7; -.
DR PaxDb; Q925R7; -.
DR PRIDE; Q925R7; -.
DR GeneID; 170501; -.
DR KEGG; rno:170501; -.
DR UCSC; RGD:69409; rat.
DR CTD; 55568; -.
DR RGD; 69409; Galnt10.
DR VEuPathDB; HostDB:ENSRNOG00000002488; -.
DR eggNOG; KOG3736; Eukaryota.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q925R7; -.
DR OMA; DHSNFNY; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; Q925R7; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 5301.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q925R7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002488; Expressed in colon and 18 other tissues.
DR Genevisible; Q925R7; RN.
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; ISO:RGD.
DR GO; GO:0016266; P:O-glycan processing; ISO:RGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
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 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_0000059124"
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"
SQ SEQUENCE 603 AA; 69117 MW; 194EDEAA626A4BBF CRC64;
MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGSGAAVAPE AIQELHSRQK
KTLFLGAEQR LKDWHNKEAI RRDAQRVGNG EQGKPYPMTD AERVDQAYRE NGFNIYVSDK
ISLNRSLPDI RHPNCNSKLY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI
VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASAATG DVITFLDSHC
EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM
EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV
VAQKKLRGSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CTDTKHGTLG
SPLRLETCIR GRGEAAWNSM QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS
MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLENF
NRN
