GLT10_CAEBR
ID GLT10_CAEBR Reviewed; 629 AA.
AC A8Y236;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 10;
DE Short=pp-GaNTase 10;
DE EC=2.4.1.41;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 10;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10;
GN Name=gly-10 {ECO:0000250|UniProtKB:O45947}; ORFNames=CBG22373;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: May catalyze 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.
CC {ECO:0000250|UniProtKB:Q86SR1}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q10472};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q86SR1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q10472}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q10472}.
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|UniProtKB:O08912}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250|UniProtKB:Q10473}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000255}.
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DR EMBL; HE600912; CAP38976.2; -; Genomic_DNA.
DR AlphaFoldDB; A8Y236; -.
DR SMR; A8Y236; -.
DR STRING; 6238.CBG22373; -.
DR PRIDE; A8Y236; -.
DR WormBase; CBG22373; CBP40797; WBGene00040946; Cbr-gly-10.
DR eggNOG; KOG3736; Eukaryota.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; A8Y236; -.
DR OMA; DHSNFNY; -.
DR OrthoDB; 276134at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008549; Chromosome IV.
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; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 3: Inferred from homology;
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..629
FT /note="Putative polypeptide N-
FT acetylgalactosaminyltransferase 10"
FT /id="PRO_0000328999"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 34..629
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 526..629
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 163..275
FT /note="Catalytic subdomain A"
FT REGION 331..393
FT /note="Catalytic subdomain B"
FT REGION 393..406
FT /note="Flexible loop"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 376..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 493..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 539..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 582..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 629 AA; 73008 MW; FCD8FD9F61829238 CRC64;
MGLSRYLSRR HHWVIQYCAL LLFLYFIYSY VAVSNDAPRL NEEIPVFREF SEDLPQGSRK
FPEQKPAAAL GDEALDPFEK YRGHEKIKWE DEVAYEKDKA REGPGEWGKP VKLPDDKETE
KEALSLYKAN GYNAYISDMI SLNRSIKDIR HKECKKMTYS AKLPTVSVIF PFHEEHNSTL
LRSVYSVINR SPPELLKEII LVDDFSEKPA LRQPLEDFLK KNKIDHIVKI LRTKKREGLI
RGRQLGAQEA TGEILIFLDA HSECNYNWLP PLLDPIADDY RTVVCPFVDV IDCETYEIRP
QDEGARGSFD WAFNYKRLPL TKKDRENPTK PFDSPVMAGG YFAISAKWFW ELGGYDEGLD
IWGGEQYELS FKVWQCHGKM VDAPCSRVAH IYRCKYAPFK NAGMGDFVSR NYKRVAEVWM
DEYKETLYKH RPGIGNADAG DLKLMKGIRE KLQCKSFDWF MKEIAFDQDK YYPAIEPKAS
AEGEIRHVAS NLCIDTQFKE QNQRFGLRKC ASEDKDGGGE QDLRLTRWHD IRPKGRKICF
DVSTSVDKAP IILFDCHSMK GNQLFKYRMP QKQIYHPVSG QCLTADENGK GFLHMKKCDS
SSKLQQWAWQ TIDQELLDQR QANEHKELE
