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   24-JAN-2024, entry version 77.
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.A8Y236; -.
DR   GlyCosmos; A8Y236; 2 sites, No reported glycans.
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; 202750at2759; -.
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: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; 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:SF134; N-ACETYLGALACTOSAMINYLTRANSFERASE 4-RELATED; 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   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
//