GALT9_MACFA
ID GALT9_MACFA Reviewed; 606 AA.
AC Q9GM01;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 9;
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q9HCQ5};
DE AltName: Full=Polypeptide GalNAc transferase 9;
DE Short=GalNAc-T9;
DE Short=pp-GaNTase 9;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
GN Name=GALNT9; ORFNames=QnpA-13140;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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. Does not
CC glycosylate apomucin or SDC3. {ECO:0000250|UniProtKB:Q9HCQ5}.
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:0000250|UniProtKB:Q9HCQ5};
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:0000250|UniProtKB:Q9HCQ5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9HCQ5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
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}.
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DR EMBL; AB050509; BAB17277.1; -; mRNA.
DR RefSeq; NP_001306356.1; NM_001319427.1.
DR AlphaFoldDB; Q9GM01; -.
DR SMR; Q9GM01; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GeneID; 102117136; -.
DR CTD; 50614; -.
DR eggNOG; KOG3736; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000233100; Unplaced.
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; IEA:UniProtKB-EC.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:UniProt.
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..606
FT /note="Polypeptide N-acetylgalactosaminyltransferase 9"
FT /id="PRO_0000059121"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 30..606
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 467..603
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..264
FT /note="Catalytic subdomain A"
FT REGION 321..383
FT /note="Catalytic subdomain B"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 366..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 480..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 528..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 570..590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 606 AA; 68318 MW; A00A97C02BD3BBBD CRC64;
MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRP LSGGCRPRPA TPAPGSPLRS
GGPRAVVAGR AELVLKGQLP AEPCSPGRLM VPEAEAEAQG GLAATLRDDG QEAEGKYEEY
GYNAQLSDRI SLDRSIPDYR PRKCRHMSYA QDLPQVSVVF IFVNEALSVI LRSVHSVVNH
TPSQLLKEVI LVDDNSDNVE LKFNLDQYVN KRYPGLVKIV RNSRREGLIR ARLQGWKAAT
APVVGFFDAH VEFNTGWAEP ALSRIREDRR RIVLPAIDNI KYSTFEVQQY ANAAHGYNWG
LWCMYIIPPQ DWLDRGDESA PIRTPAMIGC SFVVDREYFG DIGLLDPGME VYGGENVELG
MRVWQCGGSM EVLPCSRVAH IERTRKPYNN DIDYYAKRNA LRAAEVWMDD FKSHVYMAWN
IPMTNPGVDF GDVSERLALR QRLKCRSFKW YLENVYPEMR IYNNTLTYGE VRNSKASGYC
LDQGAEDGDR AILYPCHGMS SQLVRYSADG LLQLGPLGST AFLPDSKCLV DDGRGRTPTL
RKCEDVARPT QRLWDFTQSG PIVSRATGRC LEVEMSKDAN FGLRLVVQRC SGQKWMIRNW
IKHARH
