GALT8_HUMAN
ID GALT8_HUMAN Reviewed; 637 AA.
AC Q9NY28; B2RU02;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable polypeptide N-acetylgalactosaminyltransferase 8 {ECO:0000305};
DE EC=2.4.1.41 {ECO:0000250|UniProtKB:Q9HCQ5};
DE AltName: Full=Polypeptide GalNAc transferase 8;
DE Short=GalNAc-T8;
DE Short=pp-GaNTase 8;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 8;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8;
GN Name=GALNT8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ASN-53;
RP GLY-267; SER-312; VAL-337; GLY-438; PHE-515 AND MET-611.
RC TISSUE=Fetal brain;
RX PubMed=10767557; DOI=10.1016/s0378-1119(00)00050-0;
RA White K.E., Lorenz B., Evans W.E., Meitinger T., Strom T.M., Econs M.J.;
RT "Molecular cloning of a novel human UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate
RT autosomal dominant hypophosphatemic rickets (ADHR) gene.";
RL Gene 246:347-356(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Probably catalyzes the initial reaction in O-linked
CC oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
CC galactosamine residue to a serine or threonine residue on the protein
CC receptor. {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;
CC Evidence={ECO:0000250|UniProtKB:Q10471};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9HCQ5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9HCQ5}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, skeletal
CC muscle, kidney, liver, small intestine and placenta. Weakly expressed
CC in colon, thymus, spleen, lung and leukocyte.
CC {ECO:0000269|PubMed:10767557}.
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:Q8N4A0}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Probable
CC polypeptide N-acetylgalactosaminyltransferase 8;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_490";
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DR EMBL; AJ271385; CAB89199.1; -; mRNA.
DR EMBL; BC140888; AAI40889.1; -; mRNA.
DR EMBL; BC140889; AAI40890.1; -; mRNA.
DR CCDS; CCDS8533.1; -.
DR RefSeq; NP_059113.1; NM_017417.1.
DR AlphaFoldDB; Q9NY28; -.
DR SMR; Q9NY28; -.
DR BioGRID; 117671; 8.
DR IntAct; Q9NY28; 1.
DR STRING; 9606.ENSP00000252318; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q9NY28; 3 sites.
DR iPTMnet; Q9NY28; -.
DR PhosphoSitePlus; Q9NY28; -.
DR BioMuta; GALNT8; -.
DR DMDM; 51316106; -.
DR EPD; Q9NY28; -.
DR MassIVE; Q9NY28; -.
DR PaxDb; Q9NY28; -.
DR PeptideAtlas; Q9NY28; -.
DR PRIDE; Q9NY28; -.
DR ProteomicsDB; 83157; -.
DR Antibodypedia; 2423; 59 antibodies from 12 providers.
DR DNASU; 26290; -.
DR Ensembl; ENST00000252318.7; ENSP00000252318.2; ENSG00000130035.9.
DR GeneID; 26290; -.
DR KEGG; hsa:26290; -.
DR MANE-Select; ENST00000252318.7; ENSP00000252318.2; NM_017417.2; NP_059113.1.
DR UCSC; uc001qne.2; human.
DR CTD; 26290; -.
DR DisGeNET; 26290; -.
DR GeneCards; GALNT8; -.
DR HGNC; HGNC:4130; GALNT8.
DR HPA; ENSG00000130035; Group enriched (intestine, testis).
DR MIM; 606250; gene.
DR neXtProt; NX_Q9NY28; -.
DR OpenTargets; ENSG00000130035; -.
DR PharmGKB; PA28543; -.
DR VEuPathDB; HostDB:ENSG00000130035; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160161; -.
DR HOGENOM; CLU_013477_4_1_1; -.
DR InParanoid; Q9NY28; -.
DR OMA; GLHIYWD; -.
DR OrthoDB; 271144at2759; -.
DR PhylomeDB; Q9NY28; -.
DR TreeFam; TF352661; -.
DR PathwayCommons; Q9NY28; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9NY28; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 26290; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; GALNT8; human.
DR GenomeRNAi; 26290; -.
DR Pharos; Q9NY28; Tbio.
DR PRO; PR:Q9NY28; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NY28; protein.
DR Bgee; ENSG00000130035; Expressed in cortical plate and 156 other tissues.
DR ExpressionAtlas; Q9NY28; baseline and differential.
DR Genevisible; Q9NY28; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:0016266; P:O-glycan processing; TAS:Reactome.
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 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..637
FT /note="Probable polypeptide N-
FT acetylgalactosaminyltransferase 8"
FT /id="PRO_0000059119"
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 /evidence="ECO:0000255"
FT TOPO_DOM 30..637
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 496..634
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 180..294
FT /note="Catalytic subdomain A"
FT REGION 351..412
FT /note="Catalytic subdomain B"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 395..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 509..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 556..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 599..617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VARIANT 53
FT /note="Y -> D (in dbSNP:rs10849133)"
FT /id="VAR_019581"
FT VARIANT 53
FT /note="Y -> N (in dbSNP:rs10849133)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019582"
FT VARIANT 234
FT /note="E -> K (in dbSNP:rs16931676)"
FT /id="VAR_033947"
FT VARIANT 267
FT /note="E -> G (in dbSNP:rs34776842)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019583"
FT VARIANT 312
FT /note="F -> S (in dbSNP:rs34829532)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019584"
FT VARIANT 337
FT /note="A -> V (in dbSNP:rs199920896)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019585"
FT VARIANT 438
FT /note="D -> G (in dbSNP:rs559663039)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019586"
FT VARIANT 515
FT /note="V -> F (in dbSNP:rs1468556)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019587"
FT VARIANT 611
FT /note="V -> M (in dbSNP:rs34114277)"
FT /evidence="ECO:0000269|PubMed:10767557"
FT /id="VAR_019588"
FT VARIANT 630
FT /note="D -> G (in dbSNP:rs16931692)"
FT /id="VAR_049241"
SQ SEQUENCE 637 AA; 72851 MW; 4C8BA5DC9A9A1F64 CRC64;
MMFWRKLPKA LFIGLTLAIA VNLLLVFSSK GTLQNLFTGG LHRELPLHLN KRYGAVIKRL
SHLEVELQDL KESMKLALRQ QENVNSTLKR AKDEVRPLLK AMETKVNETK KHKTQMKLFP
HSQLFRQWGE DLSEAQQKAA QDLFRKFGYN AYLSNQLPLN RTIPDTRDYR CLRKTYPSQL
PSLSVILIFV NEALSIIQRA ITSIINRTPS RLLKEIILVD DFSSNGELKV HLDEKIKLYN
QKYPGLLKII RHPERKGLAQ ARNTGWEAAT ADVVAILDAH IEVNVGWAEP ILARIQEDRT
VIVSPVFDNI RFDTFKLDKY ELAVDGFNWE LWCRYDALPQ AWIDLHDVTA PVKSPSIMGI
LAANRHFLGE IGSLDGGMLI YGGENVELSL RVWQCGGKVE ILPCSRIAHL ERHHKPYALD
LTAALKRNAL RVAEIWMDEH KHMVYLAWNI PLQNSGIDFG DVSSRMALRE KLKCKTFDWY
LKNVYPLLKP LHTIVGYGRM KNLLDENVCL DQGPVPGNTP IMYYCHEFSS QNVYYHLTGE
LYVGQLIAEA SASDRCLTDP GKAEKPTLEP CSKAAKNRLH IYWDFKPGGA VINRDTKRCL
EMKKDLLGSH VLVLQTCSTQ VWEIQHTVRD WGQTNSQ
