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Probable polypeptide N-acetylgalactosaminyltransferase 8 (EC 2.4.1.41) (Polypeptide GalNAc transferase 8) (GalNAc-T8) (pp-GaNTase 8) (Protein-UDP acetylgalactosaminyltransferase 8) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8)

 GALT8_HUMAN             Reviewed;         637 AA.
Q9NY28; B2RU02;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 132.
RecName: Full=Probable polypeptide N-acetylgalactosaminyltransferase 8;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 8;
Short=GalNAc-T8;
Short=pp-GaNTase 8;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 8;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8;
Name=GALNT8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ASN-53;
GLY-267; SER-312; VAL-337; GLY-438; PHE-515 AND MET-611.
TISSUE=Fetal brain;
PubMed=10767557; DOI=10.1016/S0378-1119(00)00050-0;
White K.E., Lorenz B., Evans W.E., Meitinger T., Strom T.M.,
Econs M.J.;
"Molecular cloning of a novel human UDP-GalNAc:polypeptide N-
acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a
candidate autosomal dominant hypophosphatemic rickets (ADHR) gene.";
Gene 246:347-356(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Probably catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, skeletal
muscle, kidney, liver, small intestine and placenta. Weakly
expressed in colon, thymus, spleen, lung and leukocyte.
{ECO:0000269|PubMed:10767557}.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Probable polypeptide N-acetylgalactosaminyltransferase 8;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_490";
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EMBL; AJ271385; CAB89199.1; -; mRNA.
EMBL; BC140888; AAI40889.1; -; mRNA.
EMBL; BC140889; AAI40890.1; -; mRNA.
CCDS; CCDS8533.1; -.
RefSeq; NP_059113.1; NM_017417.1.
UniGene; Hs.511985; -.
ProteinModelPortal; Q9NY28; -.
SMR; Q9NY28; -.
BioGrid; 117671; 5.
IntAct; Q9NY28; 1.
STRING; 9606.ENSP00000252318; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q9NY28; -.
PhosphoSitePlus; Q9NY28; -.
BioMuta; GALNT8; -.
DMDM; 51316106; -.
EPD; Q9NY28; -.
PaxDb; Q9NY28; -.
PeptideAtlas; Q9NY28; -.
PRIDE; Q9NY28; -.
Ensembl; ENST00000252318; ENSP00000252318; ENSG00000130035.
GeneID; 26290; -.
KEGG; hsa:26290; -.
UCSC; uc001qne.2; human.
CTD; 26290; -.
DisGeNET; 26290; -.
EuPathDB; HostDB:ENSG00000130035.6; -.
GeneCards; GALNT8; -.
HGNC; HGNC:4130; GALNT8.
HPA; HPA012638; -.
HPA; HPA073461; -.
MIM; 606250; gene.
neXtProt; NX_Q9NY28; -.
OpenTargets; ENSG00000130035; -.
PharmGKB; PA28543; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00900000140827; -.
HOGENOM; HOG000038228; -.
HOVERGEN; HBG051699; -.
InParanoid; Q9NY28; -.
KO; K00710; -.
OrthoDB; EOG091G036Q; -.
PhylomeDB; Q9NY28; -.
TreeFam; TF352661; -.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; GALNT8; human.
GenomeRNAi; 26290; -.
PRO; PR:Q9NY28; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000130035; -.
CleanEx; HS_GALNT8; -.
ExpressionAtlas; Q9NY28; baseline and differential.
Genevisible; Q9NY28; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Polymorphism; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 637 Probable polypeptide N-
acetylgalactosaminyltransferase 8.
/FTId=PRO_0000059119.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 637 Lumenal. {ECO:0000255}.
DOMAIN 496 634 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 180 294 Catalytic subdomain A.
REGION 351 412 Catalytic subdomain B.
METAL 278 278 Manganese. {ECO:0000250}.
METAL 280 280 Manganese. {ECO:0000250}.
METAL 409 409 Manganese. {ECO:0000250}.
BINDING 221 221 Substrate. {ECO:0000250}.
BINDING 255 255 Substrate. {ECO:0000250}.
BINDING 412 412 Substrate. {ECO:0000250}.
BINDING 417 417 Substrate. {ECO:0000250}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 171 404 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 395 474 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 509 525 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 556 571 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 599 617 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VARIANT 53 53 Y -> D (in dbSNP:rs10849133).
/FTId=VAR_019581.
VARIANT 53 53 Y -> N (in dbSNP:rs10849133).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019582.
VARIANT 234 234 E -> K (in dbSNP:rs16931676).
/FTId=VAR_033947.
VARIANT 267 267 E -> G (in dbSNP:rs34776842).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019583.
VARIANT 312 312 F -> S (in dbSNP:rs34829532).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019584.
VARIANT 337 337 A -> V (in dbSNP:rs199920896).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019585.
VARIANT 438 438 D -> G (in dbSNP:rs559663039).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019586.
VARIANT 515 515 V -> F (in dbSNP:rs1468556).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019587.
VARIANT 611 611 V -> M (in dbSNP:rs34114277).
{ECO:0000269|PubMed:10767557}.
/FTId=VAR_019588.
VARIANT 630 630 D -> G (in dbSNP:rs16931692).
/FTId=VAR_049241.
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


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