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Polypeptide N-acetylgalactosaminyltransferase 9 (EC 2.4.1.41) (Polypeptide GalNAc transferase 9) (GalNAc-T9) (pp-GaNTase 9) (Protein-UDP acetylgalactosaminyltransferase 9) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9)

 GALT9_HUMAN             Reviewed;         603 AA.
Q9HCQ5; Q52LR8; Q6NT54; Q8NFR1;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 3.
28-FEB-2018, entry version 137.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 9;
EC=2.4.1.41 {ECO:0000269|PubMed:12407114};
AltName: Full=Polypeptide GalNAc transferase 9;
Short=GalNAc-T9;
Short=pp-GaNTase 9;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
Name=GALNT9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=10978536; DOI=10.1016/S0167-4781(00)00180-9;
Toba S., Tenno M., Konishi M., Mikami T., Itoh N., Kurosaka A.;
"Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-
acetylgalactosaminyltransferase (GalNAc-T9).";
Biochim. Biophys. Acta 1493:264-268(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
Guo J.H., Zan Q., Yu L.;
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
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).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=12407114; DOI=10.1074/jbc.M203094200;
Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T.,
Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M.,
Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D.,
Narimatsu H.;
"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase,
designated pp-GalNAc-T13, that is specifically expressed in neurons
and synthesizes GalNAc alpha-serine/threonine antigen.";
J. Biol. Chem. 278:573-584(2003).
-!- FUNCTION: 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. Does not glycosylate apomucin or SDC3.
{ECO:0000269|PubMed:10978536, ECO:0000269|PubMed:12407114}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:12407114}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:12407114}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HCQ5-1; Sequence=Displayed;
Name=2;
IsoId=Q9HCQ5-2; Sequence=VSP_011206;
-!- TISSUE SPECIFICITY: Specifically expressed in brain. Not expressed
in heart, placenta, lung, liver, skeletal muscle, kidney,
pancreas, spleen, thymus, prostate, testis, ovary, small
intestine, colon and leukocyte. In brain, it is expressed in
cerebellum, frontal lobe, temporal lobe, putamen and spinal cord,
weakly expressed in cerebral cortex. Not expressed in medulla and
occipital pole. {ECO:0000269|PubMed:10978536}.
-!- 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=Polypeptide N-acetylgalactosaminyltransferase 9;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_491";
-----------------------------------------------------------------------
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EMBL; AB040672; BAB13699.2; -; mRNA.
EMBL; AF458594; AAM49722.1; -; mRNA.
EMBL; BC093817; AAH93817.2; -; mRNA.
EMBL; BC093819; AAH93819.2; -; mRNA.
CCDS; CCDS41866.1; -. [Q9HCQ5-2]
CCDS; CCDS81755.1; -. [Q9HCQ5-1]
RefSeq; NP_001116108.1; NM_001122636.1.
RefSeq; NP_068580.2; NM_021808.3. [Q9HCQ5-2]
UniGene; Hs.301062; -.
UniGene; Hs.658249; -.
ProteinModelPortal; Q9HCQ5; -.
SMR; Q9HCQ5; -.
BioGrid; 119094; 1.
IntAct; Q9HCQ5; 1.
STRING; 9606.ENSP00000380488; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q9HCQ5; -.
PhosphoSitePlus; Q9HCQ5; -.
BioMuta; GALNT9; -.
DMDM; 143811393; -.
PaxDb; Q9HCQ5; -.
PeptideAtlas; Q9HCQ5; -.
PRIDE; Q9HCQ5; -.
DNASU; 50614; -.
Ensembl; ENST00000397325; ENSP00000380488; ENSG00000182870. [Q9HCQ5-2]
Ensembl; ENST00000541995; ENSP00000440544; ENSG00000182870. [Q9HCQ5-2]
GeneID; 50614; -.
KEGG; hsa:50614; -.
UCSC; uc001uka.3; human. [Q9HCQ5-1]
CTD; 50614; -.
DisGeNET; 50614; -.
EuPathDB; HostDB:ENSG00000182870.12; -.
GeneCards; GALNT9; -.
HGNC; HGNC:4131; GALNT9.
HPA; HPA075016; -.
MIM; 606251; gene.
neXtProt; NX_Q9HCQ5; -.
OpenTargets; ENSG00000182870; -.
PharmGKB; PA28544; -.
GeneTree; ENSGT00900000140827; -.
HOGENOM; HOG000038228; -.
HOVERGEN; HBG051699; -.
InParanoid; Q9HCQ5; -.
KO; K00710; -.
PhylomeDB; Q9HCQ5; -.
TreeFam; TF313267; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; GALNT9; human.
GenomeRNAi; 50614; -.
PRO; PR:Q9HCQ5; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000182870; -.
CleanEx; HS_GALNT9; -.
ExpressionAtlas; Q9HCQ5; baseline and differential.
Genevisible; Q9HCQ5; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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.
GO; GO:0006493; P:protein O-linked glycosylation; NAS:UniProtKB.
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.
InterPro; IPR001202; WW_dom.
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.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 603 Polypeptide N-
acetylgalactosaminyltransferase 9.
/FTId=PRO_0000059120.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 603 Lumenal. {ECO:0000255}.
DOMAIN 464 600 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 150 261 Catalytic subdomain A.
REGION 318 380 Catalytic subdomain B.
METAL 245 245 Manganese. {ECO:0000250}.
METAL 247 247 Manganese. {ECO:0000250}.
METAL 377 377 Manganese. {ECO:0000250}.
BINDING 191 191 Substrate. {ECO:0000250}.
BINDING 222 222 Substrate. {ECO:0000250}.
BINDING 380 380 Substrate. {ECO:0000250}.
BINDING 385 385 Substrate. {ECO:0000250}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 141 372 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 363 442 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 477 493 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 525 540 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 567 587 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 1 366 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_011206.
CONFLICT 539 539 K -> R (in Ref. 1; BAB13699).
{ECO:0000305}.
SEQUENCE 603 AA; 68359 MW; 4B5888733D8577CF CRC64;
MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR HAKVGTLGDR
EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA ATLRDDGQEA EGKYEEYGYN
AQLSDRISLD RSIPDYRPRK CRQMSYAQDL PQVSVVFIFV NEALSVILRS VHSVVNHTPS
QLLKEVILVD DNSDNVELKF NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV
VGFFDAHVEF NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC
MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG GENVELGMRV
WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA AEVWMDDFKS HVYMAWNIPM
SNPGVDFGDV SERLALRQRL KCRSFKWYLE NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ
GAEDGDRAIL YPCHGMSSQL VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC
EDVARPTQRL WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH
ARH


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