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Q9GM01 (GALT9_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 9

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 9
Short name=GalNAc-T9
Short name=pp-GaNTase 9
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Gene names
Name:GALNT9
ORF Names:QnpA-13140
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

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 By similarity.

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 606606Polypeptide N-acetylgalactosaminyltransferase 9
PRO_0000059121

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein
Topological domain30 – 606577Lumenal Potential
Domain467 – 603137Ricin B-type lectin
Region153 – 264112Catalytic subdomain A
Region321 – 38363Catalytic subdomain B

Sites

Metal binding2481Manganese By similarity
Metal binding2501Manganese By similarity
Metal binding3801Manganese By similarity
Binding site1941Substrate By similarity
Binding site2251Substrate By similarity
Binding site3831Substrate By similarity
Binding site3881Substrate By similarity

Amino acid modifications

Glycosylation4631N-linked (GlcNAc...) Potential
Disulfide bond144 ↔ 375 By similarity
Disulfide bond366 ↔ 445 By similarity
Disulfide bond480 ↔ 496 By similarity
Disulfide bond528 ↔ 543 By similarity
Disulfide bond570 ↔ 590 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GM01 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A00A97C02BD3BBBD

FASTA60668,318
        10         20         30         40         50         60 
MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRP LSGGCRPRPA TPAPGSPLRS 

        70         80         90        100        110        120 
GGPRAVVAGR AELVLKGQLP AEPCSPGRLM VPEAEAEAQG GLAATLRDDG QEAEGKYEEY 

       130        140        150        160        170        180 
GYNAQLSDRI SLDRSIPDYR PRKCRHMSYA QDLPQVSVVF IFVNEALSVI LRSVHSVVNH 

       190        200        210        220        230        240 
TPSQLLKEVI LVDDNSDNVE LKFNLDQYVN KRYPGLVKIV RNSRREGLIR ARLQGWKAAT 

       250        260        270        280        290        300 
APVVGFFDAH VEFNTGWAEP ALSRIREDRR RIVLPAIDNI KYSTFEVQQY ANAAHGYNWG 

       310        320        330        340        350        360 
LWCMYIIPPQ DWLDRGDESA PIRTPAMIGC SFVVDREYFG DIGLLDPGME VYGGENVELG 

       370        380        390        400        410        420 
MRVWQCGGSM EVLPCSRVAH IERTRKPYNN DIDYYAKRNA LRAAEVWMDD FKSHVYMAWN 

       430        440        450        460        470        480 
IPMTNPGVDF GDVSERLALR QRLKCRSFKW YLENVYPEMR IYNNTLTYGE VRNSKASGYC 

       490        500        510        520        530        540 
LDQGAEDGDR AILYPCHGMS SQLVRYSADG LLQLGPLGST AFLPDSKCLV DDGRGRTPTL 

       550        560        570        580        590        600 
RKCEDVARPT QRLWDFTQSG PIVSRATGRC LEVEMSKDAN FGLRLVVQRC SGQKWMIRNW 


IKHARH 

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References

[1]"Isolation of full-length cDNA clones from macaque brain cDNA libraries."
Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Parietal cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB050509 mRNA. Translation: BAB17277.1.
UniGeneMfa.1709.

3D structure databases

ProteinModelPortalQ9GM01.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG051699.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
IPR001202. WW_dom.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGALT9_MACFA
AccessionPrimary (citable) accession number: Q9GM01
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways