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O88422 (GALT5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. 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 5
EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 5
Short name=GalNAc-T5
Short name=pp-GaNTase 5
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene names
Name:Galnt5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length930 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. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2, Muc1b, rMuc-2 or mG-Muc substrates.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 By similarity.

Subcellular location

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

Tissue specificity

Predominantly expressed in sublingual gland. Expressed at lower level in stomach and small intestine. Weakly or not expressed in submandibular gland, parotid gland, kidney, liver, heart, brain, spleen, lung, skeletal muscle, testis, ovary, cervix and uterus. Ref.1

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 – 930930Polypeptide N-acetylgalactosaminyltransferase 5
PRO_0000059112

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 930895Lumenal Potential
Domain794 – 925132Ricin B-type lectin
Region485 – 594110Catalytic subdomain A
Region654 – 71663Catalytic subdomain B

Amino acid modifications

Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Potential
Glycosylation8171N-linked (GlcNAc...) Potential
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation9021N-linked (GlcNAc...) Potential
Disulfide bond812 ↔ 825 By similarity
Disulfide bond848 ↔ 863 By similarity
Disulfide bond898 ↔ 913 By similarity

Sequences

Sequence LengthMass (Da)Tools
O88422 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 1C906A76F320A225

FASTA930105,120
        10         20         30         40         50         60 
MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTGILKEDIM RREQTGFRVE 

        70         80         90        100        110        120 
ADQMTILSPS SRGMRPPRNG AGGKESFRKA ENRVLKVEEN VDQVQRKGKM QFLLGRGKAV 

       130        140        150        160        170        180 
SLWHRTHVQT LPVTLPMQKT QGRDSKPEVS SLHMMSKQTT VLGSEKDSFT VSRGVPLNKT 

       190        200        210        220        230        240 
AEHTETLDKK QEAPENYNLS SDTSKQASQR ALNVTISVRT DRSKQQSQTV TKSSIQFASL 

       250        260        270        280        290        300 
PILKPEEVTV TKKTEAQGKD LKYEAHKARP LLKFTADVGH LKKQSTNETG LGVLPEADGA 

       310        320        330        340        350        360 
KVAPGKKLNF SESQIVIITK EEGQKTDTKE VPNSKIQTVF PKLLGESQGK HIPRSQSQTL 

       370        380        390        400        410        420 
SSPLAPKRAV SQSKPTLAEE LHTARSNLTA KATTVGHQQS HANISENPGK HHVLRIDVTL 

       430        440        450        460        470        480 
SPRDLNAPGQ FGRPVVVPPG KKKEAEQRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL 

       490        500        510        520        530        540 
VHNDLPTTSI IMCFVDEVWS ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK DYLKANLDKY 

       550        560        570        580        590        600 
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 

       610        620        630        640        650        660 
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWRTIP PDVIAKNGIK ETDIIRCPVM 

       670        680        690        700        710        720 
AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP 

       730        740        750        760        770        780 
YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCQ 

       790        800        810        820        830        840 
SFKWYLDNVF PDLKAPVVRA SGVFINLALG KCVSIKNITV VLEDCDGSSE LQQFNYTWVR 

       850        860        870        880        890        900 
LIKHGEWCVA PIPDKGSLTL YPCDNRNNRL KWLHRSASAF HPELVDHIVF ESYQQLLCME 

       910        920        930 
GNFSQKTLKL AACNPTEPQQ KWKFEKYYDV

« Hide

References

[1]"Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family."
Ten Hagen K.G., Hagen F.K., Balys M.M., Beres T.M., Van Wuyckhuyse B., Tabak L.A.
J. Biol. Chem. 273:27749-27754(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Sublingual gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF049344 mRNA. Translation: AAC69708.1.
IPIIPI00209506.
RefSeqNP_113984.1. NM_031796.1.
UniGeneRn.30048.

3D structure databases

ProteinModelPortalO88422.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000006319.

Protein family/group databases

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

Proteomic databases

PaxDbO88422.
PRIDEO88422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006319; ENSRNOP00000006319; ENSRNOG00000004645.
GeneID83627.
KEGGrno:83627.
UCSCRGD:620361. rat.

Organism-specific databases

CTD11227.
RGD620361. Galnt5.

Phylogenomic databases

eggNOGNOG307550.
GeneTreeENSGT00680000099551.
HOGENOMHOG000231869.
HOVERGENHBG051698.
InParanoidO88422.
KOK00710.
OMAEGNFSQK.
OrthoDBEOG41G33C.

Enzyme and pathway databases

BRENDA2.4.1.41. 5301.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorO88422.
GermOnlineENSRNOG00000004645. Rattus norvegicus.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616203.

Entry information

Entry nameGALT5_RAT
AccessionPrimary (citable) accession number: O88422
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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