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O88422

- GALT5_RAT

UniProt

O88422 - GALT5_RAT

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Protein
Polypeptide N-acetylgalactosaminyltransferase 5
Gene
Galnt5
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Manganese By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei526 – 5261Substrate By similarity
Binding sitei555 – 5551Substrate By similarity
Metal bindingi578 – 5781Manganese By similarity
Binding sitei579 – 5791Substrate By similarity
Metal bindingi580 – 5801Manganese By similarity
Binding sitei685 – 6851Substrate By similarity
Metal bindingi713 – 7131Manganese By similarity
Binding sitei716 – 7161Substrate By similarity
Binding sitei721 – 7211Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 5301.
ReactomeiREACT_196259. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Galnt5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi620361. Galnt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini36 – 930895Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 930930Polypeptide N-acetylgalactosaminyltransferase 5
PRO_0000059112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi178 – 1781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi198 – 1981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi213 – 2131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi287 – 2871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi309 – 3091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi387 – 3871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi403 – 4031N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi476 ↔ 708 By similarity
Glycosylationi568 – 5681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi699 ↔ 779 By similarity
Glycosylationi766 – 7661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi812 ↔ 825 By similarity
Glycosylationi817 – 8171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi835 – 8351N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi848 ↔ 863 By similarity
Disulfide bondi898 ↔ 913 By similarity
Glycosylationi902 – 9021N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO88422.
PRIDEiO88422.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

GenevestigatoriO88422.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006319.

Structurei

3D structure databases

ProteinModelPortaliO88422.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini794 – 925132Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni485 – 594110Catalytic subdomain A
Add
BLAST
Regioni654 – 71663Catalytic subdomain B
Add
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307550.
GeneTreeiENSGT00740000115054.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiO88422.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG7J9VP2.
PhylomeDBiO88422.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88422-1 [UniParc]FASTAAdd to Basket

« Hide

MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTGILKEDIM    50
RREQTGFRVE ADQMTILSPS SRGMRPPRNG AGGKESFRKA ENRVLKVEEN 100
VDQVQRKGKM QFLLGRGKAV SLWHRTHVQT LPVTLPMQKT QGRDSKPEVS 150
SLHMMSKQTT VLGSEKDSFT VSRGVPLNKT AEHTETLDKK QEAPENYNLS 200
SDTSKQASQR ALNVTISVRT DRSKQQSQTV TKSSIQFASL PILKPEEVTV 250
TKKTEAQGKD LKYEAHKARP LLKFTADVGH LKKQSTNETG LGVLPEADGA 300
KVAPGKKLNF SESQIVIITK EEGQKTDTKE VPNSKIQTVF PKLLGESQGK 350
HIPRSQSQTL SSPLAPKRAV SQSKPTLAEE LHTARSNLTA KATTVGHQQS 400
HANISENPGK HHVLRIDVTL SPRDLNAPGQ FGRPVVVPPG KKKEAEQRWK 450
EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS 500
ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK DYLKANLDKY MSQFPKVRIL 550
RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 600
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWRTIP PDVIAKNGIK 650
ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG 700
GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF 750
YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCQ SFKWYLDNVF PDLKAPVVRA 800
SGVFINLALG KCVSIKNITV VLEDCDGSSE LQQFNYTWVR LIKHGEWCVA 850
PIPDKGSLTL YPCDNRNNRL KWLHRSASAF HPELVDHIVF ESYQQLLCME 900
GNFSQKTLKL AACNPTEPQQ KWKFEKYYDV 930
Length:930
Mass (Da):105,120
Last modified:November 1, 1998 - v1
Checksum:i1C906A76F320A225
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF049344 mRNA. Translation: AAC69708.1.
RefSeqiNP_113984.1. NM_031796.1.
UniGeneiRn.30048.

Genome annotation databases

EnsembliENSRNOT00000006319; ENSRNOP00000006319; ENSRNOG00000004645.
GeneIDi83627.
KEGGirno:83627.
UCSCiRGD:620361. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF049344 mRNA. Translation: AAC69708.1 .
RefSeqi NP_113984.1. NM_031796.1.
UniGenei Rn.30048.

3D structure databases

ProteinModelPortali O88422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000006319.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbi O88422.
PRIDEi O88422.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000006319 ; ENSRNOP00000006319 ; ENSRNOG00000004645 .
GeneIDi 83627.
KEGGi rno:83627.
UCSCi RGD:620361. rat.

Organism-specific databases

CTDi 11227.
RGDi 620361. Galnt5.

Phylogenomic databases

eggNOGi NOG307550.
GeneTreei ENSGT00740000115054.
HOGENOMi HOG000231869.
HOVERGENi HBG051698.
InParanoidi O88422.
KOi K00710.
OMAi SHVVIIT.
OrthoDBi EOG7J9VP2.
PhylomeDBi O88422.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 5301.
Reactomei REACT_196259. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 616203.
PROi O88422.

Gene expression databases

Genevestigatori O88422.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGALT5_RAT
AccessioniPrimary (citable) accession number: O88422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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