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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 – 5261SubstrateBy similarity
Binding sitei555 – 5551SubstrateBy similarity
Metal bindingi578 – 5781ManganeseBy similarity
Binding sitei579 – 5791SubstrateBy similarity
Metal bindingi580 – 5801ManganeseBy similarity
Binding sitei685 – 6851SubstrateBy similarity
Metal bindingi713 – 7131ManganeseBy similarity
Binding sitei716 – 7161SubstrateBy similarity
Binding sitei721 – 7211SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. 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

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  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 5PRO_0000059112Add
BLAST

Amino acid modifications

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

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006319.

Structurei

3D structure databases

ProteinModelPortaliO88422.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini36 – 930895LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini794 – 925132Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni485 – 594110Catalytic subdomain AAdd
BLAST
Regioni654 – 71663Catalytic subdomain BAdd
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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307550.
GeneTreeiENSGT00760000118828.
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

        10         20         30         40         50
MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTGILKEDIM
60 70 80 90 100
RREQTGFRVE ADQMTILSPS SRGMRPPRNG AGGKESFRKA ENRVLKVEEN
110 120 130 140 150
VDQVQRKGKM QFLLGRGKAV SLWHRTHVQT LPVTLPMQKT QGRDSKPEVS
160 170 180 190 200
SLHMMSKQTT VLGSEKDSFT VSRGVPLNKT AEHTETLDKK QEAPENYNLS
210 220 230 240 250
SDTSKQASQR ALNVTISVRT DRSKQQSQTV TKSSIQFASL PILKPEEVTV
260 270 280 290 300
TKKTEAQGKD LKYEAHKARP LLKFTADVGH LKKQSTNETG LGVLPEADGA
310 320 330 340 350
KVAPGKKLNF SESQIVIITK EEGQKTDTKE VPNSKIQTVF PKLLGESQGK
360 370 380 390 400
HIPRSQSQTL SSPLAPKRAV SQSKPTLAEE LHTARSNLTA KATTVGHQQS
410 420 430 440 450
HANISENPGK HHVLRIDVTL SPRDLNAPGQ FGRPVVVPPG KKKEAEQRWK
460 470 480 490 500
EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS
510 520 530 540 550
ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK DYLKANLDKY MSQFPKVRIL
560 570 580 590 600
RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK
610 620 630 640 650
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWRTIP PDVIAKNGIK
660 670 680 690 700
ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG
710 720 730 740 750
GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDEYKELF
760 770 780 790 800
YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCQ SFKWYLDNVF PDLKAPVVRA
810 820 830 840 850
SGVFINLALG KCVSIKNITV VLEDCDGSSE LQQFNYTWVR LIKHGEWCVA
860 870 880 890 900
PIPDKGSLTL YPCDNRNNRL KWLHRSASAF HPELVDHIVF ESYQQLLCME
910 920 930
GNFSQKTLKL AACNPTEPQQ KWKFEKYYDV
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 ENSGT00760000118828.
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: October 29, 2014
This is version 102 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