Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

Galnt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 or Muc1b substrates (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+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: MGI

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

ReactomeiREACT_278772. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2179403. Galnt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 930895LumenalSequence AnalysisAdd
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 5PRO_0000059111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi387 – 3871N-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

MaxQBiQ8C102.
PRIDEiQ8C102.

PTM databases

PhosphoSiteiQ8C102.

Expressioni

Tissue specificityi

Expressed at low level. Not expressed before E7.5 during embryogenesis. Expressed in dental mesenchyme and tongue. Accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 maxilla and mandible underlying the dental lamina.1 Publication

Gene expression databases

BgeeiQ8C102.
GenevestigatoriQ8C102.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028171.

Structurei

3D structure databases

ProteinModelPortaliQ8C102.
SMRiQ8C102. Positions 429-925.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ8C102.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG7J9VP2.
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.

Q8C102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII
60 70 80 90 100
RREHTGFRVE PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN
110 120 130 140 150
MDQVQRKGKM QNLLGRRKAV PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS
160 170 180 190 200
SQYMMSKWMT VLESEKTPFT ASRGVPLTKI AGRTETFDKK QEAPQNYNVS
210 220 230 240 250
SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP PILKSEEVTV
260 270 280 290 300
IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA
310 320 330 340 350
KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK
360 370 380 390 400
QIPRNQSKTS SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS
410 420 430 440 450
HANIPENPGM HHVFRIDVTL SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK
460 470 480 490 500
EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS
510 520 530 540 550
ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY MSQFPKVRIL
560 570 580 590 600
RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK
610 620 630 640 650
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK
660 670 680 690 700
ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG
710 720 730 740 750
GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDDYRELF
760 770 780 790 800
YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLDNVF PDLKAPVVRA
810 820 830 840 850
SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR LIKHGEWCVA
860 870 880 890 900
PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME
910 920 930
GNFSQKTLKL AACNPMELQQ KWKFEKYYEV
Length:930
Mass (Da):105,780
Last modified:July 27, 2011 - v2
Checksum:iC5851F6E13CDF5D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti705 – 7051I → L in BAC26396 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029323 mRNA. Translation: BAC26396.1.
AL928564, AL929144 Genomic DNA. Translation: CAM18783.1.
AL929144, AL928564 Genomic DNA. Translation: CAM24473.1.
CH466519 Genomic DNA. Translation: EDL26932.1.
CCDSiCCDS38125.1.
RefSeqiNP_766443.2. NM_172855.3.
XP_006498111.1. XM_006498048.2.
XP_006498112.1. XM_006498049.2.
UniGeneiMm.484118.

Genome annotation databases

EnsembliENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828.
ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
GeneIDi241391.
KEGGimmu:241391.
UCSCiuc012bvo.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029323 mRNA. Translation: BAC26396.1.
AL928564, AL929144 Genomic DNA. Translation: CAM18783.1.
AL929144, AL928564 Genomic DNA. Translation: CAM24473.1.
CH466519 Genomic DNA. Translation: EDL26932.1.
CCDSiCCDS38125.1.
RefSeqiNP_766443.2. NM_172855.3.
XP_006498111.1. XM_006498048.2.
XP_006498112.1. XM_006498049.2.
UniGeneiMm.484118.

3D structure databases

ProteinModelPortaliQ8C102.
SMRiQ8C102. Positions 429-925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028171.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ8C102.

Proteomic databases

MaxQBiQ8C102.
PRIDEiQ8C102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828.
ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
GeneIDi241391.
KEGGimmu:241391.
UCSCiuc012bvo.1. mouse.

Organism-specific databases

CTDi11227.
MGIiMGI:2179403. Galnt5.

Phylogenomic databases

eggNOGiNOG307550.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiQ8C102.
KOiK00710.
OMAiSHVVIIT.
OrthoDBiEOG7J9VP2.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_278772. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi384997.
PROiQ8C102.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C102.
GenevestigatoriQ8C102.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development."
    Kingsley P.D., Hagen K.G., Maltby K.M., Zara J., Tabak L.A.
    Glycobiology 10:1317-1323(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiGALT5_MOUSE
AccessioniPrimary (citable) accession number: Q8C102
Secondary accession number(s): A2AS75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 106 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.