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Q8C102

- GALT5_MOUSE

UniProt

Q8C102 - GALT5_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene
Galnt5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

Catalytic activityi

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

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

ReactomeiREACT_198517. 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: Chromosome 2

Organism-specific databases

MGIiMGI:2179403. Galnt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini36 – 930895Lumenal Reviewed predictionAdd
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...) Reviewed prediction
Glycosylationi213 – 2131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi283 – 2831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi287 – 2871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi309 – 3091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi355 – 3551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi387 – 3871N-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

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.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028171.

Structurei

3D structure databases

ProteinModelPortaliQ8C102.
SMRiQ8C102. Positions 429-925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini794 – 925132Ricin B-type lectinAdd
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307550.
GeneTreeiENSGT00740000115054.
HOGENOMiHOG000231869.
HOVERGENiHBG051698.
InParanoidiA2AS75.
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

MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII    50
RREHTGFRVE PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN 100
MDQVQRKGKM QNLLGRRKAV PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS 150
SQYMMSKWMT VLESEKTPFT ASRGVPLTKI AGRTETFDKK QEAPQNYNVS 200
SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP PILKSEEVTV 250
IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA 300
KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK 350
QIPRNQSKTS SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS 400
HANIPENPGM HHVFRIDVTL SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK 450
EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS 500
ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY MSQFPKVRIL 550
RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 600
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK 650
ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG 700
GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDDYRELF 750
YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLDNVF PDLKAPVVRA 800
SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR LIKHGEWCVA 850
PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME 900
GNFSQKTLKL AACNPMELQQ KWKFEKYYEV 930
Length:930
Mass (Da):105,780
Last modified:July 27, 2011 - v2
Checksum:iC5851F6E13CDF5D7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti705 – 7051I → L in BAC26396. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006498048.1.
XP_006498112.1. XM_006498049.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS38125.1.
RefSeqi NP_766443.2. NM_172855.3.
XP_006498111.1. XM_006498048.1.
XP_006498112.1. XM_006498049.1.
UniGenei Mm.484118.

3D structure databases

ProteinModelPortali Q8C102.
SMRi Q8C102. Positions 429-925.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000028171.

Protein family/group databases

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

PTM databases

PhosphoSitei Q8C102.

Proteomic databases

MaxQBi Q8C102.
PRIDEi Q8C102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112616 ; ENSMUSP00000108235 ; ENSMUSG00000026828 .
ENSMUST00000166729 ; ENSMUSP00000131362 ; ENSMUSG00000026828 .
GeneIDi 241391.
KEGGi mmu:241391.
UCSCi uc012bvo.1. mouse.

Organism-specific databases

CTDi 11227.
MGIi MGI:2179403. Galnt5.

Phylogenomic databases

eggNOGi NOG307550.
GeneTreei ENSGT00740000115054.
HOGENOMi HOG000231869.
HOVERGENi HBG051698.
InParanoidi A2AS75.
KOi K00710.
OMAi SHVVIIT.
OrthoDBi EOG7J9VP2.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 384997.
PROi Q8C102.
SOURCEi Search...

Gene expression databases

Bgeei Q8C102.
Genevestigatori Q8C102.

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

« 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: September 3, 2014
This is version 100 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

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