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O08832

- GALT4_MOUSE

UniProt

O08832 - GALT4_MOUSE

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Protein
Polypeptide N-acetylgalactosaminyltransferase 4
Gene
Galnt4
Organism
Mus musculus (Mouse)
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 a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b.

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 sitei175 – 1751Substrate By similarity
Binding sitei204 – 2041Substrate By similarity
Metal bindingi227 – 2271Manganese By similarity
Metal bindingi229 – 2291Manganese By similarity
Binding sitei334 – 3341Substrate By similarity
Metal bindingi362 – 3621Manganese By similarity
Binding sitei370 – 3701Substrate 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 4 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 4
Short name:
GalNAc-T4
Short name:
pp-GaNTase 4
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Gene namesi
Name:Galnt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:894692. Galnt4.

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 – 578543Lumenal 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 – 578578Polypeptide N-acetylgalactosaminyltransferase 4
PRO_0000059109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi124 ↔ 357 By similarity
Disulfide bondi348 ↔ 421 By similarity
Disulfide bondi457 ↔ 477 By similarity
Glycosylationi471 – 4711N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi503 ↔ 518 By similarity
Disulfide bondi547 ↔ 565 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO08832.
PRIDEiO08832.

PTM databases

PhosphoSiteiO08832.

Expressioni

Tissue specificityi

Highly expressed in sublingual gland, stomach, colon, small intestine and cervix. Expressed at intermediate levels in kidney, ovary, lung and uterus. Weakly expressed in spleen, liver, heart and brain. Not expressed in submandibular and parotid glands, skeletal muscle and testis.1 Publication

Gene expression databases

BgeeiO08832.
GenevestigatoriO08832.

Structurei

3D structure databases

ProteinModelPortaliO08832.
SMRiO08832. Positions 75-577.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 577134Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 243110Catalytic subdomain A
Add
BLAST
Regioni303 – 36563Catalytic 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 directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates By similarity.

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00750000117451.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
KOiK00710.
OMAiNTFEFYM.
OrthoDBiEOG7J9VP2.
PhylomeDBiO08832.
TreeFamiTF352660.

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.

O08832-1 [UniParc]FASTAAdd to Basket

« Hide

MAVRWTWAGK SCLLLALLTL AYILVEFSVS TLYASPGAGG ARELGPRRLP    50
DLDTREEDLS QPLYIKPPAD SHALGEWGRA SKLQLNEGEL KQQEELIERY 100
AINIYLSDRI SLHRHIEDKR MYECKAKKFH YRSLPTTSVI IAFYNEAWST 150
LLRTIHSVLE TSPAVLLKEI ILVDDLSDRI YLKAQLETYI SNLERVRLIR 200
TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNTGWLEPL LERISRDETA 250
IVCPVIDTID WNTFEFYMQT GEPMIGGFDW RLTFQWHSVP KHERDRRTSR 300
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG 350
KLEIHPCSHV GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP 400
ARKEAYGDLS ERKLLRERLK CKSFDWYLKN VFSNLHVPED RPGWHGAIRS 450
MGISSECLDY NAPDNNPTGA NLSLFGCHGQ GGNQFFEYTS NKEIRFNSVT 500
ELCAEVPQQK DYVGMQNCPK DGLPVPVNII WHFKEDGTIF HPHTRLCLSA 550
YRTAEGRPSV HMKTCDALDK NQLWRFEK 578
Length:578
Mass (Da):66,555
Last modified:July 1, 1997 - v1
Checksum:i10ADC0D8B8B30835
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73819 mRNA. Translation: AAB58301.1.
AK033494 mRNA. Translation: BAC28317.1.
AK148036 mRNA. Translation: BAE28303.1.
AK153253 mRNA. Translation: BAE31844.1.
BC057882 mRNA. Translation: AAH57882.1.
CCDSiCCDS48679.1.
RefSeqiNP_056552.1. NM_015737.4.
UniGeneiMm.314.

Genome annotation databases

EnsembliENSMUST00000161240; ENSMUSP00000125315; ENSMUSG00000090035.
GeneIDi14426.
KEGGimmu:14426.
UCSCiuc007gxj.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 4

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73819 mRNA. Translation: AAB58301.1 .
AK033494 mRNA. Translation: BAC28317.1 .
AK148036 mRNA. Translation: BAE28303.1 .
AK153253 mRNA. Translation: BAE31844.1 .
BC057882 mRNA. Translation: AAH57882.1 .
CCDSi CCDS48679.1.
RefSeqi NP_056552.1. NM_015737.4.
UniGenei Mm.314.

3D structure databases

ProteinModelPortali O08832.
SMRi O08832. Positions 75-577.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

PTM databases

PhosphoSitei O08832.

Proteomic databases

MaxQBi O08832.
PRIDEi O08832.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000161240 ; ENSMUSP00000125315 ; ENSMUSG00000090035 .
GeneIDi 14426.
KEGGi mmu:14426.
UCSCi uc007gxj.2. mouse.

Organism-specific databases

CTDi 8693.
MGIi MGI:894692. Galnt4.

Phylogenomic databases

GeneTreei ENSGT00750000117451.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
KOi K00710.
OMAi NTFEFYM.
OrthoDBi EOG7J9VP2.
PhylomeDBi O08832.
TreeFami TF352660.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 286029.
PROi O08832.
SOURCEi Search...

Gene expression databases

Bgeei O08832.
Genevestigatori O08832.

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. "cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
    Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A.
    J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Spleen.
  2. "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: Bone marrow and Colon.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiGALT4_MOUSE
AccessioniPrimary (citable) accession number: O08832
Secondary accession number(s): Q3U681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 106 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. 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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