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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

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Metal bindingi227 – 2271ManganeseBy similarity
Metal bindingi229 – 2291ManganeseBy similarity
Binding sitei334 – 3341SubstrateBy similarity
Metal bindingi362 – 3621ManganeseBy similarity
Binding sitei370 – 3701SubstrateBy 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

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 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 578543LumenalSequence AnalysisAdd
BLAST

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 – 578578Polypeptide N-acetylgalactosaminyltransferase 4PRO_0000059109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi124 ↔ 357PROSITE-ProRule annotation
Disulfide bondi348 ↔ 421PROSITE-ProRule annotation
Disulfide bondi457 ↔ 477PROSITE-ProRule annotation
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi503 ↔ 518PROSITE-ProRule annotation
Disulfide bondi547 ↔ 565PROSITE-ProRule annotation

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 577134Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 243110Catalytic subdomain AAdd
BLAST
Regioni303 – 36563Catalytic 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 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).By similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiO08832.
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

        10         20         30         40         50
MAVRWTWAGK SCLLLALLTL AYILVEFSVS TLYASPGAGG ARELGPRRLP
60 70 80 90 100
DLDTREEDLS QPLYIKPPAD SHALGEWGRA SKLQLNEGEL KQQEELIERY
110 120 130 140 150
AINIYLSDRI SLHRHIEDKR MYECKAKKFH YRSLPTTSVI IAFYNEAWST
160 170 180 190 200
LLRTIHSVLE TSPAVLLKEI ILVDDLSDRI YLKAQLETYI SNLERVRLIR
210 220 230 240 250
TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNTGWLEPL LERISRDETA
260 270 280 290 300
IVCPVIDTID WNTFEFYMQT GEPMIGGFDW RLTFQWHSVP KHERDRRTSR
310 320 330 340 350
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG
360 370 380 390 400
KLEIHPCSHV GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP
410 420 430 440 450
ARKEAYGDLS ERKLLRERLK CKSFDWYLKN VFSNLHVPED RPGWHGAIRS
460 470 480 490 500
MGISSECLDY NAPDNNPTGA NLSLFGCHGQ GGNQFFEYTS NKEIRFNSVT
510 520 530 540 550
ELCAEVPQQK DYVGMQNCPK DGLPVPVNII WHFKEDGTIF HPHTRLCLSA
560 570
YRTAEGRPSV HMKTCDALDK NQLWRFEK
Length:578
Mass (Da):66,555
Last modified:July 1, 1997 - v1
Checksum:i10ADC0D8B8B30835
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi O08832.
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: November 26, 2014
This is version 109 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