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P70419

- GALT3_MOUSE

UniProt

P70419 - GALT3_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

Galnt3

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 activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Glycosylates FGF23 (By similarity). Probably glycosylates fibronectin in vivo. May be involved in phosphate homeostasis.By similarity

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 sitei225 – 2251SubstrateBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Metal bindingi277 – 2771ManganeseBy similarity
Metal bindingi279 – 2791ManganeseBy similarity
Binding sitei387 – 3871SubstrateBy similarity
Metal bindingi415 – 4151ManganeseBy similarity
Binding sitei418 – 4181SubstrateBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: Ensembl
  2. carbohydrate binding Source: UniProtKB-KW
  3. manganese ion binding Source: Ensembl
  4. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein O-linked glycosylation via serine Source: Ensembl
  2. protein O-linked glycosylation via threonine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 3474.
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 3 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 3
Short name:
GalNAc-T3
Short name:
pp-GaNTase 3
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene namesi
Name:Galnt3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:894695. Galnt3.

Subcellular locationi

Golgi apparatusGolgi stack membrane By similarity; Single-pass type II membrane protein By similarity
Note: Resides preferentially in the trans and medial parts of the Golgi stack.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini38 – 633596LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3PRO_0000059107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi173 ↔ 410PROSITE-ProRule annotation
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi401 ↔ 482PROSITE-ProRule annotation
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi517 ↔ 535PROSITE-ProRule annotation
Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
Disulfide bondi605 ↔ 618PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP70419.
PaxDbiP70419.
PRIDEiP70419.

PTM databases

PhosphoSiteiP70419.

Expressioni

Tissue specificityi

Highly expressed in the reproductive tract, principally in the testis and uterus, and to a lesser degree in the cervix with only trace levels in the ovary. Also expressed at high level in sublingual gland, stomach and colon, with more moderate amounts present in the submandibular and parotid gland as well as the kidney.1 Publication

Gene expression databases

BgeeiP70419.
GenevestigatoriP70419.

Interactioni

Protein-protein interaction databases

IntActiP70419. 1 interaction.
MINTiMINT-4095534.
STRINGi10090.ENSMUSP00000028378.

Structurei

3D structure databases

ProteinModelPortaliP70419.
SMRiP70419. Positions 122-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 630127Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 293110Catalytic subdomain AAdd
BLAST
Regioni356 – 41863Catalytic 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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiP70419.
KOiK00710.
OMAiQYFEYSA.
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.

P70419-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAHLKRLVKL HIKRHYHRKF WKLGAVIFFF LVVLILMQRE VSVQYSKEES
60 70 80 90 100
KMERNLKNKN KMLDFMLEAV NNIKDAMPKM QIGAPIKENI DVRERPCLQG
110 120 130 140 150
YYTAAELKPV FDRPPQDSNA PGASGKPFKI THLSPEEQKE KERGETKHCF
160 170 180 190 200
NAFASDRISL HRDLGPDTRP PECIEQKFKR CPPLPTTSVI IVFHNEAWST
210 220 230 240 250
LLRTVHSVLY SSPAILLKEI ILVDDASVDD YLHEKLEEYI KQFSIVKIVR
260 270 280 290 300
QQERKGLITA RLLGAAVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
310 320 330 340 350
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR
360 370 380 390 400
KDETYPIKTP TFAGGLFSIS KKYFEHIGSY DEEMEIWGGE NIEMSFRVWQ
410 420 430 440 450
CGGQLEIMPC SVVGHVFRSK SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI
460 470 480 490 500
FYRRNTDAAK IVKQKSFGDL SKRFEIKKRL QCKNFTWYLN TIYPEAYVPD
510 520 530 540 550
LNPVISGYIK SVGQPLCLDV GENNQGGKPL ILYTCHGLGG NQYFEYSAQR
560 570 580 590 600
EIRHNIQKEL CLHATQGVVQ LKACVYKGHR TIAPGEQIWE IRKDQLLYNP
610 620 630
LFKMCLSSNG EHPNLVPCDA TDLLQKWIFS QND
Length:633
Mass (Da):72,932
Last modified:July 27, 2011 - v3
Checksum:i8BEE7CDDBCF56428
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti324 – 3241S → N in AAH43331. (PubMed:15489334)Curated
Sequence conflicti633 – 6331D → E in AAB09579. (PubMed:8912633)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70538 mRNA. Translation: AAB09579.1.
AK135489 mRNA. Translation: BAE22551.1.
AL929230, AL928586 Genomic DNA. Translation: CAM20333.1.
AL928586, AL929230 Genomic DNA. Translation: CAM21878.1.
CH466519 Genomic DNA. Translation: EDL27008.1.
BC043331 mRNA. Translation: AAH43331.1.
CCDSiCCDS16075.1.
PIRiJC5247.
RefSeqiNP_056551.2. NM_015736.2.
UniGeneiMm.439760.

Genome annotation databases

EnsembliENSMUST00000028378; ENSMUSP00000028378; ENSMUSG00000026994.
GeneIDi14425.
KEGGimmu:14425.
UCSCiuc008jwu.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70538 mRNA. Translation: AAB09579.1 .
AK135489 mRNA. Translation: BAE22551.1 .
AL929230 , AL928586 Genomic DNA. Translation: CAM20333.1 .
AL928586 , AL929230 Genomic DNA. Translation: CAM21878.1 .
CH466519 Genomic DNA. Translation: EDL27008.1 .
BC043331 mRNA. Translation: AAH43331.1 .
CCDSi CCDS16075.1.
PIRi JC5247.
RefSeqi NP_056551.2. NM_015736.2.
UniGenei Mm.439760.

3D structure databases

ProteinModelPortali P70419.
SMRi P70419. Positions 122-633.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P70419. 1 interaction.
MINTi MINT-4095534.
STRINGi 10090.ENSMUSP00000028378.

Protein family/group databases

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

PTM databases

PhosphoSitei P70419.

Proteomic databases

MaxQBi P70419.
PaxDbi P70419.
PRIDEi P70419.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028378 ; ENSMUSP00000028378 ; ENSMUSG00000026994 .
GeneIDi 14425.
KEGGi mmu:14425.
UCSCi uc008jwu.2. mouse.

Organism-specific databases

CTDi 2591.
MGIi MGI:894695. Galnt3.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi P70419.
KOi K00710.
OMAi QYFEYSA.
OrthoDBi EOG7J9VP2.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.41. 3474.
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi Galnt3. mouse.
NextBioi 286025.
PROi P70419.
SOURCEi Search...

Gene expression databases

Bgeei P70419.
Genevestigatori P70419.

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. "Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3."
    Zara J., Hagen F.K., Ten Hagen K.G., Van Wuyckhuyse B.C., Tabak L.A.
    Biochem. Biophys. Res. Commun. 228:38-44(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
    Strain: CD-1.
    Tissue: Testis.
  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: Muellerian duct.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. 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].
  5. "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: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiGALT3_MOUSE
AccessioniPrimary (citable) accession number: P70419
Secondary accession number(s): Q3UXL2, Q80V55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 120 of the entry and version 3 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