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Q6P9S7

- GLT10_MOUSE

UniProt

Q6P9S7 - GLT10_MOUSE

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Protein
Polypeptide N-acetylgalactosaminyltransferase 10
Gene
Galnt10
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 Muc5Ac and EA2 peptide 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 sitei185 – 1851Substrate By similarity
Binding sitei214 – 2141Substrate By similarity
Metal bindingi237 – 2371Manganese By similarity
Binding sitei238 – 2381Substrate By similarity
Metal bindingi239 – 2391Manganese By similarity
Binding sitei342 – 3421Substrate By similarity
Metal bindingi370 – 3701Manganese By similarity
Binding sitei373 – 3731Substrate By similarity
Binding sitei378 – 3781Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: MGI

GO - Biological processi

  1. protein O-linked glycosylation Source: MGI
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 10 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name:
GalNAc-T10
Short name:
pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:Galnt10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1890480. Galnt10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini32 – 603572Lumenal 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 – 603603Polypeptide N-acetylgalactosaminyltransferase 10
PRO_0000059123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi135 ↔ 365 By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi356 ↔ 432 By similarity
Disulfide bondi471 ↔ 488 By similarity
Disulfide bondi523 ↔ 538 By similarity
Disulfide bondi563 ↔ 578 By similarity
Glycosylationi593 – 5931N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ6P9S7.

PTM databases

PhosphoSiteiQ6P9S7.

Expressioni

Tissue specificityi

Expressed at higher level than GALNT9. In the developing hindbrain region of E14.5 embryos it accumulates in the rapidly dividing, undifferentiated ventricular zone adjacent to the pons. It also accumulates in the regions immediately rostral and caudal to the dorsal rhombic lips differentiating into the cerebellum. Not expressed in the developing choroid plexus.1 Publication

Gene expression databases

ArrayExpressiQ6P9S7.
BgeeiQ6P9S7.
GenevestigatoriQ6P9S7.

Structurei

3D structure databases

ProteinModelPortaliQ6P9S7.
SMRiQ6P9S7. Positions 69-603.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 590133Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 253110Catalytic subdomain A
Add
BLAST
Regioni311 – 37363Catalytic subdomain B
Add
BLAST
Regioni373 – 38412Flexible loop By similarity
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 binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00740000115054.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ6P9S7.
KOiK00710.
OMAiHSRQKKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6P9S7.
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.

Q6P9S7-1 [UniParc]FASTAAdd to Basket

« Hide

MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGLGAAVAPA    50
AVQELHSRQK KTFFLGAEQR LKDWHNKEAI RRDAQRVGYG EQGKPYPMTD 100
AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKLY LETLPNTSII 150
IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM 200
ALFPSVRILR TKKREGLIRT RMLGASAATG DVVTFLDSHC EANVNWLPPL 250
LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP 300
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS 350
FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE 400
YAEYIYQRRP EYRHLSAGDV VAQKKLRVSL NCKSFKWFMT KIAWDLPKFY 450
PPVEPPAAAW GEIRNVGTGL CTDTKLGTLG SPLRLETCIR GRGEAAWNSM 500
QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS MKGNQLWKYR 550
KDKTLYHPVS GSCMDCSESD HRVFMNTCNP SSLTQQWLFE HTNSTVLENF 600
NKN 603
Length:603
Mass (Da):69,116
Last modified:July 5, 2004 - v1
Checksum:iFF55FBA7E1DD7544
GO

Sequence cautioni

The sequence AAH16585.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAD21405.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331V → I in BAD21405. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK131155 mRNA. Translation: BAD21405.1. Different initiation.
BC016585 mRNA. Translation: AAH16585.1. Different initiation.
BC060617 mRNA. Translation: AAH60617.1.
AK033515 mRNA. Translation: BAC28334.1.
CCDSiCCDS24719.1.
RefSeqiNP_598950.2. NM_134189.2.
UniGeneiMm.271670.

Genome annotation databases

EnsembliENSMUST00000066987; ENSMUSP00000065096; ENSMUSG00000020520.
GeneIDi171212.
KEGGimmu:171212.
UCSCiuc007jab.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 10

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK131155 mRNA. Translation: BAD21405.1 . Different initiation.
BC016585 mRNA. Translation: AAH16585.1 . Different initiation.
BC060617 mRNA. Translation: AAH60617.1 .
AK033515 mRNA. Translation: BAC28334.1 .
CCDSi CCDS24719.1.
RefSeqi NP_598950.2. NM_134189.2.
UniGenei Mm.271670.

3D structure databases

ProteinModelPortali Q6P9S7.
SMRi Q6P9S7. Positions 69-603.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

PTM databases

PhosphoSitei Q6P9S7.

Proteomic databases

PRIDEi Q6P9S7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000066987 ; ENSMUSP00000065096 ; ENSMUSG00000020520 .
GeneIDi 171212.
KEGGi mmu:171212.
UCSCi uc007jab.1. mouse.

Organism-specific databases

CTDi 55568.
MGIi MGI:1890480. Galnt10.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00740000115054.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q6P9S7.
KOi K00710.
OMAi HSRQKKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6P9S7.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi GALNT10. mouse.
NextBioi 370706.
PROi Q6P9S7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q6P9S7.
Bgeei Q6P9S7.
Genevestigatori Q6P9S7.

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. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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: C57BL/6 and FVB/N.
    Tissue: Brain and Mammary tumor.
  3. "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] OF 76-603.
    Strain: C57BL/6J.
    Tissue: Colon.
  4. "Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9."
    Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K., Balys M.M., Beres T.M., Degand P., Tabak L.A.
    J. Biol. Chem. 276:17395-17404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiGLT10_MOUSE
AccessioniPrimary (citable) accession number: Q6P9S7
Secondary accession number(s): Q6KAQ2, Q8BZU8, Q91YJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.

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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