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Q8BVG5

- GLT14_MOUSE

UniProt

Q8BVG5 - GLT14_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 14

Gene
Galnt14
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. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney 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 sitei151 – 1511Substrate By similarity
Binding sitei176 – 1761Substrate By similarity
Metal bindingi199 – 1991Manganese By similarity
Binding sitei200 – 2001Substrate By similarity
Metal bindingi201 – 2011Manganese By similarity
Binding sitei305 – 3051Substrate By similarity
Metal bindingi333 – 3331Manganese By similarity
Binding sitei336 – 3361Substrate By similarity
Binding sitei339 – 3391Substrate By similarity
Binding sitei341 – 3411Substrate 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 14 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 14
Short name:
GalNAc-T14
Short name:
pp-GaNTase 14
Protein-UDP acetylgalactosaminyltransferase 14
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
Gene namesi
Name:Galnt14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1918935. Galnt14.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2620Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini27 – 550524Lumenal 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 – 550550Polypeptide N-acetylgalactosaminyltransferase 14PRO_0000059134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi101 ↔ 328 By similarity
Disulfide bondi319 ↔ 397 By similarity
Disulfide bondi430 ↔ 447 By similarity
Disulfide bondi474 ↔ 491 By similarity
Disulfide bondi515 ↔ 536 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8BVG5.

PTM databases

PhosphoSiteiQ8BVG5.

Expressioni

Gene expression databases

BgeeiQ8BVG5.
GenevestigatoriQ8BVG5.

Structurei

3D structure databases

ProteinModelPortaliQ8BVG5.
SMRiQ8BVG5. Positions 78-545.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 548134Ricin B-type lectinAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 215106Catalytic subdomain AAdd
BLAST
Regioni274 – 33663Catalytic 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

eggNOGiNOG239675.
GeneTreeiENSGT00750000117385.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BVG5.
KOiK00710.
PhylomeDBiQ8BVG5.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BVG5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD    50
DLWEQFDERR YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR 100
CSLLVYCTDL PPTSIIITFH NEARSTLLRT IRSVLNRTPM HLIQEIILVD 150
DFSNDPEDCK QLIKLPKVKC LRNNERQGLV RSRMRGADIA QGTTLTFLDS 200
HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE SASELRGGFD 250
WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV 300
DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT 350
YIKNTKRTAE VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF 400
KWNLENVYPE LRVPPDSSIQ KGNIRQRQKC LESQKQKKQE ILRLSPCAKV 450
KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL FPGAPVVLAL CKNGDERQLW 500
TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL MSQHWDIVSS 550
Length:550
Mass (Da):63,989
Last modified:June 13, 2006 - v2
Checksum:iD67054CFE6F332E1
GO
Isoform 2 (identifier: Q8BVG5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     385-429: IENRLNLRKN...QKGNIRQRQK → SHVTQCCRRR...SSPYYLSSSS
     430-550: Missing.

Note: No experimental confirmation available.

Show »
Length:429
Mass (Da):50,057
Checksum:iB14F4BE219C5B7B0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei385 – 42945IENRL…RQRQK → SHVTQCCRRRILIRGTSFRG VVPPTNLPVESPTDPSSPYY LSSSS in isoform 2. VSP_011225Add
BLAST
Alternative sequencei430 – 550121Missing in isoform 2. VSP_011226Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121P → H in BAC37208. 1 Publication
Sequence conflicti173 – 1731N → H in BAD52069. 1 Publication
Sequence conflicti260 – 2601L → I in BAB22325. 1 Publication
Sequence conflicti381 – 3811P → H in BAC37208. 1 Publication
Sequence conflicti403 – 4031N → Y in BAD52069. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB175681 mRNA. Translation: BAD52069.1.
AK002747 mRNA. Translation: BAB22325.1.
AK078292 mRNA. Translation: BAC37208.1.
CCDSiCCDS28965.1. [Q8BVG5-1]
RefSeqiNP_082140.2. NM_027864.2.
XP_006525002.1. XM_006524939.1. [Q8BVG5-2]
UniGeneiMm.271953.
Mm.450771.

Genome annotation databases

EnsembliENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
GeneIDi71685.
KEGGimmu:71685.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 14

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB175681 mRNA. Translation: BAD52069.1 .
AK002747 mRNA. Translation: BAB22325.1 .
AK078292 mRNA. Translation: BAC37208.1 .
CCDSi CCDS28965.1. [Q8BVG5-1 ]
RefSeqi NP_082140.2. NM_027864.2.
XP_006525002.1. XM_006524939.1. [Q8BVG5-2 ]
UniGenei Mm.271953.
Mm.450771.

3D structure databases

ProteinModelPortali Q8BVG5.
SMRi Q8BVG5. Positions 78-545.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

PTM databases

PhosphoSitei Q8BVG5.

Proteomic databases

PRIDEi Q8BVG5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112591 ; ENSMUSP00000108210 ; ENSMUSG00000024064 . [Q8BVG5-2 ]
GeneIDi 71685.
KEGGi mmu:71685.

Organism-specific databases

CTDi 79623.
MGIi MGI:1918935. Galnt14.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00750000117385.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8BVG5.
KOi K00710.
PhylomeDBi Q8BVG5.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 334229.
PROi Q8BVG5.
SOURCEi Search...

Gene expression databases

Bgeei Q8BVG5.
Genevestigatori Q8BVG5.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
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. "Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, mpp-GalNAc-T14."
    Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Olfactory bulb.

Entry informationi

Entry nameiGLT14_MOUSE
AccessioniPrimary (citable) accession number: Q8BVG5
Secondary accession number(s): Q60GT2, Q8BTI6, Q9DCJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 13, 2006
Last modified: September 3, 2014
This is version 97 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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