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Q9JJ61 (GLT16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 16

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 16
Short name=GalNAc-T16
Polypeptide GalNAc transferase-like protein 1
Short name=GalNAc-T-like protein 1
Short name=pp-GaNTase-like protein 1
Polypeptide N-acetylgalactosaminyltransferase-like protein 1
Protein-UDP acetylgalactosaminyltransferase-like protein 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1
Gene names
Name:Galnt16
Synonyms:Galntl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

In the CNS, it is predominantly expressed in several distinct hypothalamic, thalamic and amygdaloid nuclei. The most abundant level of expression is in the paraventricular, ventromedial and arcuate nuclei of the hypothalamus, the anterodorsal and parafascicular nuclei of the thalamus and the central, basomedial and medial nuclei of the amygdala. Also expressed in cerebral cortex, lateral septum, habenula and hippocampus. Ref.5

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Caution

Was originally termed Galnt10/pp-GaNTase 10 (Ref.5).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 558558Polypeptide N-acetylgalactosaminyltransferase 16
PRO_0000059136

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2620Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 558532Lumenal Potential
Domain428 – 555128Ricin B-type lectin
Region122 – 227106Catalytic subdomain A
Region286 – 34863Catalytic subdomain B

Sites

Metal binding2111Manganese By similarity
Metal binding2131Manganese By similarity
Metal binding3451Manganese By similarity
Binding site1631Substrate By similarity
Binding site1881Substrate By similarity
Binding site2121Substrate By similarity
Binding site3171Substrate By similarity
Binding site3481Substrate By similarity
Binding site3511Substrate By similarity
Binding site3531Substrate By similarity

Amino acid modifications

Disulfide bond113 ↔ 340 By similarity
Disulfide bond331 ↔ 409 By similarity
Disulfide bond441 ↔ 460 By similarity
Disulfide bond486 ↔ 506 By similarity
Disulfide bond530 ↔ 543 By similarity

Experimental info

Sequence conflict711K → E in BAA97985. Ref.1
Sequence conflict1981G → R in BAA97985. Ref.1
Sequence conflict2831P → L in BAA97985. Ref.1
Sequence conflict5181K → R in BAA97985. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JJ61 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1B59DBE8EDDD5C63

FASTA55862,875
        10         20         30         40         50         60 
MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSSGRGA QRAGGRPEQL REDRTIPLIV 

        70         80         90        100        110        120 
TGTPSKGFDE KAYLSAKQLK PGEDPYRQHA FNQLESDKLS SDRPIRDTRH YSCPSLSYSS 

       130        140        150        160        170        180 
DLPATSVIIT FHNEARSTLL RTVKSVLNRT PASLIQEIIL VDDFSSDPED CLLLTRIPKV 

       190        200        210        220        230        240 
KCLRNDKREG LIRSRVRGAD VAGATVLTFL DSHCEVNVEW LQPMLQRVME DHTRVVSPII 

       250        260        270        280        290        300 
DVISLDNFAY LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTKPIRTP VIAGGIFVID 

       310        320        330        340        350        360 
KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR HPYNFPEGNA 

       370        380        390        400        410        420 
LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR IEQRKKMDCK SFRWYLENVY 

       430        440        450        460        470        480 
PELTVPVKEV LPGVIKQGVN CLESQGQNTA GDLLLGMGIC RGSAKSPPPA QAWLFSDHLI 

       490        500        510        520        530        540 
QQQGKCLAAT STLMSSPGSP VILQTCNPKE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT 

       550 
SKCQTDAQAQ QWQLLPHT 

« Hide

References

« Hide 'large scale' references
[1]Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, mpp-GalNAc-T16."
Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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: Thymus.
[4]"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].
[5]"A new UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase mRNA exhibits predominant expression in the hypothalamus, thalamus and amygdala of mouse forebrain."
Nelson P.A., Sutcliffe J.G., Thomas E.A.
Gene Expr. Patterns 1:95-99(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB045325 mRNA. Translation: BAA97985.1.
AB175683 mRNA. Translation: BAD52071.1.
AK138883 mRNA. Translation: BAE23810.1.
BC110634 mRNA. Translation: AAI10635.1.
BC125015 mRNA. Translation: AAI25016.1.
RefSeqNP_001074890.1. NM_001081421.1.
UniGeneMm.308296.

3D structure databases

ProteinModelPortalQ9JJ61.
SMRQ9JJ61. Positions 64-556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000021558.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ9JJ61.

Proteomic databases

PaxDbQ9JJ61.
PRIDEQ9JJ61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021558; ENSMUSP00000021558; ENSMUSG00000021130.
GeneID108760.
KEGGmmu:108760.
UCSCuc007oaw.1. mouse.

Organism-specific databases

CTD57452.
MGIMGI:1917754. Galnt16.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00730000110798.
HOVERGENHBG051699.
InParanoidQ60GT0.
KOK00710.
OMAPEDCQLL.
OrthoDBEOG7J9VP2.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9JJ61.
BgeeQ9JJ61.
GenevestigatorQ9JJ61.

Family and domain databases

InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio361295.
PROQ9JJ61.
SOURCESearch...

Entry information

Entry nameGLT16_MOUSE
AccessionPrimary (citable) accession number: Q9JJ61
Secondary accession number(s): Q60GT0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot