Q9JJ61 (GLT16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 16
EC=2.4.1.41

Alternative name(s):
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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May catalyze 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. Calcium 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 (Ref.5) termed Galnt10/pp-GaNTase 10.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Polypeptide N-acetylgalactosaminyltransferase 16		PRO_0000059136
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 26	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 558	532	Lumenal Potential
	Domain	428 – 555	128	Ricin B-type lectin
	Region	122 – 227	106	Catalytic subdomain A
	Region	286 – 348	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	441 ↔ 460		By similarity
	Disulfide bond	486 ↔ 506		By similarity
	Disulfide bond	530 ↔ 543		By similarity
Experimental info
	Sequence conflict	71	1	K → E in BAA97985. Ref.1
	Sequence conflict	198	1	G → R in BAA97985. Ref.1
	Sequence conflict	283	1	P → L in BAA97985. Ref.1
	Sequence conflict	518	1	K → R in BAA97985. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JJ61 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 1B59DBE8EDDD5C63	FASTA	558	62,875
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00464268.
RefSeq	NP_001074890.1. NM_001081421.1.
UniGene	Mm.308296.
3D structure databases
ProteinModelPortal	Q9JJ61.
SMR	Q9JJ61. Positions 90-554.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000021558.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q9JJ61.
Proteomic databases
PaxDb	Q9JJ61.
PRIDE	Q9JJ61.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021558; ENSMUSP00000021558; ENSMUSG00000021130.
GeneID	108760.
KEGG	mmu:108760.
Organism-specific databases
CTD	57452.
MGI	MGI:1917754. Galnt16.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104275.
HOVERGEN	HBG051699.
InParanoid	Q60GT0.
KO	K00710.
OMA	PEDCQLL.
OrthoDB	EOG4DZ1V4.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9JJ61.
Bgee	Q9JJ61.
Genevestigator	Q9JJ61.
GermOnline	ENSMUSG00000021130. Mus musculus.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2_met. IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF02709. Glyco_transf_7C. 1 hit. PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	361295.
SOURCE	Search...

Entry information

Entry name

GLT16_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program