Q8BVG5 (GLT14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Galnt14

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	550 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 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.
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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BVG5-1)

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.

Isoform 2 (identifier: Q8BVG5-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 550	550	Polypeptide N-acetylgalactosaminyltransferase 14		PRO_0000059134
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 26	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 550	524	Lumenal Potential
	Domain	415 – 548	134	Ricin B-type lectin
	Region	110 – 215	106	Catalytic subdomain A
	Region	274 – 336	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	430 ↔ 447		By similarity
	Disulfide bond	474 ↔ 491		By similarity
	Disulfide bond	515 ↔ 536		By similarity
Natural variations
	Alternative sequence	385 – 429	45	IENRL…RQRQK → SHVTQCCRRRILIRGTSFRG VVPPTNLPVESPTDPSSPYY LSSSS in isoform 2.		VSP_011225
	Alternative sequence	430 – 550	121	Missing in isoform 2.		VSP_011226
Experimental info
	Sequence conflict	112	1	P → H in BAC37208. Ref.2
	Sequence conflict	173	1	N → H in BAD52069. Ref.1
	Sequence conflict	260	1	L → I in BAB22325. Ref.2
	Sequence conflict	381	1	P → H in BAC37208. Ref.2
	Sequence conflict	403	1	N → Y in BAD52069. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: D67054CFE6F332E1	FASTA	550	63,989
	10 20 30 40 50 60 MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD DLWEQFDERR 70 80 90 100 110 120 YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR CSLLVYCTDL PPTSIIITFH 130 140 150 160 170 180 NEARSTLLRT IRSVLNRTPM HLIQEIILVD DFSNDPEDCK QLIKLPKVKC LRNNERQGLV 190 200 210 220 230 240 RSRMRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE 250 260 270 280 290 300 SASELRGGFD WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV 310 320 330 340 350 360 DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE 370 380 390 400 410 420 VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF KWNLENVYPE LRVPPDSSIQ 430 440 450 460 470 480 KGNIRQRQKC LESQKQKKQE ILRLSPCAKV KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL 490 500 510 520 530 540 FPGAPVVLAL CKNGDERQLW TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL 550 MSQHWDIVSS
	Isoform 2 [UniParc]. Checksum: B14F4BE219C5B7B0	FASTA	429	50,057
	10 20 30 40 50 60 MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD DLWEQFDERR 70 80 90 100 110 120 YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR CSLLVYCTDL PPTSIIITFH 130 140 150 160 170 180 NEARSTLLRT IRSVLNRTPM HLIQEIILVD DFSNDPEDCK QLIKLPKVKC LRNNERQGLV 190 200 210 220 230 240 RSRMRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE 250 260 270 280 290 300 SASELRGGFD WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV 310 320 330 340 350 360 DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE 370 380 390 400 410 420 VWMDEYKQYY YAARPFALER PFGNSHVTQC CRRRILIRGT SFRGVVPPTN LPVESPTDPS SPYYLSSSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 14

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB175681 mRNA. Translation: BAD52069.1. AK002747 mRNA. Translation: BAB22325.1. AK078292 mRNA. Translation: BAC37208.1.
IPI	IPI00225862. IPI00459092.
RefSeq	NP_082140.2. NM_027864.2.
UniGene	Mm.271953.
3D structure databases
ProteinModelPortal	Q8BVG5.
SMR	Q8BVG5. Positions 78-545.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q8BVG5.
Proteomic databases
PRIDE	Q8BVG5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064.
GeneID	71685.
KEGG	mmu:71685.
Organism-specific databases
CTD	79623.
MGI	MGI:1918935. Galnt14.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104275.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q8BVG5.
KO	K00710.
OrthoDB	EOG483D4C.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8BVG5.
Bgee	Q8BVG5.
Genevestigator	Q8BVG5.
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	334229.
SOURCE	Search...

Entry information

Entry name

GLT14_MOUSE

Accession

Primary (citable) accession number: Q8BVG5
Secondary accession number(s): Q60GT2, Q8BTI6, Q9DCJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	June 13, 2006
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program