Q921L8 (GLT11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 11
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 11
Short name=GalNAc-T11
Short name=pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11

Gene names

Name:

Galnt11

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	608 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 the same enzyme activity toward Muc1, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin 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	Mainly expressed in kidney. Weakly expressed in other tissues. Ref.1
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.
Sequence caution	The sequence AAH34184.1 differs from that shown. Reason: Erroneous termination at position 412. Translated as Glu.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
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 – 608	608	Polypeptide N-acetylgalactosaminyltransferase 11		PRO_0000059126
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 608	579	Lumenal Potential
	Domain	476 – 607	132	Ricin B-type lectin
	Region	150 – 261	112	Catalytic subdomain A
	Region	319 – 381	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	423	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Disulfide bond	493 ↔ 512		By similarity
	Disulfide bond	536 ↔ 553		By similarity
	Disulfide bond	578 ↔ 596		By similarity
Experimental info
	Sequence conflict	545	1	S → L in BAC40096. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q921L8 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 0E452FDA1CA5668B	FASTA	608	69,201
	10 20 30 40 50 60 MGSITVRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP FPKKFYPRFT 70 80 90 100 110 120 RGPGRVLDPQ FKANRIDRLM NNHIEDPDKG LSKSSSELGM IFNERDQELR DLGYQKHAFN 130 140 150 160 170 180 MLISNRLGYH RDVPDTRNAE CRRKSYPTDL PTASIVICFY NEAFSALLRT VHSVVDRTPA 190 200 210 220 230 240 HLLHEIILVD DSSDFDDLKG ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV 250 260 270 280 290 300 LVFLDSHCEV NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF 310 320 330 340 350 360 KWDLVPVSEL GGPDGATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW GGENLEISFR 370 380 390 400 410 420 IWMCGGKLFI LPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD 430 440 450 460 470 480 LKNKSFGNIS ERVELRKKLG CQSFKWYLDN IYPEMQIPGP NAKPQQPVLI NRGPKRPRVL 490 500 510 520 530 540 QRGRLYHLQT NKCLVAQGRS SQKGGLVLLK TCDYGDPTQV WIYNEDHELI LNNLLCLDMS 550 560 570 580 590 600 ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VMDLMDQKGY VGMAICDGSS SQQWRLEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila." Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H. J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Characterization of a novel mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase." Shimoji S., Reynolds P.R., Ten Hagen K.G., Tabak L.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[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 and NOD. Tissue: Ovary and 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]. Strain: FVB/N. Tissue: Kidney and Mammary tumor.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 11

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12435 mRNA. Translation: CAC79626.1. AF495528 mRNA. Translation: AAQ06668.1. AK088014 mRNA. Translation: BAC40096.1. AK161524 mRNA. Translation: BAE36442.1. BC011428 mRNA. Translation: AAH11428.1. BC021504 mRNA. Translation: AAH21504.1. BC034184 mRNA. Translation: AAH34184.1. Sequence problems. BC034185 mRNA. Translation: AAH34185.1. BC036143 mRNA. Translation: AAH36143.1. BC036145 mRNA. Translation: AAH36145.1.
IPI	IPI00387280.
RefSeq	NP_659157.1. NM_144908.3.
UniGene	Mm.246718.
3D structure databases
ProteinModelPortal	Q921L8.
SMR	Q921L8. Positions 130-606.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q921L8.
Proteomic databases
PaxDb	Q921L8.
PRIDE	Q921L8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045737; ENSMUSP00000036240; ENSMUSG00000038072. ENSMUST00000114950; ENSMUSP00000110600; ENSMUSG00000038072. ENSMUST00000114952; ENSMUSP00000110602; ENSMUSG00000038072.
GeneID	231050.
KEGG	mmu:231050.
UCSC	uc008wss.1. mouse.
Organism-specific databases
CTD	63917.
MGI	MGI:2444392. Galnt11.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104275.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q921L8.
KO	K00710.
OMA	YFSLRPD.
OrthoDB	EOG4JQ3X7.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q921L8.
Bgee	Q921L8.
Genevestigator	Q921L8.
GermOnline	ENSMUSG00000038072. 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
ChiTaRS	GALNT11. mouse.
NextBio	380378.
SOURCE	Search...

Entry information

Entry name

GLT11_MOUSE

Accession

Primary (citable) accession number: Q921L8
Secondary accession number(s): Q3TT83, Q8BU26, Q8K032

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program