Q6P6V1 (GLT11_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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.
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
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 – 608	608	Polypeptide N-acetylgalactosaminyltransferase 11		PRO_0000059127
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
	Disulfide bond	493 ↔ 512		By similarity
	Disulfide bond	536 ↔ 553		By similarity
	Disulfide bond	578 ↔ 596		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6P6V1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: ED1295AC1EB35751	FASTA	608	69,039
	10 20 30 40 50 60 MGSVTIRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP FPKKFYPRFT 70 80 90 100 110 120 RGPGRVLEPQ FKANRMDDLM NNNIEDPDKG LSKSSSELGM IFNERDQELR DLGYQKHAFN 130 140 150 160 170 180 MLISNRLGYH RDVPDTRNAE CRGKSYPTDL PTASVVICFY 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 KWDLVPVSDL GGADSATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW GGENLEISFR 370 380 390 400 410 420 IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL RLAHVWLDEY KEQYFSLRPD 430 440 450 460 470 480 LKTKSFGNIS ERVELRKKLG CQSFKWYLDN VYPEMQVSGP KARLQQPVFI NRGPKRPRVL 490 500 510 520 530 540 LRGRLYHLQT NKCLVAQGRS SQKGGLVLLK ACDYGDPTQV WIYNEEHELI LNNLLCLDMS 550 560 570 580 590 600 ETRSSDPPRL MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VVDQMDQKGY VGMAICDGSS SQQWRLEG

References

[1]	"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]. Tissue: Prostate.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC062004 mRNA. Translation: AAH62004.1.
IPI	IPI00400738.
RefSeq	NP_001258248.1. NM_001271319.1. NP_955425.2. NM_199393.2.
UniGene	Rn.211885.
3D structure databases
ProteinModelPortal	Q6P6V1.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000011815.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q6P6V1.
Proteomic databases
PRIDE	Q6P6V1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000011814; ENSRNOP00000011815; ENSRNOG00000008117.
GeneID	311952.
KEGG	rno:311952.
Organism-specific databases
CTD	63917.
RGD	735097. Galnt11.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104275.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q6P6V1.
KO	K00710.
OMA	YFSLRPD.
OrthoDB	EOG4JQ3X7.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Genevestigator	Q6P6V1.
GermOnline	ENSRNOG00000008117. Rattus norvegicus.
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	664505.

Entry information

Entry name

GLT11_RAT

Accession

Primary (citable) accession number: Q6P6V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program