Q7TT15 (GLTL3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase-like protein 3
Short name=GalNAc-T-like protein 3
Short name=pp-GaNTase-like protein 3
Protein-UDP acetylgalactosaminyltransferase-like protein 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
Williams-Beuren syndrome chromosomal region 17 protein homolog

Gene names

Name:	Wbscr17
Synonyms:	Galntl3

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	598 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
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 Glycoprotein
Technical term	Complete proteome Direct protein sequencing 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: Q7TT15-1)

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: Q7TT15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     194-196: SDE → R

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 598	598	Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3		PRO_0000059140
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	28 – 598	571	Lumenal Potential
	Domain	465 – 594	130	Ricin B-type lectin
	Region	151 – 262	112	Catalytic subdomain A
	Region	319 – 381	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
	Glycosylation	486	1	N-linked (GlcNAc...) Potential
	Disulfide bond	478 ↔ 494		By similarity
	Disulfide bond	526 ↔ 541		By similarity
	Disulfide bond	568 ↔ 586		By similarity
Natural variations
	Alternative sequence	194 – 196	3	SDE → R in isoform 2.		VSP_011232
Experimental info
	Sequence conflict	74	1	V → D in BAC33446. Ref.3
	Sequence conflict	224	1	E → D in BAC33446. Ref.3
	Sequence conflict	264	1	Q → K in BAC33446. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 66F91B355EF571F5	FASTA	598	67,691
	10 20 30 40 50 60 MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ 70 80 90 100 110 120 DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPSEEEK AKGPHEKYGY 130 140 150 160 170 180 NSYLSEKISL DRSIPDYRPT KCKELKYSKE LPQISIIFIF VNEALSVILR SVHSAVNHTP 190 200 210 220 230 240 THLLKEIILV DDNSDEEELK APLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKAATGQ 250 260 270 280 290 300 VTGFFDAHVE FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW 310 320 330 340 350 360 CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY GGENIELGIK 370 380 390 400 410 420 VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR VAEVWMDDYK SHVYIAWNLP 430 440 450 460 470 480 LENPGIDIGD VSERKALRKS LKCKNFQWYL DHVYPEMRRY NNTIAYGELR NNKAKDVCLD 490 500 510 520 530 540 QGPLENHTAI LYPCHGWGPQ LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD 550 560 570 580 590 CDKVKSSLYK RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WAIKNPIK
	Isoform 2 [UniParc]. Checksum: 2907521731EFC58D	FASTA	596	67,516
	10 20 30 40 50 60 MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN LSAHSASPIQ 70 80 90 100 110 120 DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP ATLSPSEEEK AKGPHEKYGY 130 140 150 160 170 180 NSYLSEKISL DRSIPDYRPT KCKELKYSKE LPQISIIFIF VNEALSVILR SVHSAVNHTP 190 200 210 220 230 240 THLLKEIILV DDNREELKAP LEEYVHKRYP GLVKVVRNQK REGLIRARIE GWKAATGQVT 250 260 270 280 290 300 GFFDAHVEFT AGWAEPVLSR IQENRKRVIL PSIDNIKQDN FEVQRYENSA HGYSWELWCM 310 320 330 340 350 360 YISPPKDWWD AGDPSLPIRT PAMIGCSFVV NRKFFGEIGL LDPGMDVYGG ENIELGIKVW 370 380 390 400 410 420 LCGGSMEVLP CSRVAHIERK KKPYNSNIGF YTKRNALRVA EVWMDDYKSH VYIAWNLPLE 430 440 450 460 470 480 NPGIDIGDVS ERKALRKSLK CKNFQWYLDH VYPEMRRYNN TIAYGELRNN KAKDVCLDQG 490 500 510 520 530 540 PLENHTAILY PCHGWGPQLA RYTKEGFLHL GALGTTTLLP DTRCLVDNSK SRLPQLLDCD 550 560 570 580 590 KVKSSLYKRW NFIQNGAIMN KGTGRCLEVE NRGLAGIDLI LRSCTGQRWA IKNPIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of additional transcripts in the Williams-Beuren syndrome critical region." Merla G., Ucla C., Guipponi M., Reymond A. Hum. Genet. 110:429-438(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"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] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[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] OF 1-455 (ISOFORM 1). Strain: C57BL/6J. Tissue: Cerebellum and Embryonic spinal ganglion.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 128-143, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF467979 mRNA. Translation: AAM62404.1. AK035817 mRNA. Translation: BAC29197.1. AK048758 mRNA. Translation: BAC33446.2. AK051281 mRNA. Translation: BAC34591.2. BC052469 mRNA. Translation: AAH52469.1.
IPI	IPI00312664. IPI00458416.
RefSeq	NP_660253.2. NM_145218.3.
UniGene	Mm.299204.
3D structure databases
ProteinModelPortal	Q7TT15.
SMR	Q7TT15. Positions 93-595.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q7TT15.
Proteomic databases
PaxDb	Q7TT15.
PRIDE	Q7TT15.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040.
GeneID	212996.
KEGG	mmu:212996.
Organism-specific databases
CTD	64409.
MGI	MGI:2137594. Wbscr17.
Phylogenomic databases
eggNOG	NOG259711.
GeneTree	ENSGT00670000097647.
HOGENOM	HOG000038228.
HOVERGEN	HBG051699.
InParanoid	Q7TT15.
KO	K00710.
OMA	KGPLEEY.
OrthoDB	EOG4GB75V.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q7TT15.
Bgee	Q7TT15.
Genevestigator	Q7TT15.
GermOnline	ENSMUSG00000034040. Mus musculus.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	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	373790.
SOURCE	Search...

Entry information

Entry name

GLTL3_MOUSE

Accession

Primary (citable) accession number: Q7TT15
Secondary accession number(s): Q8BKN7 , Q8BUY1, Q8BX73, Q8BZC8, Q8K483

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program