O45947 (GLT10_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 10
Short name=pp-GaNTase 10
EC=2.4.1.41

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10

Gene names

Name:	gly-10
ORF Names:	Y45F10D.3

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	684 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 Metal-binding
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	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 a (identifier: O45947-1)

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.

Note: No experimental confirmation available.

Isoform b (identifier: O45947-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 684	684	Putative polypeptide N-acetylgalactosaminyltransferase 10		PRO_0000059153
Regions
	Topological domain	1 – 74	74	Cytoplasmic Potential
	Transmembrane	75 – 95	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	96 – 684	589	Lumenal Potential
	Domain	581 – 684	104	Ricin B-type lectin
	Region	218 – 330	113	Catalytic subdomain A
	Region	386 – 448	63	Catalytic subdomain B
	Region	448 – 461	14	Flexible loop By similarity
Sites
	Metal binding	314	1	Manganese By similarity
	Metal binding	316	1	Manganese By similarity
	Metal binding	445	1	Manganese By similarity
	Binding site	259	1	Substrate By similarity
	Binding site	314	1	Substrate By similarity
Amino acid modifications
	Glycosylation	198	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Ref.3
	Disulfide bond	209 ↔ 440		By similarity
	Disulfide bond	431 ↔ 509		By similarity
	Disulfide bond	594 ↔ 611		By similarity
	Disulfide bond	637 ↔ 653		By similarity
Natural variations
	Alternative sequence	1 – 62	62	Missing in isoform b.		VSP_032724

Sequences

	Sequence		Length	Mass (Da)
	Isoform a [UniParc]. Last modified April 8, 2008. Version 3. Checksum: 59B9B3F84C2B3445	FASTA	684	78,971
	10 20 30 40 50 60 MVAICIKIGE RERKRVHIML LAYTWKTRVS SHQCNKSPIF GLFAIQFSNI CSNLLLLQQK 70 80 90 100 110 120 LSMGLSRYLS RRHHWVIQYC GLLLFLYLIY SYVATSNDGP NLHEDIPVFQ GQGKDRANPN 130 140 150 160 170 180 PPAALGDEAL DPFEKYRGHE KIKWEDEAAY EKEKRREGPG EWGKPVKLPE DKEVEKEALS 190 200 210 220 230 240 LYKANGYNAY ISDMISLNRS IKDIRHKECK NMMYSAKLPT VSVIFPFHEE HNSTLLRSVY 250 260 270 280 290 300 SVINRSPPEL LKEIILVDDF SEKPALRQPL EDFLKKNKID HIVKVLRTKK REGLIRGRQL 310 320 330 340 350 360 GAQDATGEIL IFLDAHSEAN YNWLPPLLDP IAEDYRTVVC PFVDVIDCET YEVRPQDEGA 370 380 390 400 410 420 RGSFDWAFNY KRLPLTKKDR ESPTKPFNSP VMAGGYFAIS AKWFWELGGY DEGLDIWGGE 430 440 450 460 470 480 QYELSFKVWQ CHGRMVDAPC SRVAHIYRCK YAPFKNAGMG DFVSRNYKRV AEVWMDDYKE 490 500 510 520 530 540 TLYKHRPGVG NADAGDLKLM KGIREKLQCK SFDWFMKEIA FDQDKYYPAV EPKASAEGEI 550 560 570 580 590 600 RNVGTNFCID TQFKEQNQRF GLRKCTSDDK DGGGEQDLRL TRWHDIRPKG RKICFDCSTS 610 620 630 640 650 660 VDKAPVILFD CHSMKGNQLF KYRVAQKQIY HPISGQCLTA DENGKGFLHM KKCDSSSDLQ 670 680 KWAWQTVDNE LLETRQANEA KEQE
	Isoform b [UniParc]. Checksum: F8A3A21159C7E452	FASTA	622	71,812
	10 20 30 40 50 60 MGLSRYLSRR HHWVIQYCGL LLFLYLIYSY VATSNDGPNL HEDIPVFQGQ GKDRANPNPP 70 80 90 100 110 120 AALGDEALDP FEKYRGHEKI KWEDEAAYEK EKRREGPGEW GKPVKLPEDK EVEKEALSLY 130 140 150 160 170 180 KANGYNAYIS DMISLNRSIK DIRHKECKNM MYSAKLPTVS VIFPFHEEHN STLLRSVYSV 190 200 210 220 230 240 INRSPPELLK EIILVDDFSE KPALRQPLED FLKKNKIDHI VKVLRTKKRE GLIRGRQLGA 250 260 270 280 290 300 QDATGEILIF LDAHSEANYN WLPPLLDPIA EDYRTVVCPF VDVIDCETYE VRPQDEGARG 310 320 330 340 350 360 SFDWAFNYKR LPLTKKDRES PTKPFNSPVM AGGYFAISAK WFWELGGYDE GLDIWGGEQY 370 380 390 400 410 420 ELSFKVWQCH GRMVDAPCSR VAHIYRCKYA PFKNAGMGDF VSRNYKRVAE VWMDDYKETL 430 440 450 460 470 480 YKHRPGVGNA DAGDLKLMKG IREKLQCKSF DWFMKEIAFD QDKYYPAVEP KASAEGEIRN 490 500 510 520 530 540 VGTNFCIDTQ FKEQNQRFGL RKCTSDDKDG GGEQDLRLTR WHDIRPKGRK ICFDCSTSVD 550 560 570 580 590 600 KAPVILFDCH SMKGNQLFKY RVAQKQIYHP ISGQCLTADE NGKGFLHMKK CDSSSDLQKW 610 620 AWQTVDNELL ETRQANEAKE QE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[2]	"The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation." Wang H., Spang A., Sullivan M.A., Hryhorenko J., Hagen F.K. Mol. Biol. Cell 16:4202-4213(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL021492 Genomic DNA. Translation: CAA16378.1. AL021492 Genomic DNA. Translation: CAJ76949.1.
PIR	T26930.
RefSeq	NP_001041036.1. NM_001047571.2. NP_001041037.1. NM_001047572.2.
3D structure databases
ProteinModelPortal	O45947.
SMR	O45947. Positions 138-678.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.Y45F10D.3a.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PaxDb	O45947.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y45F10D.3a; Y45F10D.3a; Y45F10D.3.
GeneID	178343.
KEGG	cel:CELE_Y45F10D.3.
UCSC	Y45F10D.3a. c. elegans.
Organism-specific databases
CTD	178343.
WormBase	Y45F10D.3a; CE16642; WBGene00001635; gly-10. Y45F10D.3b; CE39841; WBGene00001635; gly-10.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00680000099551.
HOGENOM	HOG000038227.
InParanoid	O45947.
KO	K00710.
OMA	DKAPVIL.
Enzyme and pathway databases
UniPathway	UPA00378.
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	900740.

Entry information

Entry name

GLT10_CAEEL

Accession

Primary (citable) accession number: O45947
Secondary accession number(s): Q2HQM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	April 8, 2008
Last modified:	April 3, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project