Q23361 (ALG12_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase
EC=2.4.1.260

Alternative name(s):
Asparagine-linked glycosylation protein 12 homolog
Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
Mannosyltransferase ALG12 homolog

Gene names

ORF Names:

ZC513.5

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man7GlcNAc2) required for protein glycosylation By similarity.
Catalytic activity	Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 22 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Inferred from electronic annotation. Source: InterPro dolichol-linked oligosaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-1,6-mannosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase		PRO_0000215783
Regions
	Transmembrane	1 – 21	21	Helical; Potential
	Transmembrane	60 – 80	21	Helical; Potential
	Transmembrane	86 – 106	21	Helical; Potential
	Transmembrane	133 – 153	21	Helical; Potential
	Transmembrane	172 – 192	21	Helical; Potential
	Transmembrane	198 – 218	21	Helical; Potential
	Transmembrane	259 – 279	21	Helical; Potential
	Transmembrane	284 – 304	21	Helical; Potential
	Transmembrane	309 – 329	21	Helical; Potential
	Transmembrane	339 – 359	21	Helical; Potential
Amino acid modifications
	Glycosylation	413	1	N-linked (GlcNAc...) Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q23361 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: 73BC4F72ADA6B643	FASTA	492	57,150
	10 20 30 40 50 60 MEGTEWIVII VTIIHIILAP GTKVEESFNV QATHDLMFHL PTNLSNYDHS QFPGVVPRTF 70 80 90 100 110 120 IGPISLAILS SPMSFIFRFW AIPKMWQLLL IRATLGLMNA MAFLYFARSV NRKFGRETAM 130 140 150 160 170 180 YLRLIMCTQF HYIFYMSRPL PNTFALILVM IVFERLLEGR YESAVRYATA SVILFRCELV 190 200 210 220 230 240 LLYGPIFLGY MISGRLKVFG FDGAIAIGVR IAAMCLAVSI PIDSYFWGRP LWPEGEVMFF 250 260 270 280 290 300 NVVENRSHEY GTQPFLWYFY SALPRCLLTT TLLVPLGLLV DRRLPQIVLP SVIFIFLYSF 310 320 330 340 350 360 LPHKELRFII YVLPIFCLSA AVFCARMLIN RHKSFFRMIL FFGVILHLLA NVLCTGMFLL 370 380 390 400 410 420 VASKNYPGFD ALNYLQFQNR FDAKKPVTVY IDNACAQTGV NRFLHINDAW TYNKTENLKP 430 440 450 460 470 480 ADLENFDFLV LGTYGNTLKT EVESKFVTWH RPLFFVNSFH QYKIKKSRQF PWIYPEIIYT 490 EKAVVLKNRN YK

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: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"Identification of the hydrophobic glycoproteins of Caenorhabditis elegans." Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J. Glycobiology 15:952-964(2005) [PubMed: 15888633] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FO080486 Genomic DNA. Translation: CCD64068.1.
PIR	T28996.
RefSeq	NP_505071.1. NM_072670.2.
UniGene	Cel.7430.
3D structure databases
ProteinModelPortal	Q23361.
ModBase	Search...
Protein-protein interaction databases
STRING	Q23361.
Protein family/group databases
CAZy	GT22. Glycosyltransferase Family 22.
Proteomic databases
PRIDE	Q23361.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	ZC513.5; ZC513.5; ZC513.5.
GeneID	179185.
KEGG	cel:ZC513.5.
NMPDR	fig|6239.3.peg.18659.
UCSC	ZC513.5. c. elegans.
Organism-specific databases
CTD	179185.
WormBase	ZC513.5; CE29152; WBGene00022629.
Phylogenomic databases
eggNOG	meNOG05730.
GeneTree	EMGT00050000010281.
HOGENOM	HBG385438.
InParanoid	Q23361.
OMA	WGTSPLL.
PhylomeDB	Q23361.
Gene expression databases
ArrayExpress	Q23361.
Family and domain databases
InterPro	IPR005599. GPI_mannosylTrfase. [Graphical view]
KO	K03847.
PANTHER	PTHR22760. Alg9_trans. 1 hit.
Pfam	PF03901. Glyco_transf_22. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	904286.

Entry information

Entry name

ALG12_CAEEL

Accession

Primary (citable) accession number: Q23361

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2001
Last modified:	December 14, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project