Reviewed, UniProtKB/Swiss-Prot Q18788 (MAN12_CAEEL)

Names and origin

Protein names

Recommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5
    EC=3.2.1.113
Alternative name(s):
    Processing alpha-1,2-mannosidase C52E4.5
      Short name=Alpha-1,2-mannosidase C52E4.5

Gene names

ORF Names:

C52E4.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2 By similarity.
Catalytic activity	Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Cofactor	Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW mannosyl-oligosaccharide 1,2-alpha-mannosidase 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 – 590	590	Mannosyl-oligosaccharide 1,2-alpha-mannosidase C52E4.5		PRO_0000248514
Regions
	Topological domain	1 – 9	9	Cytoplasmic Potential
	Transmembrane	10 – 30	21	Signal-anchor for type II membrane protein Potential
	Topological domain	31 – 590	560	Lumenal Potential
Amino acid modifications
	Glycosylation	156	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Ref.3 Ref.2
	Glycosylation	402	1	N-linked (GlcNAc...) Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q18788-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B0714A3671204843	FASTA	590	66,950
	10 20 30 40 50 60 MKTVRFNKQA LAILAACFIF LLCVVCYFSA SSESHNAVVV GERARGHIAV RDVENRHLAE 70 80 90 100 110 120 EKHAVIHAKT VGKIERVVSQ EKVEILRPAR VESKPPGEKT STEPEETGVG KAPIQTSEGL 130 140 150 160 170 180 EKLIGKIHYE NKDEENDLRR QKVKEMMIHA WEGYKNYSWG ANELRPMSKK PNSQNIFGGS 190 200 210 220 230 240 QMPATIVDAA DTLFIMDLKD KYKEARDYIE NNFSMAKSTS TLSVFETTIR FLGGLLSLYA 250 260 270 280 290 300 LTQESFYIEK AREVGEALLP AFNTPSGIPK SNLDVASKHA SNYGWANGGQ SILSEIGSLH 310 320 330 340 350 360 LEFLYLSRIS NAPIFEKKVK KVRDALEKAE KPNGLYSNYI NPDTGKFTGS HMSLGALGDS 370 380 390 400 410 420 FYEYLIKSYV QSNYTDTQAK NMYWDVSDAI QKHMIKVSKQ SNLTYTVELN NGQAQHKMGH 430 440 450 460 470 480 LACFVPGMFA LQAINEDTEE EKLRIMTLAE ELAKTCHESY IRSETHIGPE MFYFNERDEA 490 500 510 520 530 540 TSKHSENGYI QRPEVIEGWF YLWRLTGKTM YRDWVWDAVQ AIEKYCRVDS GFTGLQNVYN 550 560 570 580 590 PKAGREDVMQ SFFLAEFLKY AYLTFADESL ISLDKWVFNT EAHPVPVLTN

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]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-373, MASS SPECTROMETRY.
[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: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-156; ASN-373 AND ASN-402, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z78012 Genomic DNA. Translation: CAB01415.1.
PIR	T20153.
RefSeq	NP_506006.1.
UniGene	Cel.4401
3D structure databases
HSSP	HSSP built from PDB template 1FO3 based on UniProtKB Q9UKM7.
ModBase	Search...
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Genome annotation databases
Ensembl	C52E4.5. Caenorhabditis elegans. [Contig view]
GeneID	179642.
KEGG	cel:C52E4.5.
NMPDR	fig|6239.3.peg.19871.
Organism-specific databases
WormBase	WBGene00008258. C52E4.5.
WormPep	C52E4.5. CE08947. [WorfDB]
Phylogenomic databases
OMA	Q18788. PEVIEGW.
Enzyme and pathway databases
BRENDA	3.2.1.113. 672.
Gene expression databases
ArrayExpress	Q18788.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
ProtoNet	Search...
Other Resources
NextBio	906268.

Entry information

Entry name

MAN12_CAEEL

Accession

Primary (citable) accession number: Q18788

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project