Alpha-mannosidase 2 - Mus musculus (Mouse)

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P27046 (MA2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-mannosidase 2
EC=3.2.1.114

Alternative name(s):
Golgi alpha-mannosidase II
Short name=AMan II
Short name=Man II
Mannosidase alpha class 2A member 1
Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase

Gene names

Name:	Man2a1
Synonyms:	Mana2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1150 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.
Catalytic activity	Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man₅(GlcNAc)₃.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homodimer; disulfide-linked.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	All tissues, mostly in adrenal and thymus.
Post-translational modification	Glycosylated By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-glycan processing Inferred from genetic interaction PubMed 16754854. Source: MGI in utero embryonic development Inferred from genetic interaction PubMed 16754854. Source: MGI liver development Inferred from genetic interaction PubMed 16754854. Source: MGI lung alveolus development Inferred from genetic interaction PubMed 16754854. Source: MGI mannose metabolic process Inferred from electronic annotation. Source: InterPro mitochondrion organization Inferred from genetic interaction PubMed 16754854. Source: MGI respiratory gaseous exchange Inferred from genetic interaction PubMed 16754854. Source: MGI vacuole organization Inferred from genetic interaction PubMed 16754854. Source: MGI
Cellular_component	Golgi membrane Inferred from direct assay PubMed 11042173. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing N-glycosyl compounds Inferred from direct assay PubMed 16754854. Source: MGI mannosidase activity Inferred from direct assay PubMed 16754854. Source: MGI mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1150

1150

Alpha-mannosidase 2

PRO_0000206903

Regions

Topological domain

1 – 5

Cytoplasmic Potential

Transmembrane

6 – 26

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

27 – 1150

1124

Lumenal Potential

Sites

Active site

288

Nucleophile By similarity

Metal binding

174

Zinc By similarity

Metal binding

176

Zinc By similarity

Metal binding

288

Zinc By similarity

Metal binding

568

Zinc By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.3

Modified residue

Phosphoserine Ref.3

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

1129

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

673

V → G in CAA43480. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P27046 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 5CDD9DD388DF5BC6
Show »

FASTA

1,150

131,631

        10         20         30         40         50         60 
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPRGPRQE GSFPQGQLSI LQEKIDHLER 

        70         80         90        100        110        120 
LLAENNEIIS NIRDSVINLS ESVEDGPRGS PGNASQGSIH LHSPQLALQA DPRDCLFASQ 

       130        140        150        160        170        180 
SGSQPRDVQM LDVYDLIPFD NPDGGVWKQG FDIKYEADEW DHEPLQVFVV PHSHNDPGWL 

       190        200        210        220        230        240 
KTFNDYFRDK TQYIFNNMVL KLKEDSSRKF MWSEISYLAK WWDIIDIPKK EAVKSLLQNG 

       250        260        270        280        290        300 
QLEIVTGGWV MPDEATPHYF ALIDQLIEGH QWLEKNLGVK PRSGWAIDPF GHSPTMAYLL 

       310        320        330        340        350        360 
KRAGFSHMLI QRVHYAIKKH FSLHKTLEFF WRQNWDLGSA TDILCHMMPF YSYDIPHTCG 

       370        380        390        400        410        420 
PDPKICCQFD FKRLPGGRYG CPWGVPPEAI SPGNVQSRAQ MLLDQYRKKS KLFRTKVLLA 

       430        440        450        460        470        480 
PLGDDFRFSE YTEWDLQCRN YEQLFSYMNS QPHLKVKIQF GTLSDYFDAL EKAVAAEKKS 

       490        500        510        520        530        540 
SQSVFPALSG DFFTYADRDD HYWSGYFTSR PFYKRMDRIM ESRIRAAEIL YQLALKQAQK 

       550        560        570        580        590        600 
YKINKFLSSP HYTTLTEARR NLGLFQHHDA ITGTAKDWVV VDYGTRLFQS LNSLEKIIGD 

       610        620        630        640        650        660 
SAFLLILKDK KLYQSDPSKA FLEMDTKQSS QDSLPQKIII QLSAQEPRYL VVYNPFEQER 

       670        680        690        700        710        720 
HSVVSIRVNS ATVKVLSDSG KPVEVQVSAV WNDMRTISQA AYEVSFLAHI PPLGLKVFKI 

       730        740        750        760        770        780 
LESQSSSSHL ADYVLYNNDG LAENGIFHVK NMVDAGDAIT IENPFLAIWF DRSGLMEKVR 

       790        800        810        820        830        840 
RKEDSRQHEL KVQFLWYGTT NKRDKSGAYL FLPDGQGQPY VSLRPPFVRV TRGRIYSDVT 

       850        860        870        880        890        900 
CFLEHVTHKV RLYNIQGIEG QSMEVSNIVN IRNVHNREIV MRISSKINNQ NRYYTDLNGY 

       910        920        930        940        950        960 
QIQPRRTMSK LPLQANVYPM CTMAYIQDAE HRLTLLSAQS LGASSMASGQ IEVFMDRRLM 

       970        980        990       1000       1010       1020 
QDDNRGLGQG VHDNKITANL FRILLEKRSA VNMEEEKKSP VSYPSLLSHM TSSFLNHPFL 

      1030       1040       1050       1060       1070       1080 
PMVLSGQLPS PAFELLSEFP LLQSSLPCDI HLVNLRTIQS KMGKGYSDEA ALILHRKGFD 

      1090       1100       1110       1120       1130       1140 
CQFSSRGIGL PCSTTQGKMS VLKLFNKFAV ESLVPSSLSL MHSPPDAQNM SEVSLSPMEI 

      1150 
STFRIRLRWT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans." Moremen K.W., Robbins P.W. J. Cell Biol. 115:1521-1534(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: BALB/c.
[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]. Tissue: Brain.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61172 mRNA. Translation: CAA43480.1. BC138371 mRNA. Translation: AAI38372.1. BC138372 mRNA. Translation: AAI38373.1.
IPI	IPI00114044.
PIR	A41641.
RefSeq	NP_032575.2. NM_008549.2.
UniGene	Mm.2433.
3D structure databases
ProteinModelPortal	P27046.
SMR	P27046. Positions 127-1019.
ModBase	Search...
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
PTM databases
PhosphoSite	P27046.
Proteomic databases
PaxDb	P27046.
PRIDE	P27046.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086723; ENSMUSP00000083928; ENSMUSG00000024085.
GeneID	17158.
KEGG	mmu:17158.
Organism-specific databases
CTD	4124.
MGI	MGI:104669. Man2a1.
Phylogenomic databases
eggNOG	COG0383.
GeneTree	ENSGT00510000046304.
HOGENOM	HOG000293253.
HOVERGEN	HBG052390.
InParanoid	P27046.
KO	K01231.
OMA	QIQPRMT.
OrthoDB	EOG4T782F.
Enzyme and pathway databases
BRENDA	3.2.1.114. 3474.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P27046.
Bgee	P27046.
CleanEx	MM_MAN2A1.
Genevestigator	P27046.
GermOnline	ENSMUSG00000024085. Mus musculus.
Family and domain databases
Gene3D	2.60.40.1180. 1 hit. 3.20.110.10. 1 hit.
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR013780. Glyco_hydro_13_b. IPR027291. Glyco_hydro_38/57_N. IPR011682. Glyco_hydro_38_C. IPR015341. Glyco_hydro_38_cen_dom. IPR000602. Glyco_hydro_38_N. [Graphical view]
Pfam	PF09261. Alpha-mann_mid. 1 hit. PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view]
SMART	SM00872. Alpha-mann_mid. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	MAN2A1. mouse.
NextBio	291426.
SOURCE	Search...

Entry information

Entry name

MA2A1_MOUSE

Accession

Primary (citable) accession number: P27046
Secondary accession number(s): B9EHS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents