Q16706 (MA2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1144 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 By similarity.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein 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 Reference proteome
Gene Ontology (GO)
Biological_process	N-glycan processing Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara lung alveolus development Inferred from electronic annotation. Source: Compara mannose metabolic process Inferred from electronic annotation. Source: InterPro mitochondrion organization Inferred from electronic annotation. Source: Compara post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome respiratory gaseous exchange Inferred from electronic annotation. Source: Compara vacuole organization Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome 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 electronic annotation. Source: Compara mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Traceable author statement Ref.1. Source: ProtInc 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 – 1144	1144	Alpha-mannosidase 2		PRO_0000206902
Regions
	Topological domain	1 – 5	5	Cytoplasmic Potential
	Transmembrane	6 – 26	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 1144	1118	Lumenal Potential
Sites
	Active site	289	1	Nucleophile By similarity
	Metal binding	175	1	Zinc By similarity
	Metal binding	177	1	Zinc By similarity
	Metal binding	289	1	Zinc By similarity
	Metal binding	569	1	Zinc By similarity
Amino acid modifications
	Modified residue	80	1	Phosphoserine By similarity
	Modified residue	82	1	Phosphoserine By similarity
	Glycosylation	78	1	N-linked (GlcNAc...) Ref.3
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	1125	1	N-linked (GlcNAc...) Ref.3
Experimental info
	Sequence conflict	608	1	L → G in AAC50302. Ref.1
	Sequence conflict	1026	1	Missing in BAA10017. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q16706 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: A1814C63D1CE4FAC	FASTA	1,144	131,141
	10 20 30 40 50 60 MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPRNPRRE GSFPQGQLSM LQEKIDHLER 70 80 90 100 110 120 LLAENNEIIS NIRDSVINLS ESVEDGPKSS QSNFSQGAGS HLLPSQLSLS VDTADCLFAS 130 140 150 160 170 180 QSGSHNSDVQ MLDVYSLISF DNPDGGVWKQ GFDITYESNE WDTEPLQVFV VPHSHNDPGW 190 200 210 220 230 240 LKTFNDYFRD KTQYIFNNMV LKLKEDSRRK FIWSEISYLS KWWDIIDIQK KDAVKSLIEN 250 260 270 280 290 300 GQLEIVTGGW VMPDEATPHY FALIDQLIEG HQWLENNIGV KPRSGWAIDP FGHSPTMAYL 310 320 330 340 350 360 LNRAGLSHML IQRVHYAVKK HFALHKTLEF FWRQNWDLGS VTDILCHMMP FYSYDIPHTC 370 380 390 400 410 420 GPDPKICCQF DFKRLPGGRF GCPWGVPPET IHPGNVQSRA RMLLDQYRKK SKLFRTKVLL 430 440 450 460 470 480 APLGDDFRYC EYTEWDLQFK NYQQLFDYMN SQSKFKVKIQ FGTLSDFFDA LDKADETQRD 490 500 510 520 530 540 KGQSMFPVLS GDFFTYADRD DHYWSGYFTS RPFYKRMDRI MESHLRAAEI LYYFALRQAH 550 560 570 580 590 600 KYKINKFLSS SLYTALTEAR RNLGLFQHHD AITGTAKDWV VVDYGTRLFH SLMVLEKIIG 610 620 630 640 650 660 NSAFLLILKD KLTYDSYSPD TFLEMDLKQK SQDSLPQKNI IRLSAEPRYL VVYNPLEQDR 670 680 690 700 710 720 ISLVSVYVSS PTVQVFSASG KPVEVQVSAV WDTANTISET AYEISFRAHI PPLGLKVYKI 730 740 750 760 770 780 LESASSNSHL ADYVLYKNKV EDSGIFTIKN MINTEEGITL ENSFVLLRFD QTGLMKQMMT 790 800 810 820 830 840 KEDGKHHEVN VQFSWYGTTI KRDKSGAYLF LPDGNAKPYV YTTPPFVRVT HGRIYSEVTC 850 860 870 880 890 900 FFDHVTHRVR LYHIQGIEGQ SVEVSNIVDI RKVYNREIAM KISSDIKSQN RFYTDLNGYQ 910 920 930 940 950 960 IQPRMTLSKL PLQANVYPMT TMAYIQDAKH RLTLLSAQSL GVSSLNSGQI EVIMDRRLMQ 970 980 990 1000 1010 1020 DDNRGLEQGI QDNKITANLF RILLEKRSAV NTEEEKKSVS YPSLLSHITS SLMNHPVIPM 1030 1040 1050 1060 1070 1080 ANKFSSPTLE LQGEFSPLQS SLPCDIHLVN LRTIQSKVGN GHSNEAALIL HRKGFDCRFS 1090 1100 1110 1120 1130 1140 SKGTGLFCST TQGKILVQKL LNKFIVESLT PSSLSLMHSP PGTQNISEIN LSPMEISTFR IQLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme." Misago M., Liao Y.-F., Kudo S., Eto S., Mattei M.-G., Moremen K.W., Fukuda M.N. Proc. Natl. Acad. Sci. U.S.A. 92:11766-11770(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Molecular cloning and sequence analysis of human Golgi mannosidase II." Misumi Y., Hashimoto C., Sohoda M., Ogata S., Ikehara Y. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-1125, MASS SPECTROMETRY. Tissue: Plasma.
[4]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U31520 mRNA. Translation: AAC50302.1. D63998 mRNA. Translation: BAA10017.1.
IPI	IPI00003802.
RefSeq	NP_002363.2. NM_002372.2.
UniGene	Hs.432822.
3D structure databases
ProteinModelPortal	Q16706.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2807655.
STRING	9606.ENSP00000261483.
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
PTM databases
PhosphoSite	Q16706.
Polymorphism databases
DMDM	146345453.
Proteomic databases
PaxDb	Q16706.
PRIDE	Q16706.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261483; ENSP00000261483; ENSG00000112893.
GeneID	4124.
KEGG	hsa:4124.
UCSC	uc003kou.1. human.
Organism-specific databases
CTD	4124.
GeneCards	GC05P109053.
H-InvDB	HIX0005076.
HGNC	HGNC:6824. MAN2A1.
HPA	CAB022377. HPA026896.
MIM	154582. gene.
neXtProt	NX_Q16706.
PharmGKB	PA30573.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0383.
HOGENOM	HOG000293253.
HOVERGEN	HBG052390.
InParanoid	Q16706.
KO	K01231.
OMA	QIQPRMT.
OrthoDB	EOG4T782F.
PhylomeDB	Q16706.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q16706.
Bgee	Q16706.
CleanEx	HS_MAN2A1.
Genevestigator	Q16706.
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
BindingDB	Q16706.
ChEMBL	CHEMBL4056.
GenomeRNAi	4124.
NextBio	16192.
SOURCE	Search...

Entry information

Entry name

MA2A1_HUMAN

Accession

Primary (citable) accession number: Q16706
Secondary accession number(s): Q16767

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.