P33908 (MA1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
EC=3.2.1.113

Alternative name(s):
Man(9)-alpha-mannosidase
Short name=Man9-mannosidase
Mannosidase alpha class 1A member 1
Processing alpha-1,2-mannosidase IA
Short name=Alpha-1,2-mannosidase IA

Gene names

Name:

MAN1A1

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	653 AA.
Sequence status	Complete.
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.
Catalytic activity	Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.
Cofactor	Calcium.
Enzyme regulation	Inhibited by both 1-deoxymannojirimycin and kifunensine.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endoplasmic reticulum Traceable author statement Ref.2. Source: ProtInc endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay PubMed 15308636. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Traceable author statement Ref.2. Source: ProtInc mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 653	653	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA		PRO_0000210308
Regions
	Topological domain	1 – 41	41	Cytoplasmic Potential
	Transmembrane	42 – 62	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	63 – 653	591	Lumenal Potential
Amino acid modifications
	Glycosylation	513	1	N-linked (GlcNAc...) Potential
	Disulfide bond	476 ↔ 508		By similarity
Natural variations
	Natural variant	651	1	R → G. Corresponds to variant rs35544784 [ dbSNP | Ensembl ].		VAR_034102
Experimental info
	Sequence conflict	29 – 47	19	KGSGP…VLLLV → MNSNFITFDLKMSLLPSNL in CAA52831. Ref.2
	Sequence conflict	464	1	G → R in CAA52831. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P33908 [UniParc]. Last modified April 26, 2005. Version 3. Checksum: 9B164926636D8554	FASTA	653	72,969
	10 20 30 40 50 60 MPVGGLLPLF SSPAGGVLGG GLGGGGGRKG SGPAALRLTE KFVLLLVFSA FITLCFGAIF 70 80 90 100 110 120 FLPDSSKLLS GVLFHSSPAL QPAADHKPGP GARAEDAAEG RARRREEGAP GDPEAALEDN 130 140 150 160 170 180 LARIRENHER ALREAKETLQ KLPEEIQRDI LLEKKKVAQD QLRDKAPFRG LPPVDFVPPI 190 200 210 220 230 240 GVESREPADA AIREKRAKIK EMMKHAWNNY KGYAWGLNEL KPISKGGHSS SLFGNIKGAT 250 260 270 280 290 300 IVDALDTLFI MEMKHEFEEA KSWVEENLDF NVNAEISVFE VNIRFVGGLL SAYYLSGEEI 310 320 330 340 350 360 FRKKAVELGV KLLPAFHTPS GIPWALLNMK SGIGRNWPWA SGGSSILAEF GTLHLEFMHL 370 380 390 400 410 420 SHLSGNPIFA EKVMNIRTVL NKLEKPQGLY PNYLNPSSGQ WGQHHVSVGG LGDSFYEYLL 430 440 450 460 470 480 KAWLMSDKTD LEAKKMYFDA VQAIETHLIR KSSSGLTYIA EWKGGLLEHK MGHLTCFAGG 490 500 510 520 530 540 MFALGADAAP EGMAQHYLEL GAEIARTCHE SYNRTFMKLG PEAFRFDGGV EAIATRQNEK 550 560 570 580 590 600 YYILRPEVME TYMYMWRLTH DPKYRKWAWE AVEALENHCR VNGGYSGLRD VYLLHESYDD 610 620 630 640 650 VQQSFFLAET LKYLYLIFSD DDLLPLEHWI FNSEAHLLPI LPKDKKEVEI REE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Molecular cloning and primary structure of Man9-mannosidase from human kidney." Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B. Eur. J. Biochem. 217:535-540(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-653. Tissue: Kidney.
[3]	"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	AL022722, AL078600 Genomic DNA. Translation: CAI20315.1. AL078600 Genomic DNA. Translation: CAB75695.2. X74837 mRNA. Translation: CAA52831.1.
IPI	IPI00844511.
PIR	S38965.
RefSeq	NP_005898.2. NM_005907.3.
UniGene	Hs.102788. Hs.742378.
3D structure databases
ProteinModelPortal	P33908.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000357453.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
PTM databases
PhosphoSite	P33908.
Polymorphism databases
DMDM	62906886.
Proteomic databases
PaxDb	P33908.
PRIDE	P33908.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368468; ENSP00000357453; ENSG00000111885.
GeneID	4121.
KEGG	hsa:4121.
UCSC	uc003pym.1. human.
Organism-specific databases
CTD	4121.
GeneCards	GC06M119540.
HGNC	HGNC:6821. MAN1A1.
HPA	CAB037058.
MIM	604344. gene.
neXtProt	NX_P33908.
PharmGKB	PA30570.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300315.
HOGENOM	HOG000181988.
HOVERGEN	HBG052389.
KO	K01230.
OMA	DKPEGLY.
OrthoDB	EOG4NVZJW.
PhylomeDB	P33908.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P33908.
Bgee	P33908.
CleanEx	HS_MAN1A1.
Genevestigator	P33908.
GermOnline	ENSG00000111885. Homo sapiens.
Family and domain databases
Gene3D	1.50.10.50. 1 hit.
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
PANTHER	PTHR11742. PTHR11742. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL5915.
GenomeRNAi	4121.
NextBio	16180.
SOURCE	Search...

Entry information

Entry name

MA1A1_HUMAN

Accession

Primary (citable) accession number: P33908
Secondary accession number(s): Q9NU44, Q9UJI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 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.