O60476 (MA1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	MAN1A2
Synonyms:	MAN1B

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	641 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Tissue specificity	Highest levels of expression in placenta and testis.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-glycan processing Traceable author statement Ref.1. Source: ProtInc lung alveolus development 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
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Traceable author statement Ref.1. Source: ProtInc nucleolus Inferred from direct assay. Source: HPA
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 641	641	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB		PRO_0000210312
Regions
	Topological domain	1 – 36	36	Cytoplasmic Potential
	Transmembrane	37 – 57	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	58 – 641	584	Lumenal Potential
Amino acid modifications
	Glycosylation	631	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O60476 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 19DA691A9C4B0ED3	FASTA	641	73,004
	10 20 30 40 50 60 MTTPALLPLS GRRIPPLNLG PPSFPHHRAT LRLSEKFILL LILSAFITLC FGAFFFLPDS 70 80 90 100 110 120 SKHKRFDLGL EDVLIPHVDA GKGAKNPGVF LIHGPDEHRH REEEERLRNK IRADHEKALE 130 140 150 160 170 180 EAKEKLRKSR EEIRAEIQTE KNKVVQEMKI KENKPLPPVP IPNLVGIRGG DPEDNDIREK 190 200 210 220 230 240 REKIKEMMKH AWDNYRTYGW GHNELRPIAR KGHSPNIFGS SQMGATIVDA LDTLYIMGLH 250 260 270 280 290 300 DEFLDGQRWI EDNLDFSVNS EVSVFEVNIR FIGGLLAAYY LSGEEIFKIK AVQLAEKLLP 310 320 330 340 350 360 AFNTPTGIPW AMVNLKSGVG RNWGWASAGS SILAEFGTLH MEFIHLSYLT GDLTYYKKVM 370 380 390 400 410 420 HIRKLLQKMD RPNGLYPNYL NPRTGRWGQY HTSVGGLGDS FYEYLLKAWL MSDKTDHEAR 430 440 450 460 470 480 KMYDDAIEAI EKHLIKKSRG GLTFIGEWKN GHLEKKMGHL ACFAGGMFAL GADGSRADKA 490 500 510 520 530 540 GHYLELGAEI ARTCHESYDR TALKLGPESF KFDGAVEAVA VRQAEKYYIL RPEVIETYWY 550 560 570 580 590 600 LWRFTHDPRY RQWGWEAALA IEKYCRVNGG FSGVKDVYSS TPTHDDVQQS FFLAETLKYL 610 620 630 640 YLLFSGDDLL PLDHWVFNTE AHPLPVLHLA NTTLSGNPAV R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha-1,2-mannosidase gene involved in N-glycan maturation." Tremblay L.O., Campbell-Dyke N., Herscovics A. Glycobiology 8:585-595(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain and Placenta.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF053626 , AF053622, AF053623, AF053624, AF053625 Genomic DNA. Translation: AAC26201.1. AF027156 mRNA. Translation: AAC26169.1. AF053621 , AF053619, AF053620, AF053615, AF053616, AF053617, AF053618 Genomic DNA. Translation: AAC26200.1. AL157902, AL358072 Genomic DNA. Translation: CAI22315.1. AL358072, AL157902 Genomic DNA. Translation: CAH71079.1. BC063300 mRNA. Translation: AAH63300.1.
IPI	IPI00009145.
RefSeq	NP_006690.1. NM_006699.3.
UniGene	Hs.435938.
3D structure databases
ProteinModelPortal	O60476.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60476. 3 interactions.
MINT	MINT-1184386.
STRING	9606.ENSP00000348959.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
PTM databases
PhosphoSite	O60476.
Proteomic databases
PaxDb	O60476.
PRIDE	O60476.
Protocols and materials databases
DNASU	10905.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356554; ENSP00000348959; ENSG00000198162.
GeneID	10905.
KEGG	hsa:10905.
UCSC	uc001ehd.1. human.
Organism-specific databases
CTD	10905.
GeneCards	GC01P117910.
HGNC	HGNC:6822. MAN1A2.
HPA	HPA034559.
MIM	604345. gene.
neXtProt	NX_O60476.
PharmGKB	PA30571.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG300315.
HOGENOM	HOG000181988.
HOVERGEN	HBG052389.
InParanoid	O60476.
KO	K01230.
OMA	NKVVQEM.
OrthoDB	EOG4NVZJW.
PhylomeDB	O60476.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	O60476.
Bgee	O60476.
CleanEx	HS_MAN1A2.
Genevestigator	O60476.
GermOnline	ENSG00000198162. 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
ChiTaRS	MAN1A2. human.
GenomeRNAi	10905.
NextBio	41419.
SOURCE	Search...

Entry information

Entry name

MA1A2_HUMAN

Accession

Primary (citable) accession number: O60476
Secondary accession number(s): Q9H510

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 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.