O02773 (MA1A1_PIG) 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
Synonyms:	MAN1A

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	659 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 By similarity.
Enzyme regulation	Inhibited by both 1-deoxymannojirimycin and kifunensine By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.1.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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 – 659	659	Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA		PRO_0000210310
Regions
	Topological domain	1 – 48	48	Cytoplasmic Potential
	Transmembrane	49 – 69	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	70 – 659	590	Lumenal Potential
Sites
	Metal binding	639	1	Calcium By similarity
Amino acid modifications
	Modified residue	12	1	Phosphoserine By similarity
	Disulfide bond	482 ↔ 514		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O02773 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: AA7F17FEAAFE43A6	FASTA	659	73,197
	10 20 30 40 50 60 MPVGGLLPLF SSPAGGGLGG GLGGGLGGGG GGGGRKGSGP SAFRLTEKFV LLLVFSAFIT 70 80 90 100 110 120 LCFGAIFFLP DSSKLLSGVL FHSSPALQPA ADHKPGPGAR AEDAADGRAR PGEEGAPGDP 130 140 150 160 170 180 AAALEDNLAR IRENHERALM EAKETLQKLP EEIQRDILME KEKVAQDQMS NRMGFRLPPV 190 200 210 220 230 240 YLVPLIGAID REPADAAVRE KRAKIKEMMK HAWNNYKLYA WGKNELKPVS KGGHSSSLFG 250 260 270 280 290 300 NIKGATIVDA LDTLFIMKMK NEFEEAKAWV EEHLNFNVNA EVSVFEVNIR FIGGLISAYY 310 320 330 340 350 360 LSGEEIFRKK AVELGVKLLP AFYTPSGIPW ALLNIKSGIG RNWPWASGGS SILAEFGTLH 370 380 390 400 410 420 LEFIHLSYLS GNPFFAEKVM NIRKVLNNLE KPQGLYPNYL NPNSGQWGQY HVSVGGLGDS 430 440 450 460 470 480 FYEYLLKAWL MSDKTDLEAK KMYFDAIKAI ETHLIRKSRN GLTYIAEWKG GLLEHKMGHL 490 500 510 520 530 540 TCFAGGMFAL GADDAPDGLT QHYLQLGAEI ARTCHESYSR TFVKLGPEAF RFDGGVEAIA 550 560 570 580 590 600 TRQNEKYYIL RPEVVETYLY MWRLTHDPKY RKWAWEAVEA LEKHCRVNGG YSGLRDVYVS 610 620 630 640 650 AQTYDDVQQS FFLAETLKYL YLIFSDDDLL PLEHWIFNTE AHPLPVLSRN IKKVEDNEK

References

[1]	"Man9-mannosidase from pig liver is a type-II membrane protein that resides in the endoplasmic reticulum. cDNA cloning and expression of the enzyme in COS 1 cells." Bieberich E., Treml K., Volker C., Rolfs A., Kalz-Fueller B., Bause E. Eur. J. Biochem. 246:681-689(1997) [PubMed: 9219526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION. Tissue: Liver.
[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: 8223597] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12503 mRNA. Translation: CAA73105.1.
PIR	S78554.
RefSeq	NP_999050.1. NM_213885.1.
UniGene	Ssc.14512.
3D structure databases
ProteinModelPortal	O02773.
SMR	O02773. Positions 182-647.
ModBase	Search...
Protein-protein interaction databases
STRING	O02773.
Protein family/group databases
CAZy	GH47. Glycoside Hydrolase Family 47.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396919.
KEGG	ssc:396919.
Organism-specific databases
CTD	4121.
Phylogenomic databases
GeneTree	ENSGT00390000016529.
HOVERGEN	HBG052389.
OrthoDB	EOG4NVZJW.
Family and domain databases
InterPro	IPR001382. Glyco_hydro_47. [Graphical view]
Gene3D	G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.
KO	K01230.
PANTHER	PTHR11742. Glyco_hydro_47. 1 hit.
Pfam	PF01532. Glyco_hydro_47. 1 hit. [Graphical view]
PRINTS	PR00747. GLYHDRLASE47.
SUPFAM	SSF48225. Glyco_hydro_47. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MA1A1_PIG

Accession

Primary (citable) accession number: O02773

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	July 1, 1997
Last modified:	November 16, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program