Reviewed, UniProtKB/Swiss-Prot Q9UKM7 (MA1B1_HUMAN)

Names and origin

Protein names

Recommended name:
    Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
    EC=3.2.1.113
Alternative name(s):
    ER alpha-1,2-mannosidase
    Mannosidase alpha class 1B member 1
    Man9GlcNAc2-specific-processing alpha-mannosidase

Gene names

Name:	MAN1B1
ORF Names:	UNQ747/PRO1477

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the maturation of Asn-linked oligosaccharides. Trim a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2. The only product is the Man8GlcNAc2 isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. It may be involved in glycoprotein quality control since it is important to target misfolded glycoproteins for degradation.
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	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Tissue specificity	Widely expressed.
Sequence similarities	Belongs to the glycosyl hydrolase 47 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Calcium
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oligosaccharide metabolic process Ref.2 Traceable author statement. Source: ProtInc protein amino acid N-linked glycosylation Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	endoplasmic reticulum Ref.2 Traceable author statement. Source: ProtInc integral to membrane Ref.1 Traceable author statement. Source: UniProtKB membrane fraction Ref.2 Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Ref.1 Traceable author statement. Source: UniProtKB mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Ref.1 Ref.2 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 699

699

Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase

PRO_0000210314

Regions

Topological domain

1 – 84

84

Cytoplasmic Potential

Transmembrane

85 – 105

21

Signal-anchor for type II membrane protein Potential

Topological domain

106 – 699

594

Lumenal Potential

Amino acid modifications

Disulfide bond

527 ↔ 556

Ref.6

Natural variations

Natural variant

59

1

N → S: dbSNP rs968733. Ref.1 Ref.2 Ref.3 Ref.5

VAR_055841

Experimental info

Sequence conflict

204

1

T → A in AAD45504. Ref.2

Sequence conflict

223

1

S → P in AAD45504. Ref.2

Secondary structure

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699

Helix Strand Turn

Details...

Helix

248 – 267

20

Beta strand

271 – 275

5

Turn

276 – 279

4

Beta strand

280 – 282

3

Beta strand

284 – 287

4

Helix

289 – 300

12

Helix

304 – 317

14

Beta strand

325 – 327

3

Helix

328 – 346

19

Helix

349 – 362

14

Helix

363 – 366

4

Beta strand

375 – 378

4

Turn

379 – 381

3

Beta strand

391 – 394

4

Helix

395 – 399

5

Helix

402 – 412

11

Helix

416 – 429

14

Beta strand

441 – 444

4

Turn

445 – 447

3

Beta strand

450 – 452

3

Turn

460 – 462

3

Helix

463 – 475

13

Helix

481 – 497

17

Beta strand

499 – 501

3

Turn

503 – 505

3

Beta strand

508 – 510

3

Beta strand

512 – 514

3

Beta strand

517 – 519

3

Beta strand

521 – 523

3

Helix

524 – 527

4

Helix

528 – 538

11

Helix

543 – 561

19

Beta strand

570 – 573

4

Helix

589 – 591

3

Helix

599 – 611

13

Helix

615 – 630

16

Helix

659 – 662

4

Helix

664 – 672

9

Turn

681 – 683

3

Beta strand

684 – 686

3

Beta strand

692 – 694

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UKM7-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: B8BF3BE333D90261	FASTA	699	79,580
	10 20 30 40 50 60 MAACEGRRSG ALGSSQSDFL TPPVGGAPWA VATTVVMYPP PPPPPHRDFI SVTLSFGENY 70 80 90 100 110 120 DNSKSWRRRS CWRKWKQLSR LQRNMILFLL AFLLFCGLLF YINLADHWKA LAFRLEEEQK 130 140 150 160 170 180 MRPEIAGLKP ANPPVLPAPQ KADTDPENLP EISSQKTQRH IQRGPPHLQI RPPSQDLKDG 190 200 210 220 230 240 TQEEATKRQE APVDPRPEGD PQRTVISWRG AVIEPEQGTE LPSRRAEVPT KPPLPPARTQ 250 260 270 280 290 300 GTPVHLNYRQ KGVIDVFLHA WKGYRKFAWG HDELKPVSRS FSEWFGLGLT LIDALDTMWI 310 320 330 340 350 360 LGLRKEFEEA RKWVSKKLHF EKDVDVNLFE STIRILGGLL SAYHLSGDSL FLRKAEDFGN 370 380 390 400 410 420 RLMPAFRTPS KIPYSDVNIG TGVAHPPRWT SDSTVAEVTS IQLEFRELSR LTGDKKFQEA 430 440 450 460 470 480 VEKVTQHIHG LSGKKDGLVP MFINTHSGLF THLGVFTLGA RADSYYEYLL KQWIQGGKQE 490 500 510 520 530 540 TQLLEDYVEA IEGVRTHLLR HSEPSKLTFV GELAHGRFSA KMDHLVCFLP GTLALGVYHG 550 560 570 580 590 600 LPASHMELAQ ELMETCYQMN RQMETGLSPE IVHFNLYPQP GRRDVEVKPA DRHNLLRPET 610 620 630 640 650 660 VESLFYLYRV TGDRKYQDWG WEILQSFSRF TRVPSGGYSS INNVQDPQKP EPRDKMESFF 670 680 690 LGETLKYLFL LFSDDPNLLS LDAYVFNTEA HPLPIWTPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a specific human alpha1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis." Tremblay L.O., Herscovics A. Glycobiology 9:1073-1078(1999) [PubMed: 10521544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-59. Tissue: Fetal brain, Liver, Placenta and Testis.
[2]	"Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis." Gonzalez D.S., Karaveg K., Vandersall-Nairn A.S., Lal A., Moremen K.W. J. Biol. Chem. 274:21375-21386(1999) [PubMed: 10409699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-699, VARIANT SER-59.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-59.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-59. Tissue: Lung and Placenta.
[6]	"Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases." Vallee F., Karaveg K., Herscovics A., Moremen K.W., Howell P.L. J. Biol. Chem. 275:41287-41298(2000) [PubMed: 10995765] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 243-699, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF148509 mRNA. Translation: AAF03215.1.
AF145732 mRNA. Translation: AAD45504.1.
AY358465 mRNA. Translation: AAQ88830.1.
AL929554, AL807752 Genomic DNA. Translation: CAH72887.1.
AL807752, AL929554 Genomic DNA. Translation: CAI12781.1.
BC002953 mRNA. Translation: AAH02953.1.
BC006079 mRNA. Translation: AAH06079.1.

IPI

IPI00008207.

RefSeq

NP_057303.2.

UniGene

Hs.279881

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FMI	X-ray	1.90	A	243-697	[»]
1FO2	X-ray	2.38	A	243-699	[»]
1FO3	X-ray	1.75	A	243-699	[»]
1X9D	X-ray	1.41	A	172-699	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UKM7.

Protein family/group databases

CAZy

GH47. Glycoside Hydrolase Family 47.

Proteomic databases

PRIDE

Q9UKM7.

Genome annotation databases

Ensembl

ENST00000371589; ENSP00000360645; ENSG00000177239; Homo sapiens. [Genome view]

GeneID

11253.

KEGG

hsa:11253.

UCSC

uc004cld.1. human.

Organism-specific databases

CTD

11253.

GeneCards

GC09P139101.

H-InvDB

HIX0018478.

HGNC

HGNC:6823. MAN1B1.

MIM

604346. gene.

PharmGKB

PA30572.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UKM7.

OMA

KQWIQTG.

OrthoDB

EOG937V1H.

PhylomeDB

Q9UKM7.

Enzyme and pathway databases

BRENDA

3.2.1.113. 247.

Gene expression databases

ArrayExpress

Q9UKM7.

Bgee

Q9UKM7.

CleanEx

HS_MAN1B1.

Genevestigator

Q9UKM7.

GermOnline

ENSG00000177239. Homo sapiens.

Family and domain databases

InterPro

IPR001382. Glyco_hydro_47.
[Graphical view]

Gene3D

G3DSA:1.50.10.50. Glyco_hydro_47. 1 hit.

PANTHER

PTHR11742. Glyco_hydro_47. 1 hit.

Pfam

PF01532. Glyco_hydro_47. 1 hit.
[Graphical view]

PRINTS

PR00747. GLYHDRLASE47.

ProtoNet

Search...

Other Resources

NextBio

42822.

SOURCE

Search...

Entry information

Entry name

MA1B1_HUMAN

Accession

Primary (citable) accession number: Q9UKM7
Secondary accession number(s): Q5VSG3, Q9BRS9, Q9Y5K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.