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O09159 (MA2B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal alpha-mannosidase

Short name=Laman
EC=3.2.1.24
Alternative name(s):
Lysosomal acid alpha-mannosidase
Mannosidase alpha class 2B member 1
Mannosidase alpha-B
Gene names
Name:Man2b1
Synonyms:Laman, Man2b, Manb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1013 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the glycosyl hydrolase 38 family.

Sequence caution

The sequence AAC09470.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC53369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4949 Potential
Chain50 – 1013964Lysosomal alpha-mannosidase
PRO_0000012076

Sites

Active site1961Nucleophile By similarity
Metal binding721Zinc By similarity
Metal binding741Zinc By similarity
Metal binding1961Zinc By similarity
Metal binding4461Zinc By similarity

Amino acid modifications

Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation6331N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential
Glycosylation6931N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 358 By similarity
Disulfide bond268 ↔ 273 By similarity
Disulfide bond412 ↔ 472 By similarity
Disulfide bond493 ↔ 501 By similarity

Experimental info

Sequence conflict45 – 495PGARA → LASG in AAC53369. Ref.1
Sequence conflict45 – 495PGARA → LASG in AAC78560. Ref.2
Sequence conflict3441V → A in AAC53369. Ref.1
Sequence conflict3441V → A in AAC78560. Ref.2
Sequence conflict3441V → A in AAH05430. Ref.4
Sequence conflict3441V → A in AAC09470. Ref.5
Sequence conflict9801Y → F in AAC53369. Ref.1
Sequence conflict9801Y → F in AAC78560. Ref.2
Sequence conflict9801Y → F in AAH05430. Ref.4
Sequence conflict9801Y → F in AAC09470. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O09159 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: A83B5397D9D38D31

FASTA1,013114,648
        10         20         30         40         50         60 
MGTGPLTSGV RAGGGNTGWL WMSSCNLGSP VLPISFLFWL LLAAPGARAA GYKTCPPTKP 

        70         80         90        100        110        120 
GMLNVHLLPH THDDVGWLKT VDQYYYGILS DVQHASVQYI LDSVVSSLLE KPTRRFIYVE 

       130        140        150        160        170        180 
MAFFSRWWKQ QTSATQDAVR NLVRQGRLEF VNGGWVMNDE AATHYGAIVD QMTLGLRFLQ 

       190        200        210        220        230        240 
DTFGSDGLPR VAWHIDPFGH SREQASLFAQ MGFDGFFLGR IDYQDKLNRK KKLRMEELWR 

       250        260        270        280        290        300 
ASDSLEPPAA DLFTGVLPNN YNPPKYLCWD VLCTDPPVVD NPRSPEFNAK TLVNYFLKLA 

       310        320        330        340        350        360 
SSQKGFYRTN HTVMTMGSDF HYENANMWFK NMDKLIRLVN AQQVNGSLVH VLYSTPTCYL 

       370        380        390        400        410        420 
WELNKANLTW TVKEDDFFPY ADGPHMFWTG YFSSRPALKR YERLSYNFLQ VCNQLEALVG 

       430        440        450        460        470        480 
PEANVGPYGS GDSAPLQEAM AVLQHHDAVS GTARQNVVND YARQLAAGWG PCEVLVSNAL 

       490        500        510        520        530        540 
ARLSHYKQNF SFCRELNISI CPVSQTSERF QVTLYNPLGR KVDQMVRLPV YEGNFIVKDP 

       550        560        570        580        590        600 
HDKNISSNVV MVPSYYSETY QWELLFPASV PALGFSTYSV AKMSDLNHQA HNLLSRPRKH 

       610        620        630        640        650        660 
KSHHVLVIEN KYMRATFDSG TGLLMKIENL EQNLSLPVSQ GFFWYNASVG DEESSQASGA 

       670        680        690        700        710        720 
YIFRPNVGKP IPVSRWAQIS LVKTALVQEV HQNFSAWCSQ VIRLYKGQRH LELEWTVGPI 

       730        740        750        760        770        780 
PVRDDWGKEV ISRFDTPMKT KGQFFTDSNG REILKRRDDY RPTWTLNQTE PVAGNYYPVN 

       790        800        810        820        830        840 
TRIYITDGQM QLTVLTDRSQ GGSSLQDGSL ELMVHRRLLV DDDRGVSEPL LETDTGDKVR 

       850        860        870        880        890        900 
GRHLVLLSSV SDAAARHRLL AEQEVLAPQV VLSLGGSSPY HSRATPKTQF SGLRQELPPQ 

       910        920        930        940        950        960 
VHLLTLARWG PKMLLLRLEH QFALKEDSDR NLSSPVTLNV QNLFQTFTIN YLQETTLAAN 

       970        980        990       1000       1010 
QPLSRASRLK WMTNTGPTSY PEPSKLDPTS VTLKPMEIRT FLASVQWQEH RPA 

« Hide

References

« Hide 'large scale' references
[1]"Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA."
Beccari T., Appolloni M.G., Costanzi E., Stinchi S., Stirling J.L., Della Fazia M.A., Servillo G., Viola M.P., Orlacchio A.
Biochem. J. 327:45-49(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[2]"Promoter characterization and structure of the gene encoding mouse lysosomal alpha-d-mannosidase."
Stinchi S., Orlacchio A., Costanzi E., Stirling J.L., Menghini A.R., Orlacchio A., Beccari T.
Mamm. Genome 9:869-873(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[4]"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].
Strain: C57BL/6J.
Tissue: Mammary gland.
[5]"Cloning, expression, purification, and characterization of the murine lysosomal acid alpha-mannosidase."
Merkle R.K., Zhang Y., Ruest P.J., Lal A., Liao Y.-F., Moremen K.W.
Biochim. Biophys. Acta 1336:132-146(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-1013.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29947 mRNA. Translation: AAC53369.1. Different initiation.
AF044192 expand/collapse EMBL AC list , AF044174, AF044175, AF044176, AF044177, AF044178, AF044179, AF044180, AF044181, AF044182, AF044183, AF044184, AF044185, AF044186, AF044187, AF044188, AF044189, AF044190, AF044191 Genomic DNA. Translation: AAC78560.1.
AK147928 mRNA. Translation: BAE28235.1.
AK004817 mRNA. Translation: BAB23588.1.
BC005430 mRNA. Translation: AAH05430.1.
U87240 mRNA. Translation: AAC09470.1. Different initiation.
PIRT42385.
RefSeqNP_034894.2. NM_010764.2.
UniGeneMm.4219.

3D structure databases

ProteinModelPortalO09159.
SMRO09159. Positions 51-341, 349-421, 431-583, 606-875, 886-1007.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO09159. 2 interactions.
MINTMINT-1675875.

Protein family/group databases

CAZyGH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbO09159.
PRIDEO09159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034121; ENSMUSP00000034121; ENSMUSG00000005142.
GeneID17159.
KEGGmmu:17159.
UCSCuc009mpk.1. mouse.

Organism-specific databases

CTD4125.
MGIMGI:107286. Man2b1.

Phylogenomic databases

eggNOGCOG0383.
GeneTreeENSGT00510000046304.
HOGENOMHOG000007676.
HOVERGENHBG052391.
InParanoidQ3UGH3.
KOK12311.
OMATDGNMQL.
OrthoDBEOG786H2P.
TreeFamTF313840.

Gene expression databases

BgeeO09159.
CleanExMM_MAN2B1.
GenevestigatorO09159.

Family and domain databases

Gene3D1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProIPR011013. 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.
IPR000602. Glyco_hydro_38_N.
[Graphical view]
PfamPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMAN2B1. mouse.
NextBio291430.
PROO09159.
SOURCESearch...

Entry information

Entry nameMA2B1_MOUSE
AccessionPrimary (citable) accession number: O09159
Secondary accession number(s): O55037 expand/collapse secondary AC list , Q3UGH3, Q64443, Q9DBQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 117 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries