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O09159

- MA2B1_MOUSE

UniProt

O09159 - MA2B1_MOUSE

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Protein

Lysosomal alpha-mannosidase

Gene
Man2b1, Laman, Man2b, Manb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi72 – 721Zinc By similarity
Metal bindingi74 – 741Zinc By similarity
Active sitei196 – 1961Nucleophile By similarity
Metal bindingi196 – 1961Zinc By similarity
Metal bindingi446 – 4461Zinc By similarity

GO - Molecular functioni

  1. alpha-mannosidase activity Source: MGI
  2. mannose binding Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. learning or memory Source: MGI
  2. mannose metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysosomal alpha-mannosidase (EC:3.2.1.24)
Short name:
Laman
Alternative name(s):
Lysosomal acid alpha-mannosidase
Mannosidase alpha class 2B member 1
Mannosidase alpha-B
Gene namesi
Name:Man2b1
Synonyms:Laman, Man2b, Manb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:107286. Man2b1.

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4949 Reviewed predictionAdd
BLAST
Chaini50 – 1013964Lysosomal alpha-mannosidasePRO_0000012076Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 358 By similarity
Disulfide bondi268 ↔ 273 By similarity
Glycosylationi310 – 3101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi345 – 3451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi367 – 3671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi412 ↔ 472 By similarity
Glycosylationi489 – 4891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi493 ↔ 501 By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi544 – 5441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi633 – 6331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi646 – 6461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi693 – 6931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi767 – 7671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi931 – 9311N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO09159.
PaxDbiO09159.
PRIDEiO09159.

Expressioni

Gene expression databases

BgeeiO09159.
CleanExiMM_MAN2B1.
GenevestigatoriO09159.

Interactioni

Protein-protein interaction databases

IntActiO09159. 2 interactions.
MINTiMINT-1675875.

Structurei

3D structure databases

ProteinModelPortaliO09159.
SMRiO09159. Positions 51-341, 349-421, 431-583, 606-875, 886-1007.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
HOGENOMiHOG000007676.
HOVERGENiHBG052391.
InParanoidiQ3UGH3.
KOiK12311.
OMAiNMQLTVL.
OrthoDBiEOG786H2P.
TreeFamiTF313840.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. 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.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O09159-1 [UniParc]FASTAAdd to Basket

« Hide

MGTGPLTSGV RAGGGNTGWL WMSSCNLGSP VLPISFLFWL LLAAPGARAA     50
GYKTCPPTKP GMLNVHLLPH THDDVGWLKT VDQYYYGILS DVQHASVQYI 100
LDSVVSSLLE KPTRRFIYVE MAFFSRWWKQ QTSATQDAVR NLVRQGRLEF 150
VNGGWVMNDE AATHYGAIVD QMTLGLRFLQ DTFGSDGLPR VAWHIDPFGH 200
SREQASLFAQ MGFDGFFLGR IDYQDKLNRK KKLRMEELWR ASDSLEPPAA 250
DLFTGVLPNN YNPPKYLCWD VLCTDPPVVD NPRSPEFNAK TLVNYFLKLA 300
SSQKGFYRTN HTVMTMGSDF HYENANMWFK NMDKLIRLVN AQQVNGSLVH 350
VLYSTPTCYL WELNKANLTW TVKEDDFFPY ADGPHMFWTG YFSSRPALKR 400
YERLSYNFLQ VCNQLEALVG PEANVGPYGS GDSAPLQEAM AVLQHHDAVS 450
GTARQNVVND YARQLAAGWG PCEVLVSNAL ARLSHYKQNF SFCRELNISI 500
CPVSQTSERF QVTLYNPLGR KVDQMVRLPV YEGNFIVKDP HDKNISSNVV 550
MVPSYYSETY QWELLFPASV PALGFSTYSV AKMSDLNHQA HNLLSRPRKH 600
KSHHVLVIEN KYMRATFDSG TGLLMKIENL EQNLSLPVSQ GFFWYNASVG 650
DEESSQASGA YIFRPNVGKP IPVSRWAQIS LVKTALVQEV HQNFSAWCSQ 700
VIRLYKGQRH LELEWTVGPI PVRDDWGKEV ISRFDTPMKT KGQFFTDSNG 750
REILKRRDDY RPTWTLNQTE PVAGNYYPVN TRIYITDGQM QLTVLTDRSQ 800
GGSSLQDGSL ELMVHRRLLV DDDRGVSEPL LETDTGDKVR GRHLVLLSSV 850
SDAAARHRLL AEQEVLAPQV VLSLGGSSPY HSRATPKTQF SGLRQELPPQ 900
VHLLTLARWG PKMLLLRLEH QFALKEDSDR NLSSPVTLNV QNLFQTFTIN 950
YLQETTLAAN QPLSRASRLK WMTNTGPTSY PEPSKLDPTS VTLKPMEIRT 1000
FLASVQWQEH RPA 1013
Length:1,013
Mass (Da):114,648
Last modified:July 27, 2011 - v4
Checksum:iA83B5397D9D38D31
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 495PGARA → LASG in AAC53369. 1 Publication
Sequence conflicti45 – 495PGARA → LASG in AAC78560. 1 Publication
Sequence conflicti344 – 3441V → A in AAC53369. 1 Publication
Sequence conflicti344 – 3441V → A in AAC78560. 1 Publication
Sequence conflicti344 – 3441V → A in AAH05430. 1 Publication
Sequence conflicti344 – 3441V → A in AAC09470. 1 Publication
Sequence conflicti980 – 9801Y → F in AAC53369. 1 Publication
Sequence conflicti980 – 9801Y → F in AAC78560. 1 Publication
Sequence conflicti980 – 9801Y → F in AAH05430. 1 Publication
Sequence conflicti980 – 9801Y → F in AAC09470. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29947 mRNA. Translation: AAC53369.1. Different initiation.
AF044192
, 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.
CCDSiCCDS22494.1.
PIRiT42385.
RefSeqiNP_034894.2. NM_010764.2.
UniGeneiMm.4219.

Genome annotation databases

EnsembliENSMUST00000034121; ENSMUSP00000034121; ENSMUSG00000005142.
GeneIDi17159.
KEGGimmu:17159.
UCSCiuc009mpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29947 mRNA. Translation: AAC53369.1 . Different initiation.
AF044192
, 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.
CCDSi CCDS22494.1.
PIRi T42385.
RefSeqi NP_034894.2. NM_010764.2.
UniGenei Mm.4219.

3D structure databases

ProteinModelPortali O09159.
SMRi O09159. Positions 51-341, 349-421, 431-583, 606-875, 886-1007.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O09159. 2 interactions.
MINTi MINT-1675875.

Protein family/group databases

CAZyi GH38. Glycoside Hydrolase Family 38.

Proteomic databases

MaxQBi O09159.
PaxDbi O09159.
PRIDEi O09159.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034121 ; ENSMUSP00000034121 ; ENSMUSG00000005142 .
GeneIDi 17159.
KEGGi mmu:17159.
UCSCi uc009mpk.1. mouse.

Organism-specific databases

CTDi 4125.
MGIi MGI:107286. Man2b1.

Phylogenomic databases

eggNOGi COG0383.
GeneTreei ENSGT00510000046304.
HOGENOMi HOG000007676.
HOVERGENi HBG052391.
InParanoidi Q3UGH3.
KOi K12311.
OMAi NMQLTVL.
OrthoDBi EOG786H2P.
TreeFami TF313840.

Miscellaneous databases

ChiTaRSi MAN2B1. mouse.
NextBioi 291430.
PROi O09159.
SOURCEi Search...

Gene expression databases

Bgeei O09159.
CleanExi MM_MAN2B1.
Genevestigatori O09159.

Family and domain databases

Gene3Di 1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProi IPR011013. 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.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view ]
Pfami PF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view ]
SMARTi SM00872. Alpha-mann_mid. 1 hit.
[Graphical view ]
SUPFAMi SSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMA2B1_MOUSE
AccessioniPrimary (citable) accession number: O09159
Secondary accession number(s): O55037
, Q3UGH3, Q64443, Q9DBQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 120 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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