Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O09159

- MA2B1_MOUSE

UniProt

O09159 - MA2B1_MOUSE

Protein

Lysosomal alpha-mannosidase

Gene

Man2b1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 721ZincBy similarity
    Metal bindingi74 – 741ZincBy similarity
    Active sitei196 – 1961NucleophileBy similarity
    Metal bindingi196 – 1961ZincBy similarity
    Metal bindingi446 – 4461ZincBy 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

    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

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 495PGARA → LASG in AAC53369. (PubMed:9355733)Curated
    Sequence conflicti45 – 495PGARA → LASG in AAC78560. (PubMed:9799835)Curated
    Sequence conflicti344 – 3441V → A in AAC53369. (PubMed:9355733)Curated
    Sequence conflicti344 – 3441V → A in AAC78560. (PubMed:9799835)Curated
    Sequence conflicti344 – 3441V → A in AAH05430. (PubMed:15489334)Curated
    Sequence conflicti344 – 3441V → A in AAC09470. (PubMed:9305783)Curated
    Sequence conflicti980 – 9801Y → F in AAC53369. (PubMed:9355733)Curated
    Sequence conflicti980 – 9801Y → F in AAC78560. (PubMed:9799835)Curated
    Sequence conflicti980 – 9801Y → F in AAH05430. (PubMed:15489334)Curated
    Sequence conflicti980 – 9801Y → F in AAC09470. (PubMed:9305783)Curated

    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

    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: October 1, 2014
    This is version 121 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