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Q29451

- MA2B1_BOVIN

UniProt

Q29451 - MA2B1_BOVIN

Protein

Lysosomal alpha-mannosidase

Gene

MAN2B1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 4 (16 Oct 2013)
      Previous versions | rss
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    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi73 – 731Zinc
    Metal bindingi75 – 751Zinc
    Active sitei197 – 1971Nucleophile
    Metal bindingi197 – 1971Zinc
    Metal bindingi448 – 4481Zinc

    GO - Molecular functioni

    1. alpha-mannosidase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mannose metabolic process Source: InterPro

    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
    Cleaved into the following 5 chains:
    Gene namesi
    Name:MAN2B1
    Synonyms:MANB
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 7

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5050Add
    BLAST
    Chaini51 – 999949Lysosomal alpha-mannosidasePRO_0000012060Add
    BLAST
    Chaini51 – 347297Lysosomal alpha-mannosidase A peptidePRO_0000012061Add
    BLAST
    Chaini348 – 43184Lysosomal alpha-mannosidase B peptidePRO_0000012062Add
    BLAST
    Chaini432 – 590159Lysosomal alpha-mannosidase C peptidePRO_0000012063Add
    BLAST
    Propeptidei591 – 62131Sequence AnalysisPRO_0000012064Add
    BLAST
    Chaini622 – 871250Lysosomal alpha-mannosidase D peptidePRO_0000012065Add
    BLAST
    Chaini872 – 999128Lysosomal alpha-mannosidase E peptidePRO_0000012066Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 360
    Glycosylationi134 – 1341N-linked (GlcNAc...)
    Disulfide bondi269 ↔ 274
    Glycosylationi369 – 3691N-linked (GlcNAc...)
    Disulfide bondi414 ↔ 474
    Disulfide bondi495 ↔ 503
    Glycosylationi499 – 4991N-linked (GlcNAc...)
    Glycosylationi634 – 6341N-linked (GlcNAc...)
    Glycosylationi640 – 6401N-linked (GlcNAc...)
    Glycosylationi681 – 6811N-linked (GlcNAc...)
    Glycosylationi755 – 7551N-linked (GlcNAc...)
    Glycosylationi919 – 9191N-linked (GlcNAc...)

    Post-translational modificationi

    Processed into 5 peptides of 35/38 kDa (A), 11/13 kDa (B) and 22 kDa (C), 38 kDa (D) and 13/15 kDa (E). The A, B and C peptides are disulfide-linked into a 67 kDa complex.
    Heavily glycosylated. Some sugar chains are of the high-mannose type.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ29451.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000008193.

    Structurei

    Secondary structure

    1
    999
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 7010
    Beta strandi76 – 805
    Helixi82 – 876
    Turni91 – 933
    Helixi98 – 11114
    Beta strandi117 – 1193
    Helixi122 – 1309
    Helixi134 – 14512
    Beta strandi148 – 1536
    Beta strandi155 – 1573
    Beta strandi161 – 1633
    Helixi166 – 18419
    Helixi185 – 1884
    Beta strandi191 – 20010
    Helixi203 – 2119
    Beta strandi216 – 2205
    Helixi224 – 2329
    Beta strandi236 – 2416
    Beta strandi244 – 2463
    Turni248 – 2514
    Beta strandi252 – 2576
    Helixi290 – 30516
    Beta strandi308 – 31710
    Helixi326 – 34116
    Beta strandi351 – 3555
    Helixi358 – 36710
    Helixi392 – 3943
    Helixi398 – 42023
    Helixi436 – 4449
    Turni448 – 4525
    Helixi457 – 48630
    Helixi498 – 5003
    Helixi504 – 5085
    Beta strandi510 – 5189
    Beta strandi520 – 5223
    Beta strandi524 – 5329
    Beta strandi537 – 5404
    Beta strandi542 – 5443
    Beta strandi550 – 5534
    Turni555 – 5573
    Beta strandi560 – 5689
    Beta strandi572 – 5809
    Beta strandi595 – 5973
    Beta strandi599 – 6057
    Turni607 – 6093
    Beta strandi611 – 6177
    Beta strandi623 – 6253
    Beta strandi627 – 6359
    Beta strandi653 – 6575
    Beta strandi659 – 6613
    Beta strandi666 – 6716
    Beta strandi676 – 6838
    Beta strandi686 – 6927
    Beta strandi697 – 7059
    Beta strandi716 – 7238
    Beta strandi731 – 7366
    Beta strandi739 – 7457
    Beta strandi750 – 7523
    Helixi761 – 7633
    Beta strandi765 – 77410
    Beta strandi776 – 78611
    Beta strandi788 – 7903
    Beta strandi797 – 8059
    Beta strandi811 – 8133
    Helixi822 – 8254
    Beta strandi826 – 83712
    Helixi838 – 85316
    Beta strandi857 – 8626
    Beta strandi880 – 8834
    Beta strandi890 – 8989
    Beta strandi901 – 9077
    Turni912 – 9198
    Beta strandi924 – 9274
    Beta strandi929 – 94315
    Beta strandi947 – 9504
    Helixi951 – 9533
    Beta strandi978 – 9814
    Beta strandi986 – 9949

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O7DX-ray2.70A51-348[»]
    B349-432[»]
    C433-591[»]
    D592-873[»]
    E874-999[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ29451.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0383.
    GeneTreeiENSGT00510000046304.
    HOGENOMiHOG000007676.
    HOVERGENiHBG052391.
    InParanoidiQ29451.
    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.

    Q29451-1 [UniParc]FASTAAdd to Basket

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    MVGDARPSGV RAGGCRGAVG SRTSSRALRP PLPPLSSLFV LFLAAPCAWA    50
    AGYKTCPKVK PDMLNVHLVP HTHDDVGWLK TVDQYFYGIY NNIQPAGVQY 100
    ILDSVISSLL ANPTRRFIYV EIAFFSRWWR QQTNATQKIV RELVRQGRLE 150
    FANGGWVMND EATTHYGAII DQMTLGLRFL EETFGSDGRP RVAWHIDPFG 200
    HSREQASLFA QMGFDGFFFG RLDYQDKKVR KKTLQMEQVW RASTSLKPPT 250
    ADLFTSVLPN MYNPPEGLCW DMLCADKPVV EDTRSPEYNA KELVRYFLKL 300
    ATDQGKLYRT KHTVMTMGSD FQYENANTWF KNLDKLIQLV NAQQRANGIR 350
    VNVLYSTPAC YLWELNKANL SWSVKKDDFF PYADGPYMFW TGYFSSRPAL 400
    KRYERLSYNF LQVCNQLEAL AGPAANVGPY GSGDSAPLNE AMAVLQHHDA 450
    VSGTSRQHVA NDYARQLSEG WRPCEVLMSN ALAHLSGLKE DFAFCRKLNI 500
    SICPLTQTAE RFQVIVYNPL GRKVDWMVRL PVSKHVYLVK DPGGKIVPSD 550
    VVTIPSSDSQ ELLFSALVPA VGFSIYSVSQ MPNQRPQKSW SRDLVIQNEY 600
    LRARFDPNTG LLMELENLEQ NLLLPVRQAF YWYNASTGNN LSSQASGAYI 650
    FRPNQNKPLF VSHWAQTHLV KASLVQEVHQ NFSAWCSQVV RLYPRQRHLE 700
    LEWTVGPIPV GDGWGKEVIS RFDTALATRG LFYTDSNGRE ILERRRNYRP 750
    TWKLNQTEPV AGNYYPVNSR IYITDGNMQL TVLTDRSQGG SSLRDGSLEL 800
    MVHRRLLKDD ARGVGEPLNK EGSGLWVRGR HLVLLDKKET AAARHRLQAE 850
    MEVLAPQVVL AQGGGARYRL EKAPRTQFSG LRRELPPSVR LLTLARWGPE 900
    TLLLRLEHQF AVGEDSGRNL SSPVTLDLTN LFSAFTITNL RETTLAANQL 950
    LAYASRLQWT TDTGPTPHPS PSRPVSATIT LQPMEIRTFL ASVQWEEDG 999
    Length:999
    Mass (Da):112,919
    Last modified:October 16, 2013 - v4
    Checksum:iC86DE7532925DB10
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761G → R in AAB67726. (PubMed:9208932)Curated
    Sequence conflicti176 – 1761G → R in AAC48763. (PubMed:9208932)Curated
    Sequence conflicti512 – 55039Missing in AAC48763. (PubMed:9208932)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211R → H in AM; Galloway cattle. 1 Publication
    Natural varianti321 – 3211F → L in AM; Angus cattle. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31373 mRNA. Translation: AAB67726.2.
    U97694
    , U97686, U97687, U97688, U97689, U97690, U97691, U97692, U97693 Genomic DNA. Translation: AAC48763.1.
    DAAA02019388 Genomic DNA. No translation available.
    RefSeqiNP_776986.2. NM_174561.2.
    UniGeneiBt.4622.

    Genome annotation databases

    EnsembliENSBTAT00000008193; ENSBTAP00000008193; ENSBTAG00000006241.
    GeneIDi282272.
    KEGGibta:282272.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L31373 mRNA. Translation: AAB67726.2 .
    U97694
    , U97686 , U97687 , U97688 , U97689 , U97690 , U97691 , U97692 , U97693 Genomic DNA. Translation: AAC48763.1 .
    DAAA02019388 Genomic DNA. No translation available.
    RefSeqi NP_776986.2. NM_174561.2.
    UniGenei Bt.4622.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O7D X-ray 2.70 A 51-348 [» ]
    B 349-432 [» ]
    C 433-591 [» ]
    D 592-873 [» ]
    E 874-999 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000008193.

    Chemistry

    ChEMBLi CHEMBL1932902.

    Protein family/group databases

    CAZyi GH38. Glycoside Hydrolase Family 38.

    Proteomic databases

    PRIDEi Q29451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000008193 ; ENSBTAP00000008193 ; ENSBTAG00000006241 .
    GeneIDi 282272.
    KEGGi bta:282272.

    Organism-specific databases

    CTDi 4125.

    Phylogenomic databases

    eggNOGi COG0383.
    GeneTreei ENSGT00510000046304.
    HOGENOMi HOG000007676.
    HOVERGENi HBG052391.
    InParanoidi Q29451.
    KOi K12311.
    OMAi NMQLTVL.
    OrthoDBi EOG786H2P.
    TreeFami TF313840.

    Miscellaneous databases

    EvolutionaryTracei Q29451.
    NextBioi 20806083.

    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. "Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis."
      Tollersrud O.-K., Berg T., Healy P., Evjen G., Ramachandran U., Nilssen O.
      Eur. J. Biochem. 246:410-419(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS AM HIS-221 AND LEU-321.
      Tissue: Kidney.
    2. Berg T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 358.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Hereford.
    4. "The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation."
      Heikinheimo P., Helland R., Leiros H.-K.S., Leiros I., Karlsen S., Evjen G., Ravelli R., Schoehn G., Ruigrok R., Tollersrud O.-K., McSweeney S., Hough E.
      J. Mol. Biol. 327:631-644(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-999.

    Entry informationi

    Entry nameiMA2B1_BOVIN
    AccessioniPrimary (citable) accession number: Q29451
    Secondary accession number(s): F1MMX7, O02848, O19138
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: October 16, 2013
    Last modified: October 1, 2014
    This is version 99 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3