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)

O46432

- MA2B1_FELCA

UniProt

O46432 - MA2B1_FELCA

Protein

Lysosomal alpha-mannosidase

Gene

MAN2B1

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    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 bindingi73 – 731ZincBy similarity
    Metal bindingi75 – 751ZincBy similarity
    Active sitei197 – 1971NucleophileBy similarity
    Metal bindingi197 – 1971ZincBy similarity
    Metal bindingi448 – 4481ZincBy similarity

    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
    Gene namesi
    Name:MAN2B1
    Synonyms:MANB
    OrganismiFelis catus (Cat) (Felis silvestris catus)
    Taxonomic identifieri9685 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
    ProteomesiUP000011712: Unplaced

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5050By similarityAdd
    BLAST
    Chaini51 – 1007957Lysosomal alpha-mannosidasePRO_0000012068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 360By similarity
    Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi269 ↔ 274By similarity
    Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi414 ↔ 474By similarity
    Disulfide bondi495 ↔ 503By similarity
    Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi643 – 6431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi649 – 6491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi764 – 7641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi927 – 9271N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Processed into 3 peptides of 72 kDa, 41 kDa and 12 kDa.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliO46432.
    SMRiO46432. Positions 52-342, 350-423, 433-582, 601-872, 883-1003.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG052391.
    KOiK12311.

    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.

    O46432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGADARPLGV RAGGGGRGAA RPGTSSRALP PPLPPLSFLL LLLAAPGARA     50
    AGYETCPMVH PDMLNVHLVA HTHDDVGWLK TVDQYFYGIH NDVQHAGVQY 100
    ILDSVISSLL VEPTRRFIYV EIAFFSRWWH QQTNATQEVV RDLVRQGRLE 150
    FANGGWVMND EAATHYGAII DQMTLGLRFL EDTFGKDGRP RVAWHIDPFG 200
    HSREQASLFA QMGFDGLFFG RLDYQDKRVR EENLGLEQVW RASASLKPPA 250
    ADLFTSVLPN IYNPPEKLCW DTLCADKPFV EDRRSPEYNA EELVNYFLQL 300
    ATAQGQHFRT NHTIMTMGSD FQYENANMWF RNLDRLIQLV NAQQQANGSR 350
    VNVLYSTPAC YLWELNKANL TWSVKQDDFF PYADGPHQFW SGYFSSRPAL 400
    KRYERLSYNF LQVCNQLEAL AGPAANVGPY GSGDSAPLNQ AMAVLQHHDA 450
    VSGTSKQHVA DDYARQLAAG WDPCEVLLSN ALARLSGSKE DFTYCRNLNV 500
    SVCPLSQTAK NFQVTIYNPL GRKIDWMVRL PVSKHGFVVR DPNGTVVPSD 550
    VVILPSSDGQ ELLFPASVPA LGFSIYSVSQ VPGQRPHAHK PQPRSQRPWS 600
    RVLAIQNEHI RARFDPDTGL LVEMENLDQN LLLPVRQAFY WYNASVGNNL 650
    STQVSGAYIF RPNQEKPLMV SHWAQTRLVK TPLVQEVHQN FSAWCSQVVR 700
    LYRGQRHLEL EWTVGPIPVG DGWGKEIISR FDTVLETKGL FYTDSNGREI 750
    LERRRDYRPT WKLNQTETVA GNYYPVNSRI YIRDGNMQLT VLTDRSQGGS 800
    SLRDGSMELM VHRRLLKDDG RGVGEALLED GLGRWVRGRH LVLLDKVRTA 850
    ATGHRLQAEK EVLTPQVVLA PGGGAPYHLK VAPRKQFSGL RRELPPSVHL 900
    LTLARWDQKT LLLRLEHQFA VGEDSGNLSS PVTLDLTDLF SAFTITYLQE 950
    TTLVANQLRA SASRLKWTPN TGPTPLPSPS RLDPATITLQ PMEIRTFLAS 1000
    VQWEEHG 1007
    Length:1,007
    Mass (Da):113,230
    Last modified:June 1, 1998 - v1
    Checksum:iC064A8168F5DC20A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF010191 mRNA. Translation: AAB97672.1.
    AF010192 Genomic DNA. Translation: AAB97733.1.
    PIRiT42219.
    RefSeqiNP_001009222.1. NM_001009222.1.

    Genome annotation databases

    GeneIDi493697.
    KEGGifca:493697.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF010191 mRNA. Translation: AAB97672.1 .
    AF010192 Genomic DNA. Translation: AAB97733.1 .
    PIRi T42219.
    RefSeqi NP_001009222.1. NM_001009222.1.

    3D structure databases

    ProteinModelPortali O46432.
    SMRi O46432. Positions 52-342, 350-423, 433-582, 601-872, 883-1003.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH38. Glycoside Hydrolase Family 38.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 493697.
    KEGGi fca:493697.

    Organism-specific databases

    CTDi 4125.

    Phylogenomic databases

    HOVERGENi HBG052391.
    KOi K12311.

    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 feline lysosomal alpha-mannosidase, determination of its cDNA sequence and identification of a mutation causing alpha-mannosidosis in Persian cats."
      Berg T., Tollersrud O.-K., Walkley S.U., Siegel D., Nilssen O.
      Biochem. J. 328:863-870(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE.

    Entry informationi

    Entry nameiMA2B1_FELCA
    AccessioniPrimary (citable) accession number: O46432
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3