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)

P33908

- MA1A1_HUMAN

UniProt

P33908 - MA1A1_HUMAN

Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA

Gene

MAN1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (26 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.

    Catalytic activityi

    Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

    Cofactori

    Calcium.

    Enzyme regulationi

    Inhibited by both 1-deoxymannojirimycin and kifunensine.

    Pathwayi

    GO - Molecular functioni

    1. calcium ion binding Source: ProtInc
    2. mannosidase activity Source: ProtInc
    3. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. post-translational protein modification Source: Reactome
    3. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA (EC:3.2.1.113)
    Alternative name(s):
    Man(9)-alpha-mannosidase
    Short name:
    Man9-mannosidase
    Mannosidase alpha class 1A member 1
    Processing alpha-1,2-mannosidase IA
    Short name:
    Alpha-1,2-mannosidase IA
    Gene namesi
    Name:MAN1A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6821. MAN1A1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi membrane Source: Reactome
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30570.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 653653Mannosyl-oligosaccharide 1,2-alpha-mannosidase IAPRO_0000210308Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi476 ↔ 508By similarity
    Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP33908.
    PaxDbiP33908.
    PRIDEiP33908.

    PTM databases

    PhosphoSiteiP33908.

    Expressioni

    Gene expression databases

    ArrayExpressiP33908.
    BgeeiP33908.
    CleanExiHS_MAN1A1.
    GenevestigatoriP33908.

    Organism-specific databases

    HPAiCAB037058.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000357453.

    Structurei

    3D structure databases

    ProteinModelPortaliP33908.
    SMRiP33908. Positions 176-641.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4141CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini63 – 653591LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei42 – 6221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181988.
    HOVERGENiHBG052389.
    KOiK01230.
    OMAiMAQHYLE.
    OrthoDBiEOG7X0VH1.
    PhylomeDBiP33908.
    TreeFamiTF313420.

    Family and domain databases

    Gene3Di1.50.10.50. 1 hit.
    InterProiIPR001382. Glyco_hydro_47.
    [Graphical view]
    PANTHERiPTHR11742. PTHR11742. 1 hit.
    PfamiPF01532. Glyco_hydro_47. 1 hit.
    [Graphical view]
    PRINTSiPR00747. GLYHDRLASE47.
    SUPFAMiSSF48225. SSF48225. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P33908-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPVGGLLPLF SSPAGGVLGG GLGGGGGRKG SGPAALRLTE KFVLLLVFSA    50
    FITLCFGAIF FLPDSSKLLS GVLFHSSPAL QPAADHKPGP GARAEDAAEG 100
    RARRREEGAP GDPEAALEDN LARIRENHER ALREAKETLQ KLPEEIQRDI 150
    LLEKKKVAQD QLRDKAPFRG LPPVDFVPPI GVESREPADA AIREKRAKIK 200
    EMMKHAWNNY KGYAWGLNEL KPISKGGHSS SLFGNIKGAT IVDALDTLFI 250
    MEMKHEFEEA KSWVEENLDF NVNAEISVFE VNIRFVGGLL SAYYLSGEEI 300
    FRKKAVELGV KLLPAFHTPS GIPWALLNMK SGIGRNWPWA SGGSSILAEF 350
    GTLHLEFMHL SHLSGNPIFA EKVMNIRTVL NKLEKPQGLY PNYLNPSSGQ 400
    WGQHHVSVGG LGDSFYEYLL KAWLMSDKTD LEAKKMYFDA VQAIETHLIR 450
    KSSSGLTYIA EWKGGLLEHK MGHLTCFAGG MFALGADAAP EGMAQHYLEL 500
    GAEIARTCHE SYNRTFMKLG PEAFRFDGGV EAIATRQNEK YYILRPEVME 550
    TYMYMWRLTH DPKYRKWAWE AVEALENHCR VNGGYSGLRD VYLLHESYDD 600
    VQQSFFLAET LKYLYLIFSD DDLLPLEHWI FNSEAHLLPI LPKDKKEVEI 650
    REE 653
    Length:653
    Mass (Da):72,969
    Last modified:April 26, 2005 - v3
    Checksum:i9B164926636D8554
    GO
    Isoform 2 (identifier: P33908-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         201-201: E → EEIEARKGQANCPGSSSSCEVEIQ
         331-344: SGIGRNWPWASGGS → RWMCNIPRAMEATI
         345-653: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:367
    Mass (Da):40,037
    Checksum:i3A5E1D30321CAFF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 4719KGSGP…VLLLV → MNSNFITFDLKMSLLPSNL in CAA52831. (PubMed:8223597)CuratedAdd
    BLAST
    Sequence conflicti464 – 4641G → R in CAA52831. (PubMed:8223597)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti651 – 6511R → G.
    Corresponds to variant rs35544784 [ dbSNP | Ensembl ].
    VAR_034102

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei201 – 2011E → EEIEARKGQANCPGSSSSCE VEIQ in isoform 2. 1 PublicationVSP_056372
    Alternative sequencei331 – 34414SGIGR…ASGGS → RWMCNIPRAMEATI in isoform 2. 1 PublicationVSP_056373Add
    BLAST
    Alternative sequencei345 – 653309Missing in isoform 2. 1 PublicationVSP_056374Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL022722, AL078600 Genomic DNA. Translation: CAI20315.1.
    AL078600 Genomic DNA. Translation: CAB75695.2.
    AL138886 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48185.1.
    BC065827 mRNA. Translation: AAH65827.1.
    X74837 mRNA. Translation: CAA52831.1.
    CCDSiCCDS5122.1.
    PIRiS38965.
    RefSeqiNP_005898.2. NM_005907.3.
    UniGeneiHs.102788.
    Hs.742378.

    Genome annotation databases

    EnsembliENST00000368466; ENSP00000357451; ENSG00000111885.
    ENST00000368468; ENSP00000357453; ENSG00000111885.
    GeneIDi4121.
    KEGGihsa:4121.
    UCSCiuc003pym.2. human.

    Polymorphism databases

    DMDMi62906886.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL022722 , AL078600 Genomic DNA. Translation: CAI20315.1 .
    AL078600 Genomic DNA. Translation: CAB75695.2 .
    AL138886 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48185.1 .
    BC065827 mRNA. Translation: AAH65827.1 .
    X74837 mRNA. Translation: CAA52831.1 .
    CCDSi CCDS5122.1.
    PIRi S38965.
    RefSeqi NP_005898.2. NM_005907.3.
    UniGenei Hs.102788.
    Hs.742378.

    3D structure databases

    ProteinModelPortali P33908.
    SMRi P33908. Positions 176-641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000357453.

    Chemistry

    ChEMBLi CHEMBL5915.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    PTM databases

    PhosphoSitei P33908.

    Polymorphism databases

    DMDMi 62906886.

    Proteomic databases

    MaxQBi P33908.
    PaxDbi P33908.
    PRIDEi P33908.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368466 ; ENSP00000357451 ; ENSG00000111885 .
    ENST00000368468 ; ENSP00000357453 ; ENSG00000111885 .
    GeneIDi 4121.
    KEGGi hsa:4121.
    UCSCi uc003pym.2. human.

    Organism-specific databases

    CTDi 4121.
    GeneCardsi GC06M119540.
    HGNCi HGNC:6821. MAN1A1.
    HPAi CAB037058.
    MIMi 604344. gene.
    neXtProti NX_P33908.
    PharmGKBi PA30570.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181988.
    HOVERGENi HBG052389.
    KOi K01230.
    OMAi MAQHYLE.
    OrthoDBi EOG7X0VH1.
    PhylomeDBi P33908.
    TreeFami TF313420.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_25396. Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.

    Miscellaneous databases

    GeneWikii MAN1A1.
    GenomeRNAii 4121.
    NextBioi 16180.
    PROi P33908.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33908.
    Bgeei P33908.
    CleanExi HS_MAN1A1.
    Genevestigatori P33908.

    Family and domain databases

    Gene3Di 1.50.10.50. 1 hit.
    InterProi IPR001382. Glyco_hydro_47.
    [Graphical view ]
    PANTHERi PTHR11742. PTHR11742. 1 hit.
    Pfami PF01532. Glyco_hydro_47. 1 hit.
    [Graphical view ]
    PRINTSi PR00747. GLYHDRLASE47.
    SUPFAMi SSF48225. SSF48225. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORM 2).
      Tissue: Testis.
    4. "Molecular cloning and primary structure of Man9-mannosidase from human kidney."
      Bause E., Bieberich E., Rolfs A., Voelker C., Schmidt B.
      Eur. J. Biochem. 217:535-540(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-653 (ISOFORM 1).
      Tissue: Kidney.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMA1A1_HUMAN
    AccessioniPrimary (citable) accession number: P33908
    Secondary accession number(s): E7EU32
    , Q6P052, Q9NU44, Q9UJI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3