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Q8BRK9

- MA2A2_MOUSE

UniProt

Q8BRK9 - MA2A2_MOUSE

Protein

Alpha-mannosidase 2x

Gene

Man2a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway By similarity.By similarity

    Catalytic activityi

    Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi175 – 1751ZincBy similarity
    Metal bindingi177 – 1771ZincBy similarity
    Active sitei289 – 2891NucleophileBy similarity
    Metal bindingi289 – 2891ZincBy similarity
    Metal bindingi569 – 5691ZincBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. hydrolase activity, hydrolyzing N-glycosyl compounds Source: MGI
    3. mannosidase activity Source: MGI
    4. mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Source: UniProtKB-EC
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mannose metabolic process Source: InterPro
    2. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198568. Reactions specific to the complex N-glycan synthesis pathway.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH38. Glycoside Hydrolase Family 38.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-mannosidase 2x (EC:3.2.1.114)
    Alternative name(s):
    Alpha-mannosidase IIx
    Short name:
    Man IIx
    Mannosidase alpha class 2A member 2
    Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
    Gene namesi
    Name:Man2a2
    Synonyms:Mana2x
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:2150656. Man2a2.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11521152Alpha-mannosidase 2xPRO_0000412634Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8BRK9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BRK9.
    BgeeiQ8BRK9.
    GenevestigatoriQ8BRK9.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000095949.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BRK9.
    SMRiQ8BRK9. Positions 762-1014.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 55CytoplasmicSequence Analysis
    Topological domaini27 – 796770LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili43 – 7432Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 38 family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00510000046304.
    HOVERGENiHBG052390.
    InParanoidiQ3UVK1.
    KOiK01231.
    OMAiYLEPMEI.
    OrthoDBiEOG7JQBMJ.
    PhylomeDBiQ8BRK9.
    TreeFamiTF313152.

    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BRK9-1) [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

    MKLKKQVTVC GAAIFCVAVF SLYLMLDRVQ HDPARHQNGG NFPRSQISVL     50
    QNRIEQLEQL LEENHDIISR IKDSVLELTA NAEGPPALLP YHTANGSWAV 100
    LPEPRPSFFS VSPQDCQFAL GGRGQKPELQ MLTVSEDLPF DNVEGGVWRQ 150
    GFDISYSPND WDTEDLQVFV VPHSHNDPGW IKTFDKYYTE QTQHILNSMV 200
    SKLQEDPRRR FLWAEVSFFA KWWDNISAQK RAAVRRLVGN GQLEIATGGW 250
    VMPDEANSHY FALVDQLIEG HQWLERNLGA TPRSGWAVDP FGHSSTMPYL 300
    LRRANLTSML IQRVHYAIKK HFAATHSLEF MWRQMWDSDS STDIFCHMMP 350
    FYSYDVPHTC GPDPKICCQF DFKRLPGGRI NCPWKVPPRA ITEANVADRA 400
    ALLLDQYRKK SRLFRSNVLL VPLGDDFRYD KPQEWDAQFF NYQRLFDFLN 450
    SKPEFHVQAQ FGTLSEYFDA LYKRTGVEPG ARPPGFPVLS GDFFSYADRE 500
    DHYWTGYYTS RPFYKSLDRV LEAHLRGAEI LYSLALAHAR RSGLAGQYPL 550
    SDFALLTEAR RTLGLFQHHD AITGTAKEAV VVDYGVRLLR SLVSLKQVII 600
    NAAHYLVLGD QETYSFDPGT PFLQMDDSRV SHDALPERTV IRLDSSPRFV 650
    VVFNPLEQER LSVVSLLVNS PRVRVLSEEG QPLSVQISVH WSSATDMVPD 700
    VYQVSVPVRL PGLGLGVLQL QPDLDGPYTL QSSVRVYLNG VKLSVSRQSA 750
    FPVRVVDSGA SDFAISNRYM QVWFSGLTGL LKSIRRVDEE QEQQMELEFL 800
    VYGTRTSKDK SGAYLFLPDS EAKPYVPKKP PVLRVTEGPF FSEVAVYYEH 850
    FHQVIRLYNL PGVEGLSLDM SFQVDIRDYV NKELALRIHT DIDSQGTFFT 900
    DLNGFQIQPR QYLKKLPLQA NFYPMPVMAY IQDSQRRLTL HTAQALGVSS 950
    LGNGQLEVIL DRRLMQDDNR GLGQGLKDNK ITCNRFRLLL ERRTTMSPEV 1000
    HQEQERSTSY PSLLSHLTSM YLSTPPLVLP VAKRQGTSPA LRSFHPLASP 1050
    LPCDFHLLNL RMLPAEDTLP ATDSALILHR KGFDCGLEAK NLGFNCTTSQ 1100
    GKLALGSLFH GLDVTFLQPT SLTLLYPLAS PSNSTDISLE PMEISTFRLR 1150
    LG 1152
    Length:1,152
    Mass (Da):130,649
    Last modified:September 21, 2011 - v2
    Checksum:i8A6274E9671F92DF
    GO
    Isoform 2 (identifier: Q8BRK9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         783-827: SIRRVDEEQE...PDSEAKPYVP → VKGQARGGGE...PDSQRFGCEH
         828-1152: Missing.

    Show »
    Length:827
    Mass (Da):93,450
    Checksum:i31A7AC9C5FC4CF2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971S → T in AK029913. (PubMed:16141072)Curated
    Sequence conflicti1111 – 11111G → S in BAE23268. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei783 – 82745SIRRV…KPYVP → VKGQARGGGEGPEEGMGVRG LVDSCSCSHVPSCLSPDSQR FGCEH in isoform 2. 1 PublicationVSP_041735Add
    BLAST
    Alternative sequencei828 – 1152325Missing in isoform 2. 1 PublicationVSP_041736Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029913 mRNA. No translation available.
    AK044028 mRNA. Translation: BAC31745.1.
    AK137205 mRNA. Translation: BAE23268.1.
    AC136740 Genomic DNA. No translation available.
    CCDSiCCDS57556.1. [Q8BRK9-1]
    RefSeqiNP_766491.2. NM_172903.4. [Q8BRK9-1]
    XP_006540661.1. XM_006540598.1. [Q8BRK9-1]
    XP_006540662.1. XM_006540599.1. [Q8BRK9-1]
    UniGeneiMm.269245.

    Genome annotation databases

    EnsembliENSMUST00000098346; ENSMUSP00000095949; ENSMUSG00000038886. [Q8BRK9-1]
    GeneIDi140481.
    KEGGimmu:140481.
    UCSCiuc009iap.2. mouse. [Q8BRK9-1]
    uc009iar.2. mouse. [Q8BRK9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029913 mRNA. No translation available.
    AK044028 mRNA. Translation: BAC31745.1 .
    AK137205 mRNA. Translation: BAE23268.1 .
    AC136740 Genomic DNA. No translation available.
    CCDSi CCDS57556.1. [Q8BRK9-1 ]
    RefSeqi NP_766491.2. NM_172903.4. [Q8BRK9-1 ]
    XP_006540661.1. XM_006540598.1. [Q8BRK9-1 ]
    XP_006540662.1. XM_006540599.1. [Q8BRK9-1 ]
    UniGenei Mm.269245.

    3D structure databases

    ProteinModelPortali Q8BRK9.
    SMRi Q8BRK9. Positions 762-1014.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000095949.

    Protein family/group databases

    CAZyi GH38. Glycoside Hydrolase Family 38.

    Proteomic databases

    PRIDEi Q8BRK9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098346 ; ENSMUSP00000095949 ; ENSMUSG00000038886 . [Q8BRK9-1 ]
    GeneIDi 140481.
    KEGGi mmu:140481.
    UCSCi uc009iap.2. mouse. [Q8BRK9-1 ]
    uc009iar.2. mouse. [Q8BRK9-2 ]

    Organism-specific databases

    CTDi 4122.
    MGIi MGI:2150656. Man2a2.

    Phylogenomic databases

    GeneTreei ENSGT00510000046304.
    HOVERGENi HBG052390.
    InParanoidi Q3UVK1.
    KOi K01231.
    OMAi YLEPMEI.
    OrthoDBi EOG7JQBMJ.
    PhylomeDBi Q8BRK9.
    TreeFami TF313152.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_198568. Reactions specific to the complex N-glycan synthesis pathway.

    Miscellaneous databases

    ChiTaRSi MAN2A2. mouse.
    NextBioi 369778.
    PROi Q8BRK9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BRK9.
    Bgeei Q8BRK9.
    Genevestigatori Q8BRK9.

    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. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Brain cortex, Testis and Urinary bladder.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.

    Entry informationi

    Entry nameiMA2A2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BRK9
    Secondary accession number(s): Q3UVK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3