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P0C7A1

- ENASE_CHICK

UniProt

P0C7A1 - ENASE_CHICK

Protein

Cytosolic endo-beta-N-acetylglucosaminidase

Gene

ENGASE

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    Functioni

    Endoglycosidase that releases N-glycans from glycoproteins by cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose core. Involved in the processing of free oligosaccharides in the cytosol.

    Catalytic activityi

    Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

    GO - Molecular functioni

    1. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
    Short name:
    ENGase
    Gene namesi
    Name:ENGASE
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 728728Cytosolic endo-beta-N-acetylglucosaminidasePRO_0000328869Add
    BLAST

    Proteomic databases

    PaxDbiP0C7A1.

    Interactioni

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000019265.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C7A1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini287 – 38195BRCTAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 85 family.Curated
    Contains 1 BRCT domain.Curated

    Phylogenomic databases

    eggNOGiCOG4724.
    HOGENOMiHOG000082678.
    HOVERGENiHBG107848.
    PhylomeDBiP0C7A1.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR005201. Glyco_hydro_85.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF03644. Glyco_hydro_85. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C7A1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSQSVMLEL REQDEVWVRL YKGERENAVF SDEYDTYITF SGHLINFQPA    50
    AEPLGTTVLH AAVDTRPQPA RYFDTGTTEP VSFFLSGLEE LLAWHPSSDD 100
    EFNVCAVPLA QRQPPLHSRR PRTLLCHDMR GGYLEDRFIQ GSATRNPYVF 150
    YHWRYVDIFV YFSHHTVTIP PVCWTNAAHR NGVPVLGTFI TEWADGEKLC 200
    EAFLAGGEDA YRAVSHQLAR IAQHYRFDGW LINIENALSA AAVGNLSPFL 250
    RHLTAEVHGA VPGGLVIWYD SILESGTLRW QNELNQQNRV FFDACDGLFV 300
    NYNWKEEHLE RTRELAGQRH ADVYIGVDVF ARGDVVGGGF DTNKSLSLIR 350
    KHGLSAAIFA PGWVYKHLGE ENFLLNEDKF WGLLEDYLPT HSICTLPLAT 400
    SFSVGMGTGM FLAGKEEEAG PWYNLSAQEI QPLYPERRGW LSTSCCLQDA 450
    WCGGSSLRVQ GTIPPGEERV AIRLSLWVDL GSSGFSLSIC GTLASGPHRD 500
    DFTVALELTT WHSSRCHDGT VTVLPSEDEP HGRHHPHLLP APPPALSRML 550
    AACSHGAQGW TSRCYEQELR GCSLRDLSLL VSRQQASPQE TSFSCLLGEL 600
    RVLDAGSMAA SPPQVQSLTA SQLWWQDGPS AEQLSLSLTL RWAFPPGRAA 650
    CFRVLSQGAR CHRAQPAQPQ LLGLAHGCQY RAVGLAVPRP APGQSCQLEL 700
    LVEPVLPSEL PVGPERWGRL LLVYSEPA 728
    Length:728
    Mass (Da):80,889
    Last modified:April 8, 2008 - v1
    Checksum:iCAA311512C095918
    GO

    Cross-referencesi

    3D structure databases

    ProteinModelPortali P0C7A1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000019265.

    Chemistry

    ChEMBLi CHEMBL1075083.

    Proteomic databases

    PaxDbi P0C7A1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4724.
    HOGENOMi HOG000082678.
    HOVERGENi HBG107848.
    PhylomeDBi P0C7A1.

    Miscellaneous databases

    PROi P0C7A1.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR005201. Glyco_hydro_85.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF03644. Glyco_hydro_85. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
      Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
      , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
      Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Red jungle fowl.
    2. "Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol."
      Suzuki T., Yano K., Sugimoto S., Kitajima K., Lennarz W.J., Inoue S., Inoue Y., Emori Y.
      Proc. Natl. Acad. Sci. U.S.A. 99:9691-9696(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-76, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiENASE_CHICK
    AccessioniPrimary (citable) accession number: P0C7A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 40 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, Direct protein sequencing, 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