Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C7A1 (ENASE_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic endo-beta-N-acetylglucosaminidase

Short name=ENGase
EC=3.2.1.96
Gene names
Name:ENGASE
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Subcellular location

Cytoplasmcytosol Probable Ref.2.

Sequence similarities

Belongs to the glycosyl hydrolase 85 family.

Contains 1 BRCT domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Cytosolic endo-beta-N-acetylglucosaminidase
PRO_0000328869

Regions

Domain287 – 38195BRCT

Sequences

Sequence LengthMass (Da)Tools
P0C7A1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: CAA311512C095918

FASTA72880,889
        10         20         30         40         50         60 
MQSQSVMLEL REQDEVWVRL YKGERENAVF SDEYDTYITF SGHLINFQPA AEPLGTTVLH 

        70         80         90        100        110        120 
AAVDTRPQPA RYFDTGTTEP VSFFLSGLEE LLAWHPSSDD EFNVCAVPLA QRQPPLHSRR 

       130        140        150        160        170        180 
PRTLLCHDMR GGYLEDRFIQ GSATRNPYVF YHWRYVDIFV YFSHHTVTIP PVCWTNAAHR 

       190        200        210        220        230        240 
NGVPVLGTFI TEWADGEKLC EAFLAGGEDA YRAVSHQLAR IAQHYRFDGW LINIENALSA 

       250        260        270        280        290        300 
AAVGNLSPFL RHLTAEVHGA VPGGLVIWYD SILESGTLRW QNELNQQNRV FFDACDGLFV 

       310        320        330        340        350        360 
NYNWKEEHLE RTRELAGQRH ADVYIGVDVF ARGDVVGGGF DTNKSLSLIR KHGLSAAIFA 

       370        380        390        400        410        420 
PGWVYKHLGE ENFLLNEDKF WGLLEDYLPT HSICTLPLAT SFSVGMGTGM FLAGKEEEAG 

       430        440        450        460        470        480 
PWYNLSAQEI QPLYPERRGW LSTSCCLQDA WCGGSSLRVQ GTIPPGEERV AIRLSLWVDL 

       490        500        510        520        530        540 
GSSGFSLSIC GTLASGPHRD DFTVALELTT WHSSRCHDGT VTVLPSEDEP HGRHHPHLLP 

       550        560        570        580        590        600 
APPPALSRML AACSHGAQGW TSRCYEQELR GCSLRDLSLL VSRQQASPQE TSFSCLLGEL 

       610        620        630        640        650        660 
RVLDAGSMAA SPPQVQSLTA SQLWWQDGPS AEQLSLSLTL RWAFPPGRAA CFRVLSQGAR 

       670        680        690        700        710        720 
CHRAQPAQPQ LLGLAHGCQY RAVGLAVPRP APGQSCQLEL LVEPVLPSEL PVGPERWGRL 


LLVYSEPA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

3D structure databases

ProteinModelPortalP0C7A1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000019265.

Chemistry

ChEMBLCHEMBL1075083.

Proteomic databases

PaxDbP0C7A1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4724.
HOGENOMHOG000082678.
HOVERGENHBG107848.
PhylomeDBP0C7A1.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR001073. C1q.
IPR005201. Glyco_hydro_85.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00386. C1q. 1 hit.
PF03644. Glyco_hydro_85. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0C7A1.

Entry information

Entry nameENASE_CHICK
AccessionPrimary (citable) accession number: P0C7A1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries