Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0C7A1 (ENASE_CHICK)

Last modified January 19, 2010. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

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 termDirect protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Inferred from electronic annotation. Source: 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
P0C7A1-1 [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., 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: 15592404] [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: 12114544] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-76, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

IPIIPI00587511.
UniGeneGga.39266

3D structure databases

SMRP0C7A1. Positions 1-45.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0C7A1.

Genome annotation databases

EnsemblENSGALT00000019290; ENSGALP00000019265; ENSGALG00000011816; Gallus gallus. [Genome view]

Phylogenomic databases

eggNOGveNOG04354.
HOGENOMHBG446184.

Enzyme and pathway databases

BRENDA3.2.1.96. 4.

Family and domain databases

InterProIPR001073. C1q.
IPR005201. Glyco_hydro_85.
IPR008983. Tumour_necrosis_fac-like.
[Graphical view]
Gene3DG3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit.
PANTHERPTHR13246. Glyco_hydro_85. 1 hit.
PfamPF00386. C1q. 1 hit.
PF03644. Glyco_hydro_85. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. False negative.
[Graphical view]
ProtoNetSearch...

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: January 19, 2010
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents