Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q8NFI3 (ENASE_HUMAN)

Last modified June 16, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length743 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Ref.1

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 By similarity.

Tissue specificity

Widely expressed. Expressed at higher level in thymus and spleen. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 85 family.

Contains 1 BRCT domain.

Sequence caution

The sequence AAH24213.2 differs from that shown. Reason: Frameshift at position 694.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionGlycosidase
Hydrolase
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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NFI3-1)

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.
Isoform 2 (identifier: Q8NFI3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     364-377: GWVYECLEKKDFFQ → SCSVFPGVGNLLCC
     378-743: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NFI3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     347-406: SLELIRKHGF...SLPFVTSFCL → VGGGFRPRAS...CPAPAKLCPH
     407-743: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 743743Cytosolic endo-beta-N-acetylglucosaminidase
PRO_0000328867

Regions

Domain291 – 38393BRCT

Natural variations

Alternative sequence347 – 40660SLELI…TSFCL → VGGGFRPRASGPVPPLGPHF LMDLPFPSAPQRNDSSCSSQ SGDPVALRNRCPAPAKLCPH in isoform 3.
VSP_032835
Alternative sequence364 – 37714GWVYE…KDFFQ → SCSVFPGVGNLLCC in isoform 2.
VSP_032836
Alternative sequence378 – 743366Missing in isoform 2.
VSP_032837
Alternative sequence407 – 743337Missing in isoform 3.
VSP_032838

Experimental info

Sequence conflict1521F → L in BAB15158. Ref.2
Sequence conflict2241T → A in CAH56405. Ref.4
Sequence conflict5961S → N in AAH24213. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 384DA533AE549FC5

FASTA74383,987
        10         20         30         40         50         60 
MEAAAVTVTR SATRRRRRQL QGLAAPEAGT QEEQEDQEPR PRRRRPGRSI KDEEEETVFR 

        70         80         90        100        110        120 
EVVSFSPDPL PVRYYDKDTT KPISFYLSSL EELLAWKPRL EDGFNVALEP LACRQPPLSS 

       130        140        150        160        170        180 
QRPRTLLCHD MMGGYLDDRF IQGSVVQTPY AFYHWQCIDV FVYFSHHTVT IPPVGWTNTA 

       190        200        210        220        230        240 
HRHGVCVLGT FITEWNEGGR LCEAFLAGDE RSYQAVADRL VQITQFFRFD GWLINIENSL 

       250        260        270        280        290        300 
SLAAVGNMPP FLRYLTTQLH RQVPGGLVLW YDSVVQSGQL KWQDELNQHN RVFFDSCDGF 

       310        320        330        340        350        360 
FTNYNWREEH LERMLGQAGE RRADVYVGVD VFARGNVVGG RFDTDKSLEL IRKHGFSVAL 

       370        380        390        400        410        420 
FAPGWVYECL EKKDFFQNQD KFWGRLERYL PTHSICSLPF VTSFCLGMGA RRVCYGQEEA 

       430        440        450        460        470        480 
VGPWYHLSAQ EIQPLFGEHR LGGDGRGWVR THCCLEDAWH GGSSLLVRGV IPPEVGNVAV 

       490        500        510        520        530        540 
RLFSLQAPVP PKIYLSMVYK LEGPTDVTVA LELTTGDAGS CHIGGISVLN AETSSRHSLR 

       550        560        570        580        590        600 
PLRVPPTKLA RWVGRCGRQL SGGWVQHCYE VSLRGCLLLD LLVCFSRPPG SREEESFTCR 

       610        620        630        640        650        660 
LGEIQVVDAA SLLAPLPQVQ AVTISHIRWQ PSASEREGPP ALLQLSCTLH WSFLLSQVRC 

       670        680        690        700        710        720 
FRIHCWGGMS DDSPGRELPR PEMPMFLGLA FATQYRIVDL LVEAAGPGQD RRMEFLVEPV 

       730        740 
PKEGFRVPQA EWGRAVLLYS APA 

« Hide

Isoform 2.

Checksum: A60D0AE20C2EDD79
Show »

FASTA37743,107
Isoform 3.

Checksum: 4EB91EC292C1A61A
Show »

FASTA40646,090

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hepatoma.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-680 (ISOFORM 3).
Tissue: Testis.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-743 (ISOFORM 1).
Tissue: Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF512564 mRNA. Translation: AAM80487.1.
AK025518 mRNA. Translation: BAB15158.1.
CH471099 Genomic DNA. Translation: EAW89562.1.
AL110283 mRNA. Translation: CAH56405.1.
BC024213 mRNA. Translation: AAH24213.2. Frameshift.
IPIIPI00168838.
IPI00874016.
IPI00889689.
RefSeqNP_001036038.1.
UniGeneHs.29288

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH85. Glycoside Hydrolase Family 85.

Proteomic databases

PeptideAtlasQ8NFI3.
PRIDEQ8NFI3.

Genome annotation databases

EnsemblENSG00000167280. Homo sapiens. [Contig view]
GeneID64772.
KEGGhsa:64772.

Organism-specific databases

GeneCardsGC17P074582.
HGNCHGNC:24622. ENGASE.
MIM611898. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ8NFI3.
HOVERGENQ8NFI3.
OMAQ8NFI3. SAQEIQP.

Enzyme and pathway databases

BRENDA3.2.1.96. 247.

Gene expression databases

ArrayExpressQ8NFI3.
BgeeQ8NFI3.

Family and domain databases

InterProIPR001357. BRCT.
IPR005201. Glyco_hydro_85.
[Graphical view]
PANTHERPTHR13246. Glyco_hydro_85. 1 hit.
PfamPF03644. Glyco_hydro_85. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio66783.
SOURCESearch...

Entry information

Entry nameENASE_HUMAN
AccessionPrimary (citable) accession number: Q8NFI3
Secondary accession number(s): Q659F0, Q8TB86, Q9H6U4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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