Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucosylceramidase

Gene

Gba

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.UniRule annotation

GO - Molecular functioni

  • glucosylceramidase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolismUniRule annotation

Enzyme and pathway databases

ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH30. Glycoside Hydrolase Family 30.

Names & Taxonomyi

Protein namesi
Recommended name:
GlucosylceramidaseUniRule annotation (EC:3.2.1.45UniRule annotation)
Gene namesi
Name:GbaImported
ORF Names:rCG_62590Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1589149. Gba.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 515496GlucosylceramidaseSequence analysisPRO_5007639777Add
BLAST

Proteomic databases

PeptideAtlasiB2RYC9.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063935.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 445349Glyco_hydro_30InterPro annotationAdd
BLAST
Domaini448 – 51063Glyco_hydro_30CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 30 family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiKOG2566. Eukaryota.
COG5520. LUCA.
GeneTreeiENSGT00390000009464.
HOVERGENiHBG002285.
KOiK01201.
OMAiQPDQKFQ.
OrthoDBiEOG76DTRZ.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR033452. GH30_C.
IPR001139. Glyco_hydro_30.
IPR033453. Glyco_hydro_30_TIM-barrel.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11069. PTHR11069. 1 hit.
PfamiPF02055. Glyco_hydro_30. 1 hit.
PF17189. Glyco_hydro_30C. 1 hit.
[Graphical view]
PRINTSiPR00843. GLHYDRLASE30.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

B2RYC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARFIGLFL FQAISWAYGA QPCIPKSFGY SSVVCVCNAT YCDSLDPLTL
60 70 80 90 100
PALGTFSRYE STRSGRRMEL STGSIQANRT GTGLLLTLQP EEKFQKVKGF
110 120 130 140 150
GGAMTDATAL NILALSPPAQ KLLLKSYFSS EGIEYNIIRV PMASCDFSIR
160 170 180 190 200
IYTYADTPND FQLSNFSLPE EDTKLKIPLI HRALKMSPRP ISLFASPWTS
210 220 230 240 250
PTWLKTNGAV NGKGSLKGHP GDIYHEAWAN YFVKFLDAYA THNIKFWAVT
260 270 280 290 300
AENEPSAGLF TGYPFQCLGF TAEHQRDFIS HDLGPALANS SHDVKLLILD
310 320 330 340 350
DQRLLLPRWA QVVLSDPEAA KYVHGIAVHW YMDFLAPAKA TLGETHRLFP
360 370 380 390 400
NMMLFASEAC VGSKFWEQSV RLGSWDRGMQ YSHSIITNLL YHVTGWTDWN
410 420 430 440 450
LALNPEGGPN WVRNFVDSPI IVDIPKDTFY KQPMFYHLGH FSKFIPEGSQ
460 470 480 490 500
RVGLVASEKT DLETVALIRP DGSAVVVVLN RSSKDVPLTI SDPALGFMET
510
ISPGYSIHTY LWRRQ
Length:515
Mass (Da):57,492
Last modified:July 1, 2008 - v1
Checksum:iF5C7CCCC6C23C79B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072752 Genomic DNA. No translation available.
BC166732 mRNA. Translation: AAI66732.1.
CH473976 Genomic DNA. Translation: EDM00662.1.
RefSeqiNP_001121111.1. NM_001127639.1.
UniGeneiRn.162606.

Genome annotation databases

EnsembliENSRNOT00000074727; ENSRNOP00000063935; ENSRNOG00000049281.
GeneIDi684536.
KEGGirno:684536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072752 Genomic DNA. No translation available.
BC166732 mRNA. Translation: AAI66732.1.
CH473976 Genomic DNA. Translation: EDM00662.1.
RefSeqiNP_001121111.1. NM_001127639.1.
UniGeneiRn.162606.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063935.

Protein family/group databases

CAZyiGH30. Glycoside Hydrolase Family 30.

Proteomic databases

PeptideAtlasiB2RYC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074727; ENSRNOP00000063935; ENSRNOG00000049281.
GeneIDi684536.
KEGGirno:684536.

Organism-specific databases

CTDi2629.
RGDi1589149. Gba.

Phylogenomic databases

eggNOGiKOG2566. Eukaryota.
COG5520. LUCA.
GeneTreeiENSGT00390000009464.
HOVERGENiHBG002285.
KOiK01201.
OMAiQPDQKFQ.
OrthoDBiEOG76DTRZ.

Enzyme and pathway databases

ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR033452. GH30_C.
IPR001139. Glyco_hydro_30.
IPR033453. Glyco_hydro_30_TIM-barrel.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR11069. PTHR11069. 1 hit.
PfamiPF02055. Glyco_hydro_30. 1 hit.
PF17189. Glyco_hydro_30C. 1 hit.
[Graphical view]
PRINTSiPR00843. GLHYDRLASE30.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: ProstateImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2013) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiB2RYC9_RAT
AccessioniPrimary (citable) accession number: B2RYC9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: July 6, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.