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Q5M868

- GBA2_RAT

UniProt

Q5M868 - GBA2_RAT

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Protein

Non-lysosomal glucosylceramidase

Gene
Gba2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide (GlcCer) to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O-glucosides, however, the relevance of such activity is unclear in vivo By similarity. Plays a role in central nevous system development By similarity. Required for proper formation of motor neuron axons By similarity.

Catalytic activityi

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

Enzyme regulationi

Enzymatic activity is dependent on membrane association and requires the presence of lipids By similarity.

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB
  2. glucosylceramidase activity Source: UniProtKB-EC

GO - Biological processi

  1. bile acid metabolic process Source: UniProtKB
  2. central nervous system neuron development Source: UniProtKB
  3. glucosylceramide catabolic process Source: InterPro
  4. glycoside catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_198596. Glycosphingolipid metabolism.

Protein family/group databases

CAZyiGH116. Glycoside Hydrolase Family 116.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-lysosomal glucosylceramidase (EC:3.2.1.45)
Short name:
NLGase
Alternative name(s):
Beta-glucocerebrosidase 2
Short name:
Beta-glucosidase 2
Glucosylceramidase 2
Gene namesi
Name:Gba2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1305598. Gba2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 912912Non-lysosomal glucosylceramidasePRO_0000283760Add
BLAST

Proteomic databases

PaxDbiQ5M868.
PRIDEiQ5M868.

Expressioni

Gene expression databases

GenevestigatoriQ5M868.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022002.

Structurei

3D structure databases

ProteinModelPortaliQ5M868.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4354.
HOGENOMiHOG000234168.
HOVERGENiHBG105975.
InParanoidiQ5M868.
PhylomeDBiQ5M868.
TreeFamiTF313888.

Family and domain databases

InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view]
PfamiPF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view]
PIRSFiPIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMiSSF48208. SSF48208. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5M868-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY    50
CNSEDSGQLM ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS 100
NLVKHFGMGL RYLKWWYRKT QVEKKTPFID MFNSVPLRQI YGCPLGGIGG 150
GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ FIVCLRRDGR TVYQQVLSLE 200
LPSVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT CRQITPILPH 250
DYQDSSLPVG VFVWDVENEG DETLDVSIMF SMRNGLGGED DAAGGLWNEP 300
FRLEQDGTTV QGLLLHHPTP PNPYTMAVAA RHTADTTVTY TTAFDPDSTG 350
QQVWQDLLQD GQLDSPAGQS TPTQRGEGVA GAVCASSKLL PRGRCCLEFS 400
LAWDMPRIMF GAKGQVHYRR YTRFFGSDGD VAPALSHYAL CQYAGWENSI 450
SAWQNPVLDD RSLPAWYKSA LFNELYFLAD GGTVWLEVPE DSLPEELGGS 500
MYQLRPILQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM LWPKLELSLQ 550
YDMALATFKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY 600
LIHDTADWKD LNLKFVLQVY RDYYLTGDQG FLKDMWPVCL AVMESEMKFD 650
KDQDGLIENG GYADQTYDGW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ 700
DVQDKFSSIL CRGREAYERL LWNGRYYNYD SSSQPQSRSV MSDQCAGQWF 750
LRACGLGEGD TEVFPTLHVV RALKTIFELN VQAFAGGAMG AVNGMQPHGV 800
PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY RTVWERLGLA 850
FQTPEAYCQQ RVFRSLAYMR PLSIWAMQLA LQQQQHKKNS SRPAVTQGTA 900
PSQPECGPKR SL 912
Length:912
Mass (Da):102,747
Last modified:April 3, 2007 - v2
Checksum:iC4A47C8C5F3D248A
GO
Isoform 2 (identifier: Q5M868-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-195: FIVCLRRDGRTVYQQ → VRKGAGRRRSDSWLA
     196-912: Missing.

Note: No experimental confirmation available.

Show »
Length:195
Mass (Da):21,993
Checksum:i15E7B9B8FA13E3A3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei181 – 19515FIVCL…TVYQQ → VRKGAGRRRSDSWLA in isoform 2. VSP_024385Add
BLAST
Alternative sequencei196 – 912717Missing in isoform 2. VSP_024386Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03040369 Genomic DNA. No translation available.
BC088200 mRNA. Translation: AAH88200.1.
UniGeneiRn.146071.

Genome annotation databases

UCSCiRGD:1305598. rat. [Q5M868-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03040369 Genomic DNA. No translation available.
BC088200 mRNA. Translation: AAH88200.1 .
UniGenei Rn.146071.

3D structure databases

ProteinModelPortali Q5M868.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000022002.

Protein family/group databases

CAZyi GH116. Glycoside Hydrolase Family 116.

Proteomic databases

PaxDbi Q5M868.
PRIDEi Q5M868.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1305598. rat. [Q5M868-1 ]

Organism-specific databases

RGDi 1305598. Gba2.

Phylogenomic databases

eggNOGi COG4354.
HOGENOMi HOG000234168.
HOVERGENi HBG105975.
InParanoidi Q5M868.
PhylomeDBi Q5M868.
TreeFami TF313888.

Enzyme and pathway databases

Reactomei REACT_198596. Glycosphingolipid metabolism.

Miscellaneous databases

PROi Q5M868.

Gene expression databases

Genevestigatori Q5M868.

Family and domain databases

InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR014551. Beta_glucosidase_GBA2-type.
IPR024462. GBA2_N.
IPR006775. Glucosylceramidase.
[Graphical view ]
Pfami PF04685. DUF608. 1 hit.
PF12215. GBA2_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAMi SSF48208. SSF48208. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    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 Norway.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Spleen.

Entry informationi

Entry nameiGBA2_RAT
AccessioniPrimary (citable) accession number: Q5M868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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