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Q69ZF3

- GBA2_MOUSE

UniProt

Q69ZF3 - GBA2_MOUSE

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Protein

Non-lysosomal glucosylceramidase

Gene
Gba2, Kiaa1605
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein 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. Plays a role in central nevous system development By similarity. Required for proper formation of motor neuron axons By similarity.1 Publication

Catalytic activityi

D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.1 Publication

Enzyme regulationi

Enzymatic activity is dependent on membrane association and requires the presence of lipids.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. central nervous system neuron development Source: UniProtKB
  2. glucosylceramide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_199008. 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
Synonyms:Kiaa1605
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2654325. Gba2.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side
Note: Not localized to lipid rafts By similarity.1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice have a normal bile acid metabolism but males exhibit impaired fertility due to glucosylceramides accumulation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Non-lysosomal glucosylceramidasePRO_0000283759Add
BLAST

Proteomic databases

PaxDbiQ69ZF3.
PRIDEiQ69ZF3.

PTM databases

PhosphoSiteiQ69ZF3.

Expressioni

Tissue specificityi

Widely expressed at low level. Highly expressed in testis and brain.2 Publications

Gene expression databases

ArrayExpressiQ69ZF3.
BgeeiQ69ZF3.
CleanExiMM_GBA2.
GenevestigatoriQ69ZF3.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliQ69ZF3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4354.
GeneTreeiENSGT00390000010998.
HOGENOMiHOG000234168.
HOVERGENiHBG105975.
InParanoidiQ69ZF3.
KOiK17108.
OMAiYQLPGQN.
OrthoDBiEOG7ZGX2B.
PhylomeDBiQ69ZF3.
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. 2 hits.

Sequencei

Sequence statusi: Complete.

Q69ZF3-1 [UniParc]FASTAAdd to Basket

« Hide

MVTCVPASEQ VGCAERDSQV YCEDTGGTEA VRVTDCGSPE DSGPQDEPSY    50
CNSEDSGQLM ASYEGKARGY QVPPFGWRIC LAHEFAEKRR PFQANNISLS 100
NLVKHLGMGL RYLKWWYRKT HVEKKTPFID MLNSLPLRQI YGCPLGGIGG 150
GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ FIVCLRRDGR TVYQQVLSLE 200
LPNVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT CRQVTPILPH 250
DYQDSSLPVG VFVWDVENEG DETLDVSITF SMRNGLGGED DAAGSLWNEP 300
FRLEQGGTTV QGLLLHHPTP PNPYTMAVAA RCTADTTVTH TTAFDPNGTG 350
QQVWQDLLQD GQLDSPAGQS TPTQKGEGIA GAVCVSSKLL PRSRCCLEFS 400
LAWDMPKIMF GAKSQVHYRR YTRFFGSDGD VAPALSHYAL CHYADWEDRI 450
SAWQNPVLDD RTLPAWYKSA LFNELYFLAD GGTVWLEVPA DSLPEGLGGS 500
MRQLRSTLQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM LWPKLELSLQ 550
YDMALATLKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY 600
LIHDTADWKD LNLKFVLQIY RDYYLTGDQG FLEDMWPVCL AVMESEMKFD 650
KDQDGLIENG GYADQTYDAW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ 700
DVQERFASIL CRGREAYERL LWNGRYYNYD SSSHPQSRSI MSDQCAGQWF 750
LRACGLGEGD TEVFPTLHVV RALQTIFELN VQAFAGGAMG AVNGMHPHGV 800
PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY RTVWERLGLA 850
FQTPEAYCQQ QVFRSLAYMR PLSIWAMQLA LQQQQHKKSR RPSVTQGTGL 900
STQPECGPKR SLANLNSE 918
Length:918
Mass (Da):103,294
Last modified:April 3, 2007 - v2
Checksum:iEABE7B50B96B0B59
GO

Sequence cautioni

The sequence BAD32491.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851V → I in BAC40785. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK173213 mRNA. Translation: BAD32491.1. Different initiation.
AK089192 mRNA. Translation: BAC40785.1.
AL732626 Genomic DNA. Translation: CAM17042.1.
BC056935 mRNA. Translation: AAH56935.1.
CCDSiCCDS18103.1.
RefSeqiNP_766280.2. NM_172692.3.
UniGeneiMm.229444.

Genome annotation databases

EnsembliENSMUST00000030189; ENSMUSP00000030189; ENSMUSG00000028467.
GeneIDi230101.
KEGGimmu:230101.
UCSCiuc008sqi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK173213 mRNA. Translation: BAD32491.1 . Different initiation.
AK089192 mRNA. Translation: BAC40785.1 .
AL732626 Genomic DNA. Translation: CAM17042.1 .
BC056935 mRNA. Translation: AAH56935.1 .
CCDSi CCDS18103.1.
RefSeqi NP_766280.2. NM_172692.3.
UniGenei Mm.229444.

3D structure databases

ProteinModelPortali Q69ZF3.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q69ZF3.
ChEMBLi CHEMBL5614.

Protein family/group databases

CAZyi GH116. Glycoside Hydrolase Family 116.

PTM databases

PhosphoSitei Q69ZF3.

Proteomic databases

PaxDbi Q69ZF3.
PRIDEi Q69ZF3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030189 ; ENSMUSP00000030189 ; ENSMUSG00000028467 .
GeneIDi 230101.
KEGGi mmu:230101.
UCSCi uc008sqi.2. mouse.

Organism-specific databases

CTDi 57704.
MGIi MGI:2654325. Gba2.
Rougei Search...

Phylogenomic databases

eggNOGi COG4354.
GeneTreei ENSGT00390000010998.
HOGENOMi HOG000234168.
HOVERGENi HBG105975.
InParanoidi Q69ZF3.
KOi K17108.
OMAi YQLPGQN.
OrthoDBi EOG7ZGX2B.
PhylomeDBi Q69ZF3.
TreeFami TF313888.

Enzyme and pathway databases

Reactomei REACT_199008. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi 379792.
PROi Q69ZF3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q69ZF3.
Bgeei Q69ZF3.
CleanExi MM_GBA2.
Genevestigatori Q69ZF3.

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. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility."
    Yildiz Y., Matern H., Thompson B., Allegood J.C., Warren R.L., Ramirez D.M.O., Hammer R.E., Hamra F.K., Matern S., Russell D.W.
    J. Clin. Invest. 116:2985-2994(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "The non-lysosomal beta-glucosidase GBA2 is a non-integral membrane-associated protein at the endoplasmic reticulum (ER) and Golgi."
    Korschen H.G., Yildiz Y., Raju D.N., Schonauer S., Bonigk W., Jansen V., Kremmer E., Kaupp U.B., Wachten D.
    J. Biol. Chem. 288:3381-3393(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION.

Entry informationi

Entry nameiGBA2_MOUSE
AccessioniPrimary (citable) accession number: Q69ZF3
Secondary accession number(s): Q6PGM3, Q8BTN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 79 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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