Q5M868 (GBA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Non-lysosomal glucosylceramidase
Short name=NLGase
EC=3.2.1.45

Alternative name(s):
Beta-glucocerebrosidase 2
Short name=Beta-glucosidase 2
Glucosylceramidase 2

Gene names

Name:

Gba2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	912 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide 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.
Catalytic activity	D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.
Subcellular location	Cell membrane; Single-pass membrane protein By similarity. Note: Not localized to lipid rafts By similarity.
Sequence similarities	Belongs to the non-lysosomal glucosylceramidase family.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bile acid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glucosylceramide catabolic process Inferred from electronic annotation. Source: InterPro glycoside catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to membrane Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-glucosidase activity Inferred from sequence or structural similarity. Source: UniProtKB glucosylceramidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5M868-1)

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: Q5M868-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 912	912	Non-lysosomal glucosylceramidase		PRO_0000283760
Regions
	Topological domain	1 – 678	678	Extracellular Potential
	Transmembrane	679 – 699	21	Helical; Potential
	Topological domain	700 – 912	213	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	181 – 195	15	FIVCL…TVYQQ → VRKGAGRRRSDSWLA in isoform 2.		VSP_024385
	Alternative sequence	196 – 912	717	Missing in isoform 2.		VSP_024386

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: C4A47C8C5F3D248A	FASTA	912	102,747
	10 20 30 40 50 60 MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY CNSEDSGQLM 70 80 90 100 110 120 ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS NLVKHFGMGL RYLKWWYRKT 130 140 150 160 170 180 QVEKKTPFID MFNSVPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ 190 200 210 220 230 240 FIVCLRRDGR TVYQQVLSLE LPSVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT 250 260 270 280 290 300 CRQITPILPH DYQDSSLPVG VFVWDVENEG DETLDVSIMF SMRNGLGGED DAAGGLWNEP 310 320 330 340 350 360 FRLEQDGTTV QGLLLHHPTP PNPYTMAVAA RHTADTTVTY TTAFDPDSTG QQVWQDLLQD 370 380 390 400 410 420 GQLDSPAGQS TPTQRGEGVA GAVCASSKLL PRGRCCLEFS LAWDMPRIMF GAKGQVHYRR 430 440 450 460 470 480 YTRFFGSDGD VAPALSHYAL CQYAGWENSI SAWQNPVLDD RSLPAWYKSA LFNELYFLAD 490 500 510 520 530 540 GGTVWLEVPE DSLPEELGGS MYQLRPILQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM 550 560 570 580 590 600 LWPKLELSLQ YDMALATFKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY 610 620 630 640 650 660 LIHDTADWKD LNLKFVLQVY RDYYLTGDQG FLKDMWPVCL AVMESEMKFD KDQDGLIENG 670 680 690 700 710 720 GYADQTYDGW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQDKFSSIL CRGREAYERL 730 740 750 760 770 780 LWNGRYYNYD SSSQPQSRSV MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALKTIFELN 790 800 810 820 830 840 VQAFAGGAMG AVNGMQPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY 850 860 870 880 890 900 RTVWERLGLA FQTPEAYCQQ RVFRSLAYMR PLSIWAMQLA LQQQQHKKNS SRPAVTQGTA 910 PSQPECGPKR SL
	Isoform 2 [UniParc]. Checksum: 15E7B9B8FA13E3A3	FASTA	195	21,993
	10 20 30 40 50 60 MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY CNSEDSGQLM 70 80 90 100 110 120 ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS NLVKHFGMGL RYLKWWYRKT 130 140 150 160 170 180 QVEKKTPFID MFNSVPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ 190 VRKGAGRRRS DSWLA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03040369 Genomic DNA. No translation available. BC088200 mRNA. Translation: AAH88200.1.
IPI	IPI00844835. IPI00896234.
UniGene	Rn.146071.
3D structure databases
ProteinModelPortal	Q5M868.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000022002.
Protein family/group databases
CAZy	GH116. Glycoside Hydrolase Family 116.
Proteomic databases
PaxDb	Q5M868.
PRIDE	Q5M868.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:1305598. rat.
Organism-specific databases
RGD	1305598. Gba2.
Phylogenomic databases
eggNOG	COG4354.
HOGENOM	HOG000234168.
HOVERGEN	HBG105975.
InParanoid	Q5M868.
OMA	YQLPGQN.
Gene expression databases
ArrayExpress	Q5M868.
Genevestigator	Q5M868.
Family and domain databases
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR014551. Beta_glucosidase_GBA2-type. IPR024462. GBA2_N. IPR006775. Glucosylceramidase. [Graphical view]
Pfam	PF04685. DUF608. 1 hit. PF12215. GBA2_N. 1 hit. [Graphical view]
PIRSF	PIRSF028944. Beta_gluc_GBA2. 1 hit.
SUPFAM	SSF48208. Glyco_trans_6hp. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GBA2_RAT

Accession

Primary (citable) accession number: Q5M868

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	April 3, 2007
Last modified:	April 3, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program