GenomeNet

Database: UniProt
Entry: D4A6U0_RAT
LinkDB: D4A6U0_RAT
Original site: D4A6U0_RAT 
ID   D4A6U0_RAT              Unreviewed;       904 AA.
AC   D4A6U0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   23-MAY-2018, entry version 63.
DE   RecName: Full=Non-lysosomal glucosylceramidase {ECO:0000256|PIRNR:PIRNR028944};
DE            Short=NLGase {ECO:0000256|PIRNR:PIRNR028944};
DE            EC=3.2.1.45 {ECO:0000256|PIRNR:PIRNR028944};
GN   Name=Gba2 {ECO:0000313|EMBL:EDL98757.1,
GN   ECO:0000313|Ensembl:ENSRNOP00000059311, ECO:0000313|RGD:1305598};
GN   ORFNames=rCG_54897 {ECO:0000313|EMBL:EDL98757.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000059311, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000059311, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059311,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|EMBL:EDL98757.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL98757.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [3] {ECO:0000313|EMBL:EDL98757.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL98757.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
RA   Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
RA   Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSRNOP00000059311}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000059311};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the
CC       conversion of glucosylceramide to free glucose and ceramide.
CC       {ECO:0000256|PIRNR:PIRNR028944}.
CC   -!- CATALYTIC ACTIVITY: D-glucosyl-N-acylsphingosine + H(2)O = D-
CC       glucose + N-acylsphingosine. {ECO:0000256|PIRNR:PIRNR028944}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR028944}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028944}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR028944}. Golgi apparatus membrane
CC       {ECO:0000256|PIRNR:PIRNR028944}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR028944}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR028944}. Note=Not localized to lipid
CC       rafts. {ECO:0000256|PIRNR:PIRNR028944}.
CC   -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase
CC       family. {ECO:0000256|PIRNR:PIRNR028944}.
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DR   EMBL; AC121204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473962; EDL98757.1; -; Genomic_DNA.
DR   RefSeq; NP_001013109.2; NM_001013091.2.
DR   UniGene; Rn.146071; -.
DR   PeptideAtlas; D4A6U0; -.
DR   Ensembl; ENSRNOT00000066708; ENSRNOP00000059311; ENSRNOG00000016364.
DR   GeneID; 298399; -.
DR   KEGG; rno:298399; -.
DR   CTD; 57704; -.
DR   RGD; 1305598; Gba2.
DR   eggNOG; KOG2119; Eukaryota.
DR   eggNOG; COG4354; LUCA.
DR   GeneTree; ENSGT00390000010998; -.
DR   KO; K17108; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000016364; -.
DR   ExpressionAtlas; D4A6U0; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR014551; B_Glucosidase_GBA2-typ.
DR   InterPro; IPR006775; GH116_catalytic.
DR   InterPro; IPR024462; GH116_N.
DR   Pfam; PF04685; DUF608; 1.
DR   Pfam; PF12215; Glyco_hydr_116N; 1.
DR   PIRSF; PIRSF028944; Beta_gluc_GBA2; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR028944};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR028944};
KW   Golgi apparatus {ECO:0000256|PIRNR:PIRNR028944};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR028944};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR028944};
KW   Membrane {ECO:0000256|PIRNR:PIRNR028944};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:D4A6U0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN      142    446       Glyco_hydr_116N. {ECO:0000259|Pfam:
FT                                PF12215}.
FT   DOMAIN      512    877       DUF608. {ECO:0000259|Pfam:PF04685}.
SQ   SEQUENCE   904 AA;  101823 MW;  036D5A4212222901 CRC64;
     MVTCVPASEQ IGCAERDSQI YSEDTGGTEA VRVTDCRSPE DSGPQNEPGY CNSEDSGQLM
     ASYEGKARGY QVPPFGWRIC LAHEFAEKRK PFQANNVSLS NLVKHFGMGL RYLKWWYRKT
     QVEKKTPFID MFNSVPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ
     FIVCLRRDGR TVYQQVLSLE LPSVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT
     CRQITPILPH DYQDSSLPVG VFVWDVENEG DETLDVSIMF SMRNGLGGED DAAGGLWNEP
     FRLEQDGTTV QGLLLHHPTP PNPYTMAVAA RHTADTTVTY TTAFDPDSTG QQVWQDLLQD
     GQLDSPAGQS TPTQRGEGVA GAVCASSKLL PRGRCCLEFS LAWDMPRIMF GAKGQVHYRR
     YTRFFGSDGD VAPALSHYAL CQYAGWENSI SAWQNPVLDD RSLPAWYKSA LFNELYFLAD
     GGTVWLEVPE DSLPEELGGS MYQLRPILQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM
     LWPKLELSLQ YDMALATFKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY
     LIHDTADWKD LNLKFVLQVY RDYYLTGDQG FLKDMWPVCL AVMESEMKFD KDQDGLIENG
     GYADQTYDGW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQDKFSSIL CRGREAYERL
     LWNGRYYNYD SSSQPQSRSV MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALKTIFELN
     VQAFAGGAMG AVNGMQPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY
     RTVWERLGLA FQTPEAYCQQ RVFRSLAYMR PLSIWAMQLA LQQQQHKKNS SRPAVTQGTA
     PSTA
//
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