ID NCER3_ARATH Reviewed; 733 AA. AC F4KHQ8; Q93ZI6; Q9FIL4; DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 25-OCT-2017, entry version 47. DE RecName: Full=Neutral ceramidase 3 {ECO:0000303|PubMed:26150824}; DE Short=AtNCER3 {ECO:0000303|PubMed:26150824}; DE Short=N-CDase 3 {ECO:0000303|PubMed:26150824}; DE Short=NCDase 3 {ECO:0000303|PubMed:26150824}; DE EC=3.5.1.23 {ECO:0000250|UniProtKB:O06769}; DE AltName: Full=Acylsphingosine deacylase 3; DE AltName: Full=N-acylsphingosine amidohydrolase 3; DE Flags: Precursor; GN Name=NCER3 {ECO:0000303|PubMed:26150824}; GN OrderedLocusNames=At5g58980 {ECO:0000312|Araport:AT5G58980}; GN ORFNames=K19M22.17 {ECO:0000312|EMBL:BAB09641.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10048488; DOI=10.1093/dnares/5.6.379; RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. RT Sequence features of the regions of 1,081,958 bp covered by seventeen RT physically assigned P1 and TAC clones."; RL DNA Res. 5:379-391(1998). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE. RC STRAIN=cv. Columbia; RX PubMed=26150824; DOI=10.3389/fpls.2015.00460; RA Li J., Bi F.-C., Yin J., Wu J.-X., Rong C., Wu J.-L., Yao N.; RT "An Arabidopsis neutral ceramidase mutant ncer1 accumulates RT hydroxyceramides and is sensitive to oxidative stress."; RL Front. Plant Sci. 6:460-460(2015). CC -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine CC and free fatty acid (By similarity). Promotes oxidative stress CC resistance (PubMed:26150824). {ECO:0000250|UniProtKB:F4HQM3, CC ECO:0000269|PubMed:26150824}. CC -!- CATALYTIC ACTIVITY: N-acylsphingosine + H(2)O = a carboxylate + CC sphingosine. {ECO:0000250|UniProtKB:O06769}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VA70}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:F4HQM3}. Golgi CC apparatus {ECO:0000250|UniProtKB:Q0JL46}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=F4KHQ8-1; Sequence=Displayed; CC Name=2; CC IsoId=F4KHQ8-2; Sequence=VSP_058913; CC Note=No experimental confirmation available. CC {ECO:0000312|EMBL:AAL09747.1}; CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to C2-ceramide induced CC cell death. {ECO:0000269|PubMed:26150824}. CC -!- SIMILARITY: Belongs to the neutral ceramidase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB09641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016885; BAB09641.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002688; AED97126.1; -; Genomic_DNA. DR EMBL; AY057506; AAL09747.1; -; mRNA. DR RefSeq; NP_200706.1; NM_125288.4. [F4KHQ8-1] DR UniGene; At.29250; -. DR ProteinModelPortal; F4KHQ8; -. DR STRING; 3702.AT5G58980.1; -. DR PaxDb; F4KHQ8; -. DR PRIDE; F4KHQ8; -. DR EnsemblPlants; AT5G58980.1; AT5G58980.1; AT5G58980. [F4KHQ8-1] DR GeneID; 836015; -. DR Gramene; AT5G58980.1; AT5G58980.1; AT5G58980. DR KEGG; ath:AT5G58980; -. DR Araport; AT5G58980; -. DR TAIR; locus:2154598; AT5G58980. DR eggNOG; KOG2232; Eukaryota. DR eggNOG; ENOG410XQWE; LUCA. DR HOGENOM; HOG000209915; -. DR InParanoid; F4KHQ8; -. DR KO; K12349; -. DR OMA; STATIEW; -. DR OrthoDB; EOG093603YK; -. DR BioCyc; ARA:AT5G58980-MONOMER; -. DR Reactome; R-ATH-1660662; Glycosphingolipid metabolism. DR PRO; PR:F4KHQ8; -. DR Proteomes; UP000006548; Chromosome 5. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0017040; F:ceramidase activity; IEA:UniProtKB-EC. DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB. DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR006823; Ceramidase_alk. DR InterPro; IPR031331; NEUT/ALK_ceramidase_C. DR InterPro; IPR031329; NEUT/ALK_ceramidase_N. DR PANTHER; PTHR12670; PTHR12670; 1. DR Pfam; PF04734; Ceramidase_alk; 1. DR Pfam; PF17048; Ceramidse_alk_C; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Glycoprotein; Golgi apparatus; Hydrolase; Lipid metabolism; KW Reference proteome; Secreted; Signal; Sphingolipid metabolism. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 733 Neutral ceramidase 3. FT /FTId=PRO_5003311651. FT ACT_SITE 307 307 Nucleophile. FT {ECO:0000250|UniProtKB:Q9NR71}. FT CARBOHYD 325 325 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT VAR_SEQ 1 432 MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGP FT AADVNMMGYANMEQVASGVHFRLRARAFIVAEPYKKRIAFV FT NLDAGMASQLVTIKVIERLKQRYGELYTEENVAISGTHTHA FT GPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENL FT RPGSILINKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDK FT EMTLVKFVDDQWGPVARIMEDWFERENGCRSVDVESPRRVS FT SIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFR FT HADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGLPCEFNQST FT CGGKNEQCYGRGPGYPDEFESTRIIGERQFKKAADLFTKAS FT EEIQGKVDYRHAYVDFSQLEVTINGQNGGSEVVKTCPAAMG FT FGFAAGTTDGPGAFDFKQGDDQ -> MFSTILYVVTLCK FT (in isoform 2). FT /FTId=VSP_058913. SQ SEQUENCE 733 AA; 81838 MW; 4E00C150E5FCEED9 CRC64; MTRWSMSMHC TLFLLFLLRL TCIFSDSDYL MGLGSYDITG PAADVNMMGY ANMEQVASGV HFRLRARAFI VAEPYKKRIA FVNLDAGMAS QLVTIKVIER LKQRYGELYT EENVAISGTH THAGPGGYLQ YILYLVTSLG FVHQSFNALV DGIEQSIIQA HENLRPGSIL INKGELLDAG VNRSPSAYLN NPAHERSKYE YDVDKEMTLV KFVDDQWGPV ARIMEDWFER ENGCRSVDVE SPRRVSSIIS DPYDQDLMEM ASSLLSTGGK TVTRMSSVAR RVRSRFRHAD KPRFVSAFCQ TNCGDVSPNV LGAFCIDTGL PCEFNQSTCG GKNEQCYGRG PGYPDEFEST RIIGERQFKK AADLFTKASE EIQGKVDYRH AYVDFSQLEV TINGQNGGSE VVKTCPAAMG FGFAAGTTDG PGAFDFKQGD DQGNPFWRLV RNLLKNPTEE QVRCQRPKPI LLDTGEMKQP YDWAPSILPV QILRIGQLVI LCVPGEFTTM AGRRLRDAVK TVLKEGSNGR EFSVVIAGLT NSYSQYIATF EEYQVQRYEG ASTLYGPHTL SGYIQEFKKL ANDLLSAQTT DPGPQPPDLL HKQISLLTPV VADMTPIGTA FGDVTSDVPR LSKFRKGADI VRVQFRSANP RNDLMTEGTF ALVERWLEGR ETWVPVYDDD DFCLRFKWSR PFKLSTQSTA TIEWRIPETA SPGVYRITHF GSAKTPISSI HHFSGSSSAF VVY //