NCER3_ARATH
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 03-AUG-2022, entry version 68.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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 and
CC free fatty acid (By similarity). Promotes oxidative stress resistance
CC (PubMed:26150824). {ECO:0000250|UniProtKB:F4HQM3,
CC ECO:0000269|PubMed:26150824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC Evidence={ECO:0000250|UniProtKB:O06769};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VA70}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:F4HQM3}. Golgi apparatus
CC {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 -!- DISRUPTION PHENOTYPE: Increased sensitivity to C2-ceramide induced cell
CC death. {ECO:0000269|PubMed:26150824}.
CC -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; F4KHQ8; -.
DR SMR; F4KHQ8; -.
DR STRING; 3702.AT5G58980.1; -.
DR PaxDb; F4KHQ8; -.
DR PRIDE; F4KHQ8; -.
DR ProteomicsDB; 251206; -. [F4KHQ8-1]
DR EnsemblPlants; AT5G58980.1; AT5G58980.1; AT5G58980. [F4KHQ8-1]
DR GeneID; 836015; -.
DR Gramene; AT5G58980.1; AT5G58980.1; AT5G58980. [F4KHQ8-1]
DR KEGG; ath:AT5G58980; -.
DR Araport; AT5G58980; -.
DR TAIR; locus:2154598; AT5G58980.
DR eggNOG; KOG2232; Eukaryota.
DR HOGENOM; CLU_011300_2_0_1; -.
DR InParanoid; F4KHQ8; -.
DR OMA; DWPGAFD; -.
DR OrthoDB; 967085at2759; -.
DR PRO; PR:F4KHQ8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KHQ8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.60.40.2300; -; 1.
DR InterPro; IPR006823; Ceramidase_alk.
DR InterPro; IPR038445; NCDase_C_sf.
DR InterPro; IPR031331; NEUT/ALK_ceramidase_C.
DR InterPro; IPR031329; NEUT/ALK_ceramidase_N.
DR PANTHER; PTHR12670; PTHR12670; 2.
DR Pfam; PF04734; Ceramidase_alk; 1.
DR Pfam; PF17048; Ceramidse_alk_C; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Hydrolase; Lipid metabolism; Reference proteome; Secreted; Signal;
KW Sphingolipid metabolism.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..733
FT /note="Neutral ceramidase 3"
FT /id="PRO_5003311651"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9NR71"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..432
FT /note="MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGPAADVNMMGYAN
FT MEQVASGVHFRLRARAFIVAEPYKKRIAFVNLDAGMASQLVTIKVIERLKQRYGELYTE
FT ENVAISGTHTHAGPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENLRPGSIL
FT INKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDKEMTLVKFVDDQWGPVARIMEDWFE
FT RENGCRSVDVESPRRVSSIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFRH
FT ADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGLPCEFNQSTCGGKNEQCYGRGPGYPDEF
FT ESTRIIGERQFKKAADLFTKASEEIQGKVDYRHAYVDFSQLEVTINGQNGGSEVVKTCP
FT AAMGFGFAAGTTDGPGAFDFKQGDDQ -> MFSTILYVVTLCK (in isoform 2)"
FT /id="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
