NCER1_ARATH
ID NCER1_ARATH Reviewed; 779 AA.
AC F4HQM3; Q9LNV7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Neutral ceramidase 1 {ECO:0000303|PubMed:26150824};
DE Short=AtNCER1 {ECO:0000303|PubMed:26150824};
DE Short=N-CDase 1 {ECO:0000303|PubMed:26150824};
DE Short=NCDase 1 {ECO:0000303|PubMed:26150824};
DE EC=3.5.1.23 {ECO:0000250|UniProtKB:O06769};
DE AltName: Full=Acylsphingosine deacylase 1;
DE AltName: Full=N-acylsphingosine amidohydrolase 1;
DE Flags: Precursor;
GN Name=NCER1 {ECO:0000303|PubMed:26150824};
GN OrderedLocusNames=At1g07380 {ECO:0000312|Araport:AT1G07380};
GN ORFNames=F22G5.28 {ECO:0000312|EMBL:AAF79556.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP 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. Regulates sphingolipid homeostasis. Promotes oxidative
CC stress resistance. {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:0000269|PubMed:26150824}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q0JL46}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000312|Araport:AT1G07380};
CC Name=1;
CC IsoId=F4HQM3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, leaves, roots and
CC siliques, and, to a lower extent, in flowers.
CC {ECO:0000269|PubMed:26150824}.
CC -!- DISRUPTION PHENOTYPE: Increased accumulation of hydroxyceramides.
CC Enhanced sensitivity to oxidative stress induced by methyl viologen.
CC Increased sensitivity to C2-ceramide induced cell death.
CC {ECO:0000269|PubMed:26150824}.
CC -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79556.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022464; AAF79556.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28116.1; -; Genomic_DNA.
DR PIR; G86208; G86208.
DR RefSeq; NP_172218.1; NM_100612.2. [F4HQM3-1]
DR AlphaFoldDB; F4HQM3; -.
DR SMR; F4HQM3; -.
DR STRING; 3702.AT1G07380.1; -.
DR PaxDb; F4HQM3; -.
DR PRIDE; F4HQM3; -.
DR EnsemblPlants; AT1G07380.1; AT1G07380.1; AT1G07380. [F4HQM3-1]
DR GeneID; 837250; -.
DR Gramene; AT1G07380.1; AT1G07380.1; AT1G07380. [F4HQM3-1]
DR KEGG; ath:AT1G07380; -.
DR Araport; AT1G07380; -.
DR TAIR; locus:2025042; AT1G07380.
DR eggNOG; KOG2232; Eukaryota.
DR HOGENOM; CLU_011300_2_0_1; -.
DR InParanoid; F4HQM3; -.
DR OMA; VWHRTNT; -.
DR BRENDA; 3.5.1.23; 399.
DR PRO; PR:F4HQM3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQM3; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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:TAIR.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IMP:TAIR.
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; 1.
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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..779
FT /note="Neutral ceramidase 1"
FT /id="PRO_0000439757"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9NR71"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 779 AA; 86771 MW; BE9FBACD3AA91540 CRC64;
MELSLVRLWN TCFPSFFYIS TVLFLLTGGG VYSHSEYLIG LGSYDITGPA ADVNMMGYAN
MEQVASGIHF RLRARTFIVS EPQGKRVVFV NLDACMASQI VKLKVIERLK ARYGDLYTEQ
NVGISGIHTH AGPGGYLQYV VYIVTSLGFV RQSFDALVDG IENSIIQAHE NLRPGSIFLN
NGELLDAGVN RSPSAYLNNP SKERSKHKYN VDKEMTLLKF VDDQWGPVGS FNWFATHGTS
MSRTNSLISG DNKGAASRFM EDWYEQNTAE RSYSEEFISD EIPRRVSSLI ENHQDSHHEL
LELASYFESQ PGKPVTRISS SARRVRSALR KADKPGFVSA FCQTNCGDVS PNVLGAFCLD
TGLPCDFNHS TCGGKNEMCY GRGPGYPDEF ESTRIIGERQ FKMALELFNK ASEQLQGKVD
YRHVYVDFSQ LNVTLPKKDG KSEVVKTCPA AMGFAFAAGT TDGPGAFDFT QGDDKGNPFW
RLVRNVLKTP DKKQIDCHYP KPILLDTGEM TKPYDWAPSI LSLQVLRIGQ LFILSVPGEF
TTMAGRRLRY AVKTQLKNSG NKDLSGEIHV VIAGLANGYS QYVTTFEEYQ VQRYEGASTL
YGPHTLSGYI QEFKKLSKSL VLDMPVQPGP QPPDLLDKQL SFLTPVMMDT TPSGDSFGDV
ISDVPKNLSL KRGNGQVTVV FRSACPRNDL LTEGTFTLVE RLEQKDKTWT PVYDDDDLCL
RFKWSRHKKL SSRSQATVEW RIPESASPGV YRITHFGAAK KLFGSVHHFT GSSSAFVVT
