ID   NCASE_ORYSJ             Reviewed;         785 AA.
AC   Q0JL46; A0A0P0V5E9; B9EY48; Q5ZE61;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Neutral ceramidase;
DE            Short=N-CDase;
DE            Short=NCDase;
DE            Short=OsCDase;
DE            EC=3.5.1.23;
DE   AltName: Full=Acylsphingosine deacylase;
DE   AltName: Full=N-acylsphingosine amidohydrolase;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os01g0624000, LOC_Os01g43520;
GN   ORFNames=OsJ_02661, P0501G01.30-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18547394; DOI=10.1111/j.1365-313x.2008.03569.x;
RA   Pata M.O., Wu B.X., Bielawski J., Xiong T.C., Hannun Y.A., Ng C.K.-Y.;
RT   "Molecular cloning and characterization of OsCDase, a ceramidase enzyme
RT   from rice.";
RL   Plant J. 55:1000-1009(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC       free fatty acid. Uses ceramide instead of phytoceramide as substrate.
CC       {ECO:0000269|PubMed:18547394}.
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   -!- ACTIVITY REGULATION: Enhanced activity in the presence of calcium,
CC       magnesium, manganese and zinc ions, but inhibited activity in the
CC       presence of iron ion. {ECO:0000269|PubMed:18547394}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=39.34 uM for D-erythro-C12-NBD-ceramide (at pH 5.7 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:18547394};
CC         Vmax=0.079 pmol/h/ug enzyme with D-erythro-C12-NBD-ceramide as
CC         substrate {ECO:0000269|PubMed:18547394};
CC       pH dependence:
CC         Optimum pH is 5.7-6. {ECO:0000269|PubMed:18547394};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:18547394}. Golgi apparatus
CC       {ECO:0000269|PubMed:18547394}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q0JL46-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, with higher levels in roots
CC       than in shoots. {ECO:0000269|PubMed:18547394}.
CC   -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD61179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EEE55011.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EU422991; ACA49516.1; -; mRNA.
DR   EMBL; AP002819; BAD61179.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008207; BAF05532.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS73237.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE55011.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK099625; BAG94227.1; -; mRNA.
DR   RefSeq; XP_015620868.1; XM_015765382.1. [Q0JL46-1]
DR   AlphaFoldDB; Q0JL46; -.
DR   SMR; Q0JL46; -.
DR   STRING; 4530.OS01T0624000-01; -.
DR   PaxDb; Q0JL46; -.
DR   PRIDE; Q0JL46; -.
DR   EnsemblPlants; Os01t0624000-01; Os01t0624000-01; Os01g0624000. [Q0JL46-1]
DR   EnsemblPlants; Os01t0624000-02; Os01t0624000-02; Os01g0624000. [Q0JL46-1]
DR   GeneID; 4326680; -.
DR   Gramene; Os01t0624000-01; Os01t0624000-01; Os01g0624000. [Q0JL46-1]
DR   Gramene; Os01t0624000-02; Os01t0624000-02; Os01g0624000. [Q0JL46-1]
DR   KEGG; osa:4326680; -.
DR   eggNOG; KOG2232; Eukaryota.
DR   HOGENOM; CLU_011300_2_0_1; -.
DR   InParanoid; Q0JL46; -.
DR   OMA; DWPGAFD; -.
DR   OrthoDB; 967085at2759; -.
DR   BioCyc; MetaCyc:MON-15591; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q0JL46; baseline and differential.
DR   Genevisible; Q0JL46; OS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
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: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   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..785
FT                   /note="Neutral ceramidase"
FT                   /id="PRO_0000403419"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        675
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        685
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   785 AA;  86593 MW;  C8AD952C8A3053C0 CRC64;
     MEASSWLCYQ ARGFGSSRVW LWLLLALVLL NCSLVLSASP YLVGMGSFDI TGPAADVNMM
     GYANTEQIAS GIHFRLKSRA FIVAEPNGKR VVFVNIDACM ASQIVTIKVL ERLKARYGDL
     YNENNVAISG IHTHAGPGGY LQYVVYIVTS LGFVRQSFDV IVDGIEQSIV EAHNNLRPGK
     IFVNKGDLLD AGVNRSPSAY LNNPAEERSK YEYNVDKEMT LIKFVDDELG PVGSFNWFAT
     HGTSMSRTNS LISGDNKGAA ARFMEDWAEQ MGLPKQSAHA NSDDLRSLHK TSVLPRRVST
     IIPEPNEITD DLIQLASSYE ASGGRRLAGS SITRRIRSTQ QNKPKFVSAF CQSNCGDVSP
     NVLGTFCIDT NLPCDFNHST CNGKNELCYG RGPGYPDEFE STRVIGNRQF LKARDLFDSA
     SEEIQGKIDY RHTYLDFSKL EVKVSTSAGG QQTVKTCPAA MGFAFAAGTT DGPGAFDFRQ
     GDVKGNPFWK LVRNLLKTPG KDQVECHSPK PILLDTGEMK EPYDWAPAIL PVQMIRIGQL
     VILCVPGEFT TMAGRRLRDA VKTVLTSGNS EFDKNIHVVL AGLTNSYSQY ITTFEEYQIQ
     RYEGASTLYG PHTLSAYIQE FQKLAMAMIA NKEVPTNFQP PDMLDKQIGL LPGVVFDSTP
     LGVKFGDVNS DVPGNSTFNK GSTVNATFYS ACPRNDLLTD GTFALVEKLD GNNNWVPVYD
     DDDWSLRFKW SRPARLSSRS FATLEWTVPE DAAAGVYRLR HFGASKPMFG SVRHFTGTSR
     AFAVR