NCSEA_DICDI
ID NCSEA_DICDI Reviewed; 714 AA.
AC Q54BK2; O15913; Q75WL6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Neutral ceramidase A;
DE Short=N-CDase A;
DE Short=NCDase A;
DE EC=3.5.1.23;
DE AltName: Full=Acylsphingosine deacylase 2A;
DE AltName: Full=N-acylsphingosine amidohydrolase 2A;
DE Flags: Precursor;
GN Name=dcd2A; Synonyms=dcd, rsc25; ORFNames=DDB_G0293538;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AX4;
RX PubMed=12943537; DOI=10.1042/bj20030652;
RA Monjusho H., Okino N., Tani M., Maeda M., Yoshida M., Ito M.;
RT "A neutral ceramidase homologue from Dictyostelium discoideum exhibits an
RT acidic pH optimum.";
RL Biochem. J. 376:473-479(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-714.
RC STRAIN=AX4;
RA Iranfar N., Loomis W.F.;
RT "A neutral ceramidase homologue of Dictyostelium discoideum exhibits an
RT acidic pH optimum.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC free fatty acid at an optimal pH of 3.0. Has no activity toward
CC glycosphingolipids, such as GalCer and Galbeta1-3GalNAcbeta1-
CC 4(NeuAcalpha2-3)Galbeta1-4Glcbeta1-1'Cer or sphingomyelin.
CC {ECO:0000269|PubMed:12943537}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.0. {ECO:0000269|PubMed:12943537};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- MISCELLANEOUS: In contrast to other members of the family, it displays
CC a highest activity at acidic and not neutral pH.
CC -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
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DR EMBL; AB121061; BAC92751.1; -; mRNA.
DR EMBL; AAFI02000218; EAL60581.1; -; Genomic_DNA.
DR EMBL; U82513; AAB69633.1; -; mRNA.
DR RefSeq; XP_629027.1; XM_629025.1.
DR AlphaFoldDB; Q54BK2; -.
DR SMR; Q54BK2; -.
DR STRING; 44689.DDB0215370; -.
DR PaxDb; Q54BK2; -.
DR EnsemblProtists; EAL60581; EAL60581; DDB_G0293538.
DR GeneID; 8629313; -.
DR KEGG; ddi:DDB_G0293538; -.
DR dictyBase; DDB_G0293538; dcd2A.
DR eggNOG; KOG2232; Eukaryota.
DR HOGENOM; CLU_011300_2_0_1; -.
DR InParanoid; Q54BK2; -.
DR OMA; VWHRTNT; -.
DR PhylomeDB; Q54BK2; -.
DR Reactome; R-DDI-1660662; Glycosphingolipid metabolism.
DR PRO; PR:Q54BK2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; ISS:dictyBase.
DR GO; GO:0046514; P:ceramide catabolic process; IBA:GO_Central.
DR GO; GO:0006672; P:ceramide metabolic process; IC:dictyBase.
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 Glycoprotein; Hydrolase; Lipid metabolism; Reference proteome; Secreted;
KW Signal; Sphingolipid metabolism.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..714
FT /note="Neutral ceramidase A"
FT /id="PRO_0000247108"
FT ACT_SITE 293
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 714 AA; 78438 MW; 51D96FD13E4A266F CRC64;
MKRSIVFIYS LVILLLSVGF IDAFKISIEN HIKLSDDSSY QIGTGIYDIT GPGAETNMMG
YAMPGQITGG IHFRQRARAF VFIDSEGNRA VYVSTDSCMI FQEVKIQVIQ DLQEIFGPTL
YTHDNVLLSG THTHSGPAGF SEYALYGITA LGFYKKNFDT ICDGIVQAIV KAHKSVQPAR
MLTQQGELWN SNINRSPYAY DNNPEEEKAM YDANVDKNMT VIRIEDMSGN PFAAISFFGV
HCTSMNNTNH LISGDNKGYA SYLWEKHANG QSSLPGTGPF IAAFGQSNEG DVSPNTRGPT
CRDGKPCDYK TSTCNGKVEE CWALGPGTDG DMFESTQIIG GNQFNKALEL FNNATIQVSG
KIQYRHTWKP FTNVSVEAPY NSGVEGATTC RGAMGYSFAG GTTDGPGAFN FIQGDNSTTN
PFWNFIGGII AKPTPQQTAC QAPKPILIDV GMVEPIPWVP DVMPLQIITL GQIVLVAVPG
EFTTMSGRRL RNTVREIIGQ SIENPIVLIA GLANTYSGYI ATFEEFQVQR YEGASTVFGP
HTLGAYQQEF ANLAQSIVDG SQADPGTFPR NMSGHTPFFL PPVIVDVAPK FDDFGDIYTD
VSTTTPYSIN QTVTVIFYGA NLRNNFMTES SFLTVDQLQS NGQWTTILND GDWDTKLYWK
MHDLGFSLIT VDWTISPITQ PGTYRITHSG YAKKNPFSDN LTFYQGISSN FNVQ
