NCSEB_DICDI
ID NCSEB_DICDI Reviewed; 718 AA.
AC Q55G11;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Neutral ceramidase B;
DE Short=N-CDase B;
DE Short=NCDase B;
DE EC=3.5.1.23;
DE AltName: Full=Acylsphingosine deacylase 2B;
DE AltName: Full=N-acylsphingosine amidohydrolase 2B;
DE Flags: Precursor;
GN Name=dcd2B; ORFNames=DDB_G0268374;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
CC -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine and
CC free fatty acid. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neutral ceramidase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73640.1; -; Genomic_DNA.
DR RefSeq; XP_647372.1; XM_642280.1.
DR AlphaFoldDB; Q55G11; -.
DR SMR; Q55G11; -.
DR STRING; 44689.DDB0232168; -.
DR PaxDb; Q55G11; -.
DR EnsemblProtists; EAL73640; EAL73640; DDB_G0268374.
DR GeneID; 8616181; -.
DR KEGG; ddi:DDB_G0268374; -.
DR dictyBase; DDB_G0268374; dcd2B.
DR eggNOG; KOG2232; Eukaryota.
DR HOGENOM; CLU_011300_2_0_1; -.
DR InParanoid; Q55G11; -.
DR OMA; DWPGAFD; -.
DR PhylomeDB; Q55G11; -.
DR PRO; PR:Q55G11; -.
DR Proteomes; UP000002195; Chromosome 1.
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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Lipid metabolism; Reference proteome; Secreted;
KW Signal; Sphingolipid metabolism.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..718
FT /note="Neutral ceramidase B"
FT /id="PRO_0000247109"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
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 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 718 AA; 78609 MW; BDAE0B6C79271AFA CRC64;
MINSFKKLII LISLVIILLS SNNIFIDSFK IPVNQKNVKS SGDSSYQIGA GIYDITGASA
EVNLMGYANP LQVGAGIHFR QRARAFVFVD SNGNRAVYVS TDSCMIFQEV KIHVVELLQD
IFGPNVYTEA NVLLSGTHTH SGPAGFSQYA LYGITSLGFY KKNFDTICNG IVQAIVKAHK
SVQPANMFTE TGELWNTNIN RSPFAYDNNP EEEKAMYDSN VDKNMTVLRI EDMNGNPFAA
ISFFAVHCTS MNNTNHLISG DNKGYASYLW EKQVNGPGTA GKGPFVAAFG QSNEGDVSPN
TRGPTCRDGS PCDYKTSTCN GRNEECWSLG PGKDGDMFES TQIIGGNQFN KALELFNNAS
IQVSGPVQYR HSWVQFTNVS VEPPYNSGVD NATTCRGAMG YSFAAGTTDG PGAFNFVQSD
NNTSGNPFWN FIGDFIAKPT PDQIRCQSPK PILLDVGMVE PIPWVPDVMP IQIVTIGQIV
LVAVPGEFTT MSGRRLRNSV REIIGESIEN PIVLIAGLSN TYSGYIATFE EYQVQRYEGA
STVFGPHTLG SYMQEFGKLA QSIVDGTTVP AGPTPRNLTG HTLFFLPPVI VDAAPDFDDF
GEVSIDVNLN YSVNETVSCV FYGGNPRNDF MIESSFLSVD LLTGTDQWTT VLDDGDWDTK
FKWKMHDLGF SLITIEWVIA PDTTPGTYRI THSGFAKKNP FSSNLTPYQG ISRNFVVQ