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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
 
 
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