ID L9LCV0_TUPCH Unreviewed; 1287 AA.
AC L9LCV0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=ceramidase {ECO:0000256|ARBA:ARBA00011891};
DE EC=3.5.1.23 {ECO:0000256|ARBA:ARBA00011891};
GN ORFNames=TREES_T100007069 {ECO:0000313|EMBL:ELW72489.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW72489.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate
CC + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996;
CC Evidence={ECO:0000256|ARBA:ARBA00000115};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC Evidence={ECO:0000256|ARBA:ARBA00000115};
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:0000256|ARBA:ARBA00000595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857;
CC Evidence={ECO:0000256|ARBA:ARBA00000595};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + H2O = a fatty acid + sphinganine;
CC Xref=Rhea:RHEA:33551, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:31488, ChEBI:CHEBI:57817;
CC Evidence={ECO:0000256|ARBA:ARBA00000351};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33552;
CC Evidence={ECO:0000256|ARBA:ARBA00000351};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family.
CC {ECO:0000256|ARBA:ARBA00009780}.
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DR EMBL; KB320406; ELW72489.1; -; Genomic_DNA.
DR STRING; 246437.L9LCV0; -.
DR eggNOG; KOG2127; Eukaryota.
DR InParanoid; L9LCV0; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:InterPro.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:UniProt.
DR Gene3D; 2.100.10.50; -; 1.
DR InterPro; IPR008901; ACER.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR037516; Tripartite_DENN.
DR PANTHER; PTHR12296; DENN DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR12296:SF17; DENN DOMAIN-CONTAINING PROTEIN 4C; 1.
DR Pfam; PF05875; Ceramidase; 1.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR SMART; SM00801; dDENN; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS51498; MABP; 1.
PE 3: Inferred from homology;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1001..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1029..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1059..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..200
FT /note="MABP"
FT /evidence="ECO:0000259|PROSITE:PS51498"
FT DOMAIN 264..411
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT REGION 506..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 142507 MW; BE79D5264A37A8BE CRC64;
MIEDKGPRVT DYFVVAGLTD TSTLLDPEVN RLDSKSIGPK APITDIAVII KSAGETVPEG
YTCVEATPSA LQANLNYGSL KSPELFLCYK RGRDKPPLSD IGVLYEGKER LIPGCEVIQA
TPYGRCANVN NSSTTSQRIF ITYRRAPLIR PQNSLAVTDI CVIVTSKGET PPHTFCKVDK
NLNCGMVYGA AIQFYEPYSR ELLTEKQLMQ LGLVTPVERK VVSKSINSNK CICLLSHWPF
FEAFRKFLMF IYKLSVSGPH PLPIEKSDEK KNMNWKQLPK KPCKNLLSTL KKLYPQLASV
HRKTQEGSAI DMTPIEADFS WQKKMTQLEM EIQEAFLRFM ASILKGYRTY LKPITEAPSN
KATAVDSLFD RQGFLKSRDR AYTKFYTLLS KTQIFIRFIE ECSFVSDKDT GLAFFDDCIE
KVCYRVVMQL CGLWGHPVLA VRVLFEMKTA KIKPNAITYG YYNKVVLESP WPSSTRSGIF
LWTKVRNVIH GLAQFRQPLK KTMQKAQVSS ISAPQNATGG SDGDTVSHGS VDSSNDANSG
EHTVFVRDLI RLDSIDNHSS TDICDVSAIV AKHSQSSSEP QSPTEPPAWG SSIVKVPSGI
FDINSRKSST GSVSNVLFSA QDQIEDTVFG EVTNLKKNGD RGEKRQKHFP ERSCSFSFES
RAGMLLKKSS LDLNSSEMAI MMGADAKILT AALTCPKTSS LHIARTRSFE NASCHPVDSR
TRTSESTWDP ESRSSPVLEM LEESQELLEP VADDNMTKMT TTQDESDGLQ NDSNSDQSRD
LKAGSRDLIN KRSSLYGVAK AVEREDVETG LDPLSLLATE CTGEKTPDAE EKMFSPVIAR
NLADEIESYM NLKSPLGSKS SSMELHGDGN RESGVTTAVT HPLERRSSLP LDHGPPVQEN
AENEKSSPAV SRSKTFTGRF KQQTPSRTHK ERSTSLSALM RSSPHGSLGS VVNSFSGLKL
DNILSGPKID VLKSSMKQAA TVASKMWVAV ASAYNYSDDE ISNVLFFILP PICMCLFRQY
ATCFNSGIYL IWTLLVVVGI GSVYFHATLS FLGQMLDELA ILWVLMCALA MWFPRRYLPK
IFRNDRGRFK AVVCVLSAVT TCLAFVKPAI NNISLMTLGV PCTALLIAEL KRHILICLAA
YLGCVCFAYF DAASEIPEQG PVIKFWPSEK WAFIGVPYVS LLCANKKSPK KKEAEAEEVA
EEEKGKEKKQ AFEGLEPGLT SASKAPDEAV LSGKCVQEDK WALRRAVWLP FPCWVVLREC
LLPAACSEKG LLVHLLRRAS VASAAKR
//
