ID L5JLY9_PTEAL Unreviewed; 957 AA.
AC L5JLY9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ceramidase {ECO:0000256|ARBA:ARBA00011891};
DE EC=3.5.1.23 {ECO:0000256|ARBA:ARBA00011891};
GN ORFNames=PAL_GLEAN10025528 {ECO:0000313|EMBL:ELK00389.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK00389.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(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 -!- 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}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KB031158; ELK00389.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JLY9; -.
DR STRING; 9402.L5JLY9; -.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; L5JLY9; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:UniProt.
DR CDD; cd04046; C2_Calpain; 1.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR008901; ACER.
DR InterPro; IPR033884; C2_Calpain.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF402; CALPAIN-5; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF05875; Ceramidase; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..660
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 816..931
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 569
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 601
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 957 AA; 108843 MW; 5F404D241DE86992 CRC64;
MAPAADREGY WGPTTSTLDW CEENYAVTWY IAEFWNTVSN LIMIIPPIFG AIQSIKDGLE
KRYIASYLAL TVVGMGSWCF HMTLKYEMQL LDELPMIYSC CIFVYCMFEC FKMKNSVNYH
MLFTLVLFSL VVTTVYLKVK EPVFHQVMYG MLVFTLVLRS IYIVTWVYPW LRGLGYTSLG
LFLLGFLLWN IDNIFCVSLR NFRKKVPPVI GVTTQFHAWW HILTGLGSYL HILFRRPRNR
PLTCCSRLRG GGPEERLGDS AAAFLWLRHE PGSCGSATRL DAARGGLGKA GAPGTAHSPA
ETPRCPVWAF APRAVAAMFS CMKPYGDQNY SALKRACLRK KVLFEDPSFP ATDDSLYYKG
TPGPAVRWQR PKDICEDPRL FVDGISSHDL HQGQVGNCWF VAACSSLASR ESLWQKVIPD
WKEQEWDPEK PDAYAGIFHF HFWRFGEWID VVIDDRLPTV NNQLIYCHSN SRNEFWCALV
EKAYAKLAGC YQALDGGNTA DALVDFTGGV SEPIDLTEGD FANDEGKRNQ LFERVLKVHS
RGGLISASIK AVTAADMEAR LACGLVKGHA YAITDVRKVR LGHGLLAFFK SEKLDMIRLR
NPWGEREWNG PWSDTSEEWQ KVSKSEREKM GVTVQDDGEF WMTFEDLCRY FTDIIKCRLI
NTSYLSVHKT WEEARLHGAW TQHEDPWQNR SGGCINHKDT FFQNPQYIFD VKKPEDEVLI
CIQQRPKQST RRDGKGENLA IGFDIYKVEE NRQYRMHRLQ HRAASSIYIN SRSVFLRTDQ
PEGRYVIIPT TFEPGHTGQF LLRVFTDVPS NCRELCLDEP PRSCWSSLCG YPQQVTQVHV
LGAAGLKDSS TGANSYVIIK CEGDKVRSAV QKGTSTPEYN VKGIFYRKKP GQPITVQVWN
HRVLKDEFLG QVRLKADSDD LQALHTLHLQ DRSSRQPSDL PGTIAVHILS SASLTAV
//
