ID A0A2U3X860_LEPWE Unreviewed; 395 AA.
AC A0A2U3X860;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Acid ceramidase {ECO:0000256|ARBA:ARBA00040588};
DE EC=3.5.1.23 {ECO:0000256|ARBA:ARBA00011891};
GN Name=ASAH1 {ECO:0000313|RefSeq:XP_006727669.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006727669.1};
RN [1] {ECO:0000313|RefSeq:XP_006727669.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006727669.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00036977};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR017632}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371,
CC ECO:0000256|PIRNR:PIRNR017632}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the acid ceramidase family.
CC {ECO:0000256|ARBA:ARBA00005730, ECO:0000256|PIRNR:PIRNR017632}.
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DR RefSeq; XP_006727669.1; XM_006727606.2.
DR AlphaFoldDB; A0A2U3X860; -.
DR STRING; 9713.A0A2U3X860; -.
DR GeneID; 102745505; -.
DR KEGG; lww:102745505; -.
DR CTD; 427; -.
DR OrthoDB; 5485766at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:InterPro.
DR GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01903; Ntn_AC_NAAA; 1.
DR InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR PANTHER; PTHR28583; ACID AMIDASE; 1.
DR PANTHER; PTHR28583:SF1; ACID CERAMIDASE; 1.
DR Pfam; PF02275; CBAH; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR017632};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR017632}; Lysosome {ECO:0000256|PIRNR:PIRNR017632};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..395
FT /note="Acid ceramidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015713488"
FT DOMAIN 45..107
FT /note="Acid ceramidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15508"
FT DOMAIN 143..382
FT /note="Choloylglycine hydrolase/NAAA C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02275"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ SEQUENCE 395 AA; 44779 MW; 44623376BEBEA4D0 CRC64;
MLGRSRVTLV LLTVAVTCAL AQQAPPWTEN CRKSTYPPSG PTYRGPVPWY TINLDLPPYK
RWHELMADKA PALRIIVNSL KDLVNAFVPS GKIMQIVDQK LPGLLGNFPG PFEEEMKGIA
AATEIPLGEI ISFNVFYEFF TICTSIITED KEGHLLHGRN MDFGVFLGWN INNNTWVITE
QLKPLTVNLD FQRNNKTVFK ASSFAGYVGM LTGFKPGLLS LTLNERFSIN GGYMGVIEWI
WGKKDAMWIG FITRSVLENS TSYEEAKNIL TKTKILAPAY FILGGNKTGE GCVITRDRKQ
SLDVYELNPK QDRWYVVQTN YDRWKSPFFL DDRRTPAKMC LNQTTQKNIS FATIYDVLST
KPVLNKLTVF TALMDVTKGQ YETYLRDCPD PCIGW
//
