ID Q23R98_TETTS Unreviewed; 382 AA.
AC Q23R98;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=N-acylethanolamine-hydrolyzing acid amidase {ECO:0000256|ARBA:ARBA00040404};
DE EC=3.5.1.60 {ECO:0000256|ARBA:ARBA00039046};
GN ORFNames=TTHERM_00389900 {ECO:0000313|EMBL:EAR99150.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR99150.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, produced by
CC autocatalytic cleavage. {ECO:0000256|ARBA:ARBA00038527}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the acid ceramidase family.
CC {ECO:0000256|ARBA:ARBA00005730}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG662644; EAR99150.2; -; Genomic_DNA.
DR RefSeq; XP_001019395.2; XM_001019395.3.
DR AlphaFoldDB; Q23R98; -.
DR STRING; 312017.Q23R98; -.
DR EnsemblProtists; EAR99150; EAR99150; TTHERM_00389900.
DR GeneID; 7834817; -.
DR KEGG; tet:TTHERM_00389900; -.
DR eggNOG; ENOG502REHN; Eukaryota.
DR HOGENOM; CLU_054401_0_0_1; -.
DR InParanoid; Q23R98; -.
DR OMA; HKESTTH; -.
DR OrthoDB; 178549at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR PANTHER; PTHR28583; ACID AMIDASE; 1.
DR PANTHER; PTHR28583:SF4; N-ACYLETHANOLAMINE-HYDROLYZING ACID AMIDASE; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAR99150.2};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..382
FT /note="N-acylethanolamine-hydrolyzing acid amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004202078"
FT DOMAIN 27..65
FT /note="Acid ceramidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15508"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ SEQUENCE 382 AA; 43661 MW; 5CDB14E76B3948F0 CRC64;
MNQFKYLILI IAIFMINIET TQAVGSDPLF IINLDLPHLE RWREIMGVKG QILKEFAYKY
KQHVNISEDL AEQFLSYGKA HPEIAKNIEA ISTLTGIDLP TLYTFNFMYD LENMGCTSVI
IRQPDNTLFH ARNLDYSFQE EISKLAIQAQ WTRNGQIIYK SETLVGFVSL ITVTKVGQFS
ISINYRTSDS IQKNIDALIK DHYYQGIYLP QIAVDQANNF DEAVQILKTV NVSSPIYFIV
SGLQGNQGVV IERNRDSVLN VYTLSESDWF LVQTNTDRSN TKIKDFRYRE TVKNIQALGQ
QNCTKENILN KVMGVFPANN KLTISTSVYS AYDGDFISRN YLIDDQAIQQ SLLREQISSS
LSNGSIIQNL LFLTFILCFS LY
//
