ID I7MA68_TETTS Unreviewed; 349 AA.
AC I7MA68;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
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_00657610 {ECO:0000313|EMBL:EAS03816.1};
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:EAS03816.1, 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}.
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DR EMBL; GG662471; EAS03816.1; -; Genomic_DNA.
DR RefSeq; XP_001024061.1; XM_001024061.1.
DR AlphaFoldDB; I7MA68; -.
DR STRING; 312017.I7MA68; -.
DR EnsemblProtists; EAS03816; EAS03816; TTHERM_00657610.
DR GeneID; 7842271; -.
DR KEGG; tet:TTHERM_00657610; -.
DR eggNOG; ENOG502RT09; Eukaryota.
DR HOGENOM; CLU_054401_0_0_1; -.
DR InParanoid; I7MA68; -.
DR OMA; RYSINLD; -.
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 CDD; cd01903; Ntn_AC_NAAA; 1.
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};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..349
FT /note="N-acylethanolamine-hydrolyzing acid amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003712109"
FT DOMAIN 30..88
FT /note="Acid ceramidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15508"
FT ACT_SITE 124
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR017632-1"
SQ SEQUENCE 349 AA; 40011 MW; 76136710F3E528DE CRC64;
MKLTLLFIGL FLGLSSAIMI PHPGPLHFHN PPRYQVDIDA PPKVQWAPIM NDFKEPLSIF
IAEFEHLLPI PKWIFNAVGV YGKTIFKYQK YVKQVEAIAE LTGLPFNTLF TLNFMYELAS
WKACTGVVVR NNNGTIYHGR NLDFEFFRYF SNLTMTIDYY RNNQHIFSVD GLAGAIFFHS
GVKPGKFGLT QTTRNSKSLF TNLQAIAKGN FPSVWLIKET LETEDSFEGA VQKLNTTAIA
CPIYYMVSGP GINDGVVIER NYDSIHGFYQ LNETTSFLVQ TNYDRDVPDP WYDRRRIPAQ
ERLEKLNGNI NETILMEDIM MKYPTLNVAT IMSTVVNPRT GYFNTSTWW
//
