FAAH_ORYSJ
ID FAAH_ORYSJ Reviewed; 608 AA.
AC Q0JFH7; A0A0N7KIG0; Q15KE3; Q7XTB3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Fatty acid amide hydrolase {ECO:0000303|PubMed:16624618};
DE EC=3.5.1.- {ECO:0000269|PubMed:16624618};
DE AltName: Full=N-acylethanolamine amidohydrolase {ECO:0000303|PubMed:16624618};
GN Name=FAAH {ECO:0000303|PubMed:16624618};
GN OrderedLocusNames=Os04g0102700 {ECO:0000312|EMBL:BAS87513.1};
GN ORFNames=OsJ_13498 {ECO:0000312|EMBL:EEE60367.1},
GN OSJNBa0068L06.10 {ECO:0000312|EMBL:CAE01584.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16624618; DOI=10.1016/j.bbalip.2006.03.004;
RA Shrestha R., Kim S.C., Dyer J.M., Dixon R.A., Chapman K.D.;
RT "Plant fatty acid (ethanol) amide hydrolases.";
RL Biochim. Biophys. Acta 1761:324-334(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of bioactive endogenous fatty acid
CC amides to their corresponding acids (PubMed:16624618). The hydrolysis
CC of endogenous amidated lipids terminates their participation as lipid
CC mediators in various signaling systems (Probable). Converts a wide
CC range of N-acylethanolamines (NAEs) to their corresponding free fatty
CC acids and ethanolamine (PubMed:16624618). {ECO:0000269|PubMed:16624618,
CC ECO:0000305|PubMed:16624618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z,12Z-octadecadienoyl)-ethanolamine = (9Z,12Z)-
CC octadecadienoate + ethanolamine; Xref=Rhea:RHEA:35567,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30245, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:64032; Evidence={ECO:0000269|PubMed:16624618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35568;
CC Evidence={ECO:0000269|PubMed:16624618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine +
CC hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464;
CC Evidence={ECO:0000269|PubMed:16624618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065;
CC Evidence={ECO:0000269|PubMed:16624618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC Evidence={ECO:0000269|PubMed:16624618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC Evidence={ECO:0000269|PubMed:16624618};
CC -!- ACTIVITY REGULATION: Inhibited by methyl arachidonyl fluorophosphonate
CC (MAFP). {ECO:0000269|PubMed:16624618}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for N-acylethanolamine 18:2 {ECO:0000269|PubMed:16624618};
CC KM=24 uM for N-acylethanolamine 16:0 {ECO:0000269|PubMed:16624618};
CC KM=68 uM for N-acylethanolamine 12:0 {ECO:0000269|PubMed:16624618};
CC -!- SUBUNIT: Forms homodimers. {ECO:0000250|UniProtKB:Q7XJJ7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7XJJ7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q7XJJ7}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ94202.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE01584.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE60367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ118178; AAZ94202.1; ALT_INIT; mRNA.
DR EMBL; AL606442; CAE01584.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF13910.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS87513.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE60367.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015633439.1; XM_015777953.1.
DR AlphaFoldDB; Q0JFH7; -.
DR SMR; Q0JFH7; -.
DR STRING; 4530.OS04T0102700-01; -.
DR PaxDb; Q0JFH7; -.
DR PRIDE; Q0JFH7; -.
DR EnsemblPlants; Os04t0102700-01; Os04t0102700-01; Os04g0102700.
DR GeneID; 4334893; -.
DR Gramene; Os04t0102700-01; Os04t0102700-01; Os04g0102700.
DR KEGG; osa:4334893; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_2_1; -.
DR InParanoid; Q0JFH7; -.
DR OMA; NVLGWPS; -.
DR OrthoDB; 1036483at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047412; F:N-(long-chain-acyl)ethanolamine deacylase activity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..608
FT /note="Fatty acid amide hydrolase"
FT /id="PRO_0000451042"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT ACT_SITE 306
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
FT BINDING 303..306
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7XJJ7"
SQ SEQUENCE 608 AA; 66547 MW; 9CE942BAA8E1222A CRC64;
MGKPPRAMTP VEEVDLSAVR YQSPSLQAPH LTGFSLRAFV WLMESPLFGR LLTSVLKSQN
NITRMLQDTV IPERPMYLPE YPPQEPEQGV LLLGDDRDPV DRVEEALHCL PPYDPSLRWP
AGDKPPFLYW KIRDFAHAYR SGITTPSVVA EHIIAGVEEW SNKKPPMPML VYFNADDLRK
QAEASTKRFQ QGNPISILDG IFIAIKDDID CFPYPSKGAT TFFDKIRSVE KDAVCVARLR
KCGVLFIGKA NMHELGLGVT GNNPNYGTAR NPHSIDRYTG GSSSGPAALV SSGLCSAAIG
TDGGGSVRIP SSLCGIIGLK TTYGRTDMTG ALCDCGTVEV ASPLAASVED ALLVYSAIAG
SRPMDKLTLR PSPLCVPNLV SPDNNNILGS VKIGKYTEWF HDVSDRDISN TCEDALNLLC
SSFGCQIEEI ILPELEEMRT AHVVSIGTES FCDLNPHYRA GKRTEFTLDT RTSLALFGSF
TSTDYVASQR IRRRIMYYHN EAFKKVDVIA TPTTGITAPE IPQSSLKLGE SNYVVSAYLM
RFVIAGNLLG LPAITVPVGH DKQGLPIGLQ LIGRPWGEAS LLRVASAIEE LCLQKRKRPS
AFHDILNA
