ACNT1_MOUSE
ID ACNT1_MOUSE Reviewed; 416 AA.
AC A2AKK5; A2AKK4; Q0QBA1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acyl-coenzyme A amino acid N-acyltransferase 1 {ECO:0000303|PubMed:17116739};
DE EC=2.3.1.-;
GN Name=Acnat1 {ECO:0000312|MGI:MGI:2140197};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABE98441.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=129/Sv {ECO:0000312|EMBL:ABE98441.1};
RX PubMed=17116739; DOI=10.1096/fj.06-6919com;
RA Reilly S.-J., O'Shea E.M., Andersson U., O'Byrne J., Alexson S.E.H.,
RA Hunt M.C.;
RT "A peroxisomal acyltransferase in mouse identifies a novel pathway for
RT taurine conjugation of fatty acids.";
RL FASEB J. 21:99-107(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acyltransferase which efficiently conjugates very long-chain
CC and long-chain fatty acids to taurine (PubMed:17116739). Shows no
CC conjugation activity in the presence of glycine (PubMed:17116739).
CC {ECO:0000269|PubMed:17116739}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurine + tetracosanoyl-CoA = CoA + H(+) + N-tetracosanoyl-
CC taurine; Xref=Rhea:RHEA:50120, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:132049, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + taurine = CoA + H(+) + N-eicosanoyl-taurine;
CC Xref=Rhea:RHEA:50116, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57380, ChEBI:CHEBI:132048, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + taurine = CoA + H(+) + N-octadecanoyl-
CC taurine; Xref=Rhea:RHEA:50112, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:132047, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + taurine = CoA + H(+) + N-hexadecanoyl-
CC taurine; Xref=Rhea:RHEA:50108, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:132045, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=taurine + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoyl-
CC taurine; Xref=Rhea:RHEA:50104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:132043, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + taurine = CoA + H(+) + N-dodecanoyl-taurine;
CC Xref=Rhea:RHEA:50100, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:132042, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000269|PubMed:17116739};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for C16:0-coenzyme A {ECO:0000269|PubMed:17116739};
CC Vmax=159.5 nmol/min/mg enzyme {ECO:0000269|PubMed:17116739};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17116739}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:17116739};
CC IsoId=A2AKK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AKK5-2; Sequence=VSP_052953;
CC -!- TISSUE SPECIFICITY: Expressed mainly in liver and kidney with low
CC levels in adrenal and little or no expression in other tissues.
CC {ECO:0000269|PubMed:17116739}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000255}.
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DR EMBL; DQ469311; ABE98441.1; -; mRNA.
DR EMBL; AL772310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51174.1; -. [A2AKK5-1]
DR RefSeq; NP_001158037.1; NM_001164565.1. [A2AKK5-1]
DR RefSeq; XP_006537905.1; XM_006537842.3. [A2AKK5-1]
DR RefSeq; XP_006537906.1; XM_006537843.3. [A2AKK5-1]
DR RefSeq; XP_011248303.1; XM_011250001.2.
DR RefSeq; XP_011248304.1; XM_011250002.2. [A2AKK5-1]
DR RefSeq; XP_011248305.1; XM_011250003.2. [A2AKK5-1]
DR RefSeq; XP_011248306.1; XM_011250004.2. [A2AKK5-1]
DR RefSeq; XP_011248307.1; XM_011250005.2. [A2AKK5-1]
DR AlphaFoldDB; A2AKK5; -.
DR SMR; A2AKK5; -.
DR BioGRID; 230942; 1.
DR STRING; 10090.ENSMUSP00000092702; -.
DR SwissLipids; SLP:000001601; -. [A2AKK5-1]
DR ESTHER; mouse-acnt1; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A49; -.
DR iPTMnet; A2AKK5; -.
DR PhosphoSitePlus; A2AKK5; -.
DR jPOST; A2AKK5; -.
DR MaxQB; A2AKK5; -.
DR PaxDb; A2AKK5; -.
DR PeptideAtlas; A2AKK5; -.
DR PRIDE; A2AKK5; -.
DR ProteomicsDB; 285589; -. [A2AKK5-1]
DR ProteomicsDB; 285590; -. [A2AKK5-2]
DR Ensembl; ENSMUST00000095086; ENSMUSP00000092702; ENSMUSG00000070985. [A2AKK5-1]
DR Ensembl; ENSMUST00000107697; ENSMUSP00000103325; ENSMUSG00000070985. [A2AKK5-2]
DR GeneID; 230161; -.
DR KEGG; mmu:230161; -.
DR UCSC; uc008svr.2; mouse. [A2AKK5-1]
DR CTD; 230161; -.
DR MGI; MGI:2140197; Acnat1.
DR VEuPathDB; HostDB:ENSMUSG00000070985; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; A2AKK5; -.
DR OMA; VPLRYKD; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; A2AKK5; -.
DR TreeFam; TF314911; -.
DR SABIO-RK; A2AKK5; -.
DR BioGRID-ORCS; 230161; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Acnat1; mouse.
DR PRO; PR:A2AKK5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AKK5; protein.
DR Bgee; ENSMUSG00000070985; Expressed in liver and 34 other tissues.
DR ExpressionAtlas; A2AKK5; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Fatty acid metabolism;
KW Lipid metabolism; Peroxisome; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..416
FT /note="Acyl-coenzyme A amino acid N-acyltransferase 1"
FT /id="PRO_0000352774"
FT MOTIF 414..416
FT /note="Microbody targeting signal"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 359
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63276"
FT VAR_SEQ 156..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_052953"
FT CONFLICT 4
FT /note="K -> Q (in Ref. 1; ABE98441)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="F -> L (in Ref. 1; ABE98441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46071 MW; EA313ED0782260F4 CRC64;
MMIKLIATPS NALVDEPVSI RATGLPPSQI VTIKATVKDE NDNVFQSQAF YKTNEAGEVD
LEKTPALGGD YVGVHPMGLF FSLKPKKAFH RLMKKDVMNS PFCICLDLYD SVNWLETVRI
PSKASQRVQR WFVGPGVKRE QIQEGRVRGA LFLPPGKGPF PGIIDLFGVI GGLVEFRASL
LASHGFAVLA LAYFAYKDLP EKLQEVDLEY FEEAANFLLS HPKIQQPGIG VISTSKGAEI
GLAMACYLKQ VIATVCINGA TTTTAVPLRY QDLVVTPIQQ ALERMEVHVS GAVCFRHTTQ
YLQNKNILPV EKAQGKILFI VGENDELLDS KLHAQRAMDR LRRHGRSSGR MLAYPGAGHL
IEPPYSPLCF ASWQPVLGRP MCFGGDLMAH AAAQEHSWRE IQKFFRKHLL QSGSKL
