ACNT2_RAT
ID ACNT2_RAT Reviewed; 418 AA.
AC Q5FVR5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Acyl-coenzyme A amino acid N-acyltransferase 2 {ECO:0000250|UniProtKB:Q8BGG9};
DE EC=2.3.1.-;
GN Name=Acnat2 {ECO:0000250|UniProtKB:Q8BGG9};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH89827.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:AAH89827.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acyltransferase which efficiently conjugates very long-chain
CC and long-chain fatty acids to taurine. Shows no conjugation activity in
CC the presence of glycine (By similarity).
CC {ECO:0000250|UniProtKB:A2AKK5}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:A2AKK5}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000255}.
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DR EMBL; BC089827; AAH89827.1; -; mRNA.
DR RefSeq; NP_001014085.1; NM_001014063.1.
DR AlphaFoldDB; Q5FVR5; -.
DR SMR; Q5FVR5; -.
DR STRING; 10116.ENSRNOP00000056642; -.
DR ESTHER; ratno-q5fvr5; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A50; -.
DR iPTMnet; Q5FVR5; -.
DR PhosphoSitePlus; Q5FVR5; -.
DR PaxDb; Q5FVR5; -.
DR PRIDE; Q5FVR5; -.
DR GeneID; 313220; -.
DR KEGG; rno:313220; -.
DR UCSC; RGD:1359532; rat.
DR CTD; 209186; -.
DR RGD; 1359532; Acnat2.
DR VEuPathDB; HostDB:ENSRNOG00000051912; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q5FVR5; -.
DR OMA; FANVENQ; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q5FVR5; -.
DR TreeFam; TF314911; -.
DR PRO; PR:Q5FVR5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000051912; Expressed in liver and 1 other tissue.
DR ExpressionAtlas; Q5FVR5; baseline.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0016410; F:N-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS: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 2: Evidence at transcript level;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism; Peroxisome;
KW Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="Acyl-coenzyme A amino acid N-acyltransferase 2"
FT /id="PRO_0000352776"
FT MOTIF 416..418
FT /note="Microbody targeting signal"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 361
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
SQ SEQUENCE 418 AA; 46011 MW; 72297A19BE58CF00 CRC64;
MLQLIATPSN ALADEPVSIR AIGLPPSQIV TITATVKDEK ENLFQSKAFY KANEAGEVDL
EQASALGGDY VGVHPMGLFC CLKPKRAFQR LIKKDVMNSP LCICLDLYDS VCWLETVRIP
PKASQIVHRW FAGPGVKREQ IREGRVRGAL FLPPGKGPFP GIIDLFGSIG GLVEFRASLL
ASRGFAVLAL AYFAYEDLPK VLLEEDLDYF EEAANFLLAH PKIQQPGIGV ISVSKGAEIG
LAMACYLKQV VATVCINGPS AIFDFPLKYR DLVVTPMRLA FEKIQFHGSG AACFRHCWDP
QNMLNPPKIL PVEKAQGKIL FIVGENDQCL ASKLHAQRAM DRLRSHGRSS GRMLAYPGAG
HLIEPPYSPF CFACWDSVLG KPMLWGGDPI AHAAAQVHSW REIQKFFRQH LLQSGGKL