ACNT2_MOUSE
ID ACNT2_MOUSE Reviewed; 420 AA.
AC Q8BGG9; B2D099; Q91XC7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acyl-coenzyme A amino acid N-acyltransferase 2 {ECO:0000303|Ref.1};
DE EC=2.3.1.-;
GN Name=Acnat2 {ECO:0000312|EMBL:ACB55609.1};
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:ACB55609.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Sv {ECO:0000312|EMBL:ACB55609.1};
RA Reilly S.-J., Alexson S.E.H., Hunt M.C.;
RT "Identification and characterization of a novel peroxisomal acyl-CoA:amino
RT acid N-acyltransferase (Acnat2).";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC34180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC34180.1};
RC TISSUE=Liver tumor {ECO:0000312|EMBL:BAC34180.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH10829.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10829.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH10829.1};
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).
RN [5]
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. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|Ref.1};
CC IsoId=Q8BGG9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8BGG9-2; Sequence=VSP_052954;
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10829.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM27903.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EU564338; ACB55609.1; -; mRNA.
DR EMBL; AK050308; BAC34180.1; -; mRNA.
DR EMBL; AK050357; BAC34207.1; -; mRNA.
DR EMBL; BX537352; CAM27903.3; ALT_INIT; Genomic_DNA.
DR EMBL; BX537352; CAM27904.1; -; Genomic_DNA.
DR EMBL; BC010829; AAH10829.1; ALT_INIT; mRNA.
DR CCDS; CCDS18171.1; -. [Q8BGG9-1]
DR RefSeq; NP_663343.2; NM_145368.2. [Q8BGG9-1]
DR RefSeq; XP_006537789.1; XM_006537726.2.
DR RefSeq; XP_011248270.1; XM_011249968.1.
DR AlphaFoldDB; Q8BGG9; -.
DR SMR; Q8BGG9; -.
DR STRING; 10090.ENSMUSP00000080256; -.
DR ESTHER; mouse-Q8BGG9; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A50; -.
DR iPTMnet; Q8BGG9; -.
DR PhosphoSitePlus; Q8BGG9; -.
DR jPOST; Q8BGG9; -.
DR MaxQB; Q8BGG9; -.
DR PaxDb; Q8BGG9; -.
DR PeptideAtlas; Q8BGG9; -.
DR PRIDE; Q8BGG9; -.
DR ProteomicsDB; 285840; -. [Q8BGG9-1]
DR ProteomicsDB; 285841; -. [Q8BGG9-2]
DR DNASU; 209186; -.
DR Ensembl; ENSMUST00000081541; ENSMUSP00000080256; ENSMUSG00000060317. [Q8BGG9-1]
DR Ensembl; ENSMUST00000107698; ENSMUSP00000103326; ENSMUSG00000060317. [Q8BGG9-2]
DR GeneID; 209186; -.
DR KEGG; mmu:209186; -.
DR UCSC; uc008svq.1; mouse. [Q8BGG9-1]
DR UCSC; uc012deb.1; mouse. [Q8BGG9-2]
DR CTD; 209186; -.
DR MGI; MGI:2444345; Acnat2.
DR VEuPathDB; HostDB:ENSMUSG00000060317; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q8BGG9; -.
DR OMA; FANVENQ; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q8BGG9; -.
DR TreeFam; TF314911; -.
DR BioGRID-ORCS; 209186; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Acnat2; mouse.
DR PRO; PR:Q8BGG9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BGG9; protein.
DR Bgee; ENSMUSG00000060317; Expressed in right kidney and 16 other tissues.
DR ExpressionAtlas; Q8BGG9; baseline and differential.
DR Genevisible; Q8BGG9; MM.
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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Fatty acid metabolism;
KW Lipid metabolism; Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Acyl-coenzyme A amino acid N-acyltransferase 2"
FT /id="PRO_0000352775"
FT MOTIF 418..420
FT /note="Microbody targeting signal"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 329
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O55137"
FT VAR_SEQ 156..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052954"
FT CONFLICT 244
FT /note="M -> K (in Ref. 1; ACB55609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46595 MW; 9ACD12AB4FD73452 CRC64;
MMIQLIATPS NALVDEPVSI RATGLPPSQI VTIKATVKDE NDNVFQSQAF YKTNEAGEVD
LEKTPALGGD YVGVHPMGLF FSLKPKKAFH RLMKKDVMNS PLCICLDLYD SVNWLETVRI
PSKASQRVQR WFVGPGVKRE QIQEGRVRGA LFLPPGKGPF PGIIDLFGLI GGLVEFRASL
LASHGFAVLA LAYFAYEDLP EKPQEVDLEY FEEAANFLLS HPKIQQPGIG VISTSKGAEI
GLAMACYLKQ VIATVCINGP TTITIFPLRY QDLVMTPIHP ALERIQVHDS GALLFRYTTQ
YLHNKLNSQN ILPVEKAQGK ILFIVGENDE CLDSKLHAQK AMDRLQRHGR SSGRMLAYPG
AGHLIEPPYS PVCFVAWFPV LGQPMCFGGD LMAHAAAQEH SWREIQKFFR KHLLQSGSKL
