ID   ACOT4_MOUSE             Reviewed;         421 AA.
AC   Q8BWN8; Q8BJQ1; Q8BL20; Q9QYR8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Acyl-coenzyme A thioesterase 4;
DE            Short=Acyl-CoA thioesterase 4;
DE            EC=3.1.2.2;
DE   AltName: Full=Peroxisomal acyl coenzyme A thioester hydrolase Ib;
DE   AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase Ib;
DE            Short=PTE-Ib;
DE   AltName: Full=PTE-2b;
GN   Name=Acot4; Synonyms=Pte1b, Pte2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=20036578; PubMed=10567408; DOI=10.1074/jbc.274.48.34317;
RA   Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T.,
RA   Alexson S.E.H.;
RT   "Peroxisome proliferator-induced long chain acyl-CoA thioesterases
RT   comprise a highly conserved novel multi-gene family involved in lipid
RT   metabolism.";
RL   J. Biol. Chem. 274:34317-34326(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Liver;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
CC       catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
CC       coenzyme A (CoASH), providing the potential to regulate
CC       intracellular levels of acyl-CoAs, free fatty acids and CoASH (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, intestine, adrenal
CC       gland and white and brown tissues. Not detected in other tissues.
CC   -!- INDUCTION: In the liver, by peroxisome proliferator (Clofibrate)
CC       treatment, via the peroxisome proliferator-activated receptors
CC       (PPARs) or fasting for 24 hours.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
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DR   EMBL; AF180801; AAF13872.1; -; Genomic_DNA.
DR   EMBL; AF180799; AAF13872.1; JOINED; Genomic_DNA.
DR   EMBL; AF180800; AAF13872.1; JOINED; Genomic_DNA.
DR   EMBL; AK046630; BAC32814.1; -; mRNA.
DR   EMBL; AK050420; BAC34246.1; -; mRNA.
DR   EMBL; AK080883; BAC38060.1; -; mRNA.
DR   IPI; IPI00308769; -.
DR   RefSeq; NP_599008.2; -.
DR   UniGene; Mm.475660; -.
DR   PhosphoSite; Q8BWN8; -.
DR   Ensembl; ENSMUSG00000052392; Mus musculus.
DR   GeneID; 171282; -.
DR   KEGG; mmu:171282; -.
DR   MGI; MGI:2159621; Acot4.
DR   HOGENOM; Q8BWN8; -.
DR   HOVERGEN; Q8BWN8; -.
DR   OMA; Q8BWN8; PSMIPIE.
DR   BRENDA; 3.1.2.2; 244.
DR   NextBio; 370951; -.
DR   ArrayExpress; Q8BWN8; -.
DR   Bgee; Q8BWN8; -.
DR   CleanEx; MM_ACOT4; -.
DR   GermOnline; ENSMUSG00000052392; Mus musculus.
DR   GO; GO:0005777; C:peroxisome; IDA:HGNC.
DR   GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:EC.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; IDA:HGNC.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA:HGNC.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:HGNC.
DR   InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR   InterPro; IPR014940; BAAT_C.
DR   InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR   Pfam; PF08840; BAAT_C; 1.
DR   Pfam; PF04775; Bile_Hydr_Trans; 1.
DR   PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Peroxisome; Serine esterase.
FT   CHAIN         1    421       Acyl-coenzyme A thioesterase 4.
FT                                /FTId=PRO_0000202150.
FT   MOTIF       419    421       Microbody targeting signal (Potential).
FT   ACT_SITE    232    232       Charge relay system (By similarity).
FT   ACT_SITE    326    326       Charge relay system (By similarity).
FT   ACT_SITE    360    360       Charge relay system (By similarity).
FT   CONFLICT     87     87       D -> N (in Ref. 2; BAC32814).
FT   CONFLICT    136    136       R -> G (in Ref. 1; AAF13872).
FT   CONFLICT    215    215       M -> K (in Ref. 2; BAC38060).
SQ   SEQUENCE   421 AA;  46481 MW;  93DB75F0191D49F7 CRC64;
     MAATLSVEPT GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA RYRADSHGEL
     DLARVPALGG SFSGLEPMGL LWAMEPDRPF WRLIKRDVQT PFLVELEVLD GHEPDGGRRL
     ARTVHERHFM APGVRRVPVR EGRVRATLFL PPGQGPFPGI IDVYGVGGGL LEYRAGLVAG
     HGFATLALAF YDFEDLPKEL NVIEVDYFEE AVRYMLRHPK VKGPDIGLLG LSLGADVCLI
     MASFLNNVSA TVSINGSAFS GNRHIKYKQT MIPPLGHDLR RMKVAFSGIL DIVDIRNDAV
     GGCENPSMIP IEKAKGPILF VAGQDDHCWR SELYTQIASD RLQAHGKERP QVLSYPGTGH
     YIEPPYFPMC PASLHKIVNE AVIWGGEVKA HSKAQIDAWK QILFFFGKHL GSTHSRASCR
     L
//