ID   ACOT4_HUMAN             Reviewed;         421 AA.
AC   Q8N9L9; Q17RF4; Q5BKT6; Q86TX0; Q86TX1; Q96N88;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   16-JUN-2009, entry version 54.
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=PTE2B, PTEIB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum, and Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuroblastoma, and Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-57.
RC   TISSUE=Colon, and Urinary bladder;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK094223; BAC04313.1; -; mRNA.
DR   EMBL; AK055797; BAB71017.1; -; mRNA.
DR   EMBL; BX248023; CAD62346.1; -; mRNA.
DR   EMBL; BX248047; CAD62354.1; -; mRNA.
DR   EMBL; BC031799; AAH31799.2; -; mRNA.
DR   EMBL; BC090945; AAH90945.1; -; mRNA.
DR   EMBL; BC117341; AAI17342.1; -; mRNA.
DR   EMBL; BC117343; AAI17344.1; -; mRNA.
DR   IPI; IPI00171211; -.
DR   RefSeq; NP_689544.3; -.
DR   UniGene; Hs.49433; -.
DR   PhosphoSite; Q8N9L9; -.
DR   PRIDE; Q8N9L9; -.
DR   Ensembl; ENSG00000177465; Homo sapiens.
DR   GeneID; 122970; -.
DR   KEGG; hsa:122970; -.
DR   GeneCards; GC14P073129; -.
DR   HGNC; HGNC:19748; ACOT4.
DR   HPA; HPA000779; -.
DR   PharmGKB; PA142672654; -.
DR   HOGENOM; Q8N9L9; -.
DR   HOVERGEN; Q8N9L9; -.
DR   OMA; Q8N9L9; PSMIPIE.
DR   BRENDA; 3.1.2.2; 247.
DR   NextBio; 81045; -.
DR   ArrayExpress; Q8N9L9; -.
DR   Bgee; Q8N9L9; -.
DR   CleanEx; HS_ACOT4; -.
DR   GermOnline; ENSG00000177465; Homo sapiens.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
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:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC.
DR   GO; GO:0032788; P:saturated monocarboxylic acid metabolic pro...; 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   GO; GO:0032789; P:unsaturated monocarboxylic acid metabolic p...; IDA:HGNC.
DR   GO; GO:0000038; P:very-long-chain fatty acid 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; Polymorphism; Serine esterase.
FT   CHAIN         1    421       Acyl-coenzyme A thioesterase 4.
FT                                /FTId=PRO_0000202149.
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   VARIANT      57     57       R -> C (in dbSNP:rs3742819).
FT                                /FTId=VAR_052300.
FT   VARIANT     187    187       A -> D (in dbSNP:rs35724886).
FT                                /FTId=VAR_052301.
FT   CONFLICT    130    130       L -> P (in Ref. 1; BAC04313).
FT   CONFLICT    187    190       ALAY -> DLQS (in Ref. 1; BAC04313).
SQ   SEQUENCE   421 AA;  46327 MW;  41BBE5AA826A9F2C CRC64;
     MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA RYCADARGEL
     DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI PFVVELEVLD GHDPEPGRLL
     CQAQHERHFL PPGVRRQSVR AGRVRATLFL PPGPGPFPGI IDIFGIGGGL LEYRASLLAG
     HGFATLALAY YNFEDLPNNM DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS
     MASFLKNVSA TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV
     GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP QIICYPGTGH
     YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK QILAFFCKHL GGTQKTAVPK
     L
//