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Acyl-coenzyme A thioesterase 4 (Acyl-CoA thioesterase 4) (EC 3.1.2.2) (PTE-2b) (Peroxisomal acyl coenzyme A thioester hydrolase Ib) (Peroxisomal long-chain acyl-CoA thioesterase Ib) (PTE-Ib)

 ACOT4_HUMAN             Reviewed;         421 AA.
Q8N9L9; Q17RF4; Q5BKT6; Q86TX0; Q86TX1; Q96N88;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
27-SEP-2017, entry version 127.
RecName: Full=Acyl-coenzyme A thioesterase 4;
Short=Acyl-CoA thioesterase 4;
EC=3.1.2.2 {ECO:0000269|PubMed:16940157};
AltName: Full=PTE-2b;
AltName: Full=Peroxisomal acyl coenzyme A thioester hydrolase Ib;
AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase Ib;
Short=PTE-Ib;
Name=ACOT4; Synonyms=PTE2B, PTEIB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neuroblastoma, and Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-57.
TISSUE=Colon, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16940157; DOI=10.1096/fj.06-6042com;
Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.;
"Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene
clusters shows that convergent, functional evolution results in a
reduced number of human peroxisomal ACOTs.";
FASEB J. 20:1855-1864(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[6]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
Siponen M.I., Moche M., Arrowsmith C.H., Berglund H., Bountra C.,
Collins R., Edwards A.M., Flodin S., Flores A., Graslund S.,
Hammarstrom M., Johansson A., Johansson I., Kallas A., Karlberg T.,
Kraulis P., Kotenyova T., Kotzsch A., Markova N., Nielsen T.K.,
Nordlund P., Nyman T., Persson C., Roos A.K., Schutz P., Svensson L.,
Thorsell A.G., Tresaugues L., Van Den Berg S., Wahlberg E.,
Weigelt J., Welin M., Wisniewska M., Schuler H.;
"Human Acyl-coenzyme A thioesterase 4.";
Submitted (SEP-2009) to the PDB data bank.
-!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
coenzyme A (CoASH), providing the potential to regulate
intracellular levels of acyl-CoAs, free fatty acids and CoASH (By
similarity). Succinyl-CoA thioesterase that also hydrolyzes long
chain saturated and unsaturated monocarboxylic acyl-CoAs.
{ECO:0000250, ECO:0000269|PubMed:16940157}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
{ECO:0000269|PubMed:16940157}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for succinyl-CoA {ECO:0000269|PubMed:16940157};
KM=147 uM for glutaryl-CoA {ECO:0000269|PubMed:16940157};
KM=3.4 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157};
Vmax=581 nmol/min/mg enzyme toward succinyl-CoA
{ECO:0000269|PubMed:16940157};
Vmax=132 nmol/min/mg enzyme toward glutaryl-CoA
{ECO:0000269|PubMed:16940157};
Vmax=137 nmol/min/mg enzyme toward C14-acyl-CoA
{ECO:0000269|PubMed:16940157};
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16940157}.
-!- TISSUE SPECIFICITY: Strongest expression in liver and kidney and
weaker expression in placenta, heart, and muscle.
{ECO:0000269|PubMed:16940157}.
-!- MISCELLANEOUS: Human ACOT4 may have acquired the combined
activities of mouse ACOT3, ACOT4, and ACOT5.
-!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
{ECO:0000305}.
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EMBL; AK094223; BAC04313.1; -; mRNA.
EMBL; AK055797; BAB71017.1; -; mRNA.
EMBL; BX248023; CAD62346.1; -; mRNA.
EMBL; BX248047; CAD62354.1; -; mRNA.
EMBL; BC031799; AAH31799.2; -; mRNA.
EMBL; BC090945; AAH90945.1; -; mRNA.
EMBL; BC117341; AAI17342.1; -; mRNA.
EMBL; BC117343; AAI17344.1; -; mRNA.
CCDS; CCDS9817.1; -.
RefSeq; NP_689544.3; NM_152331.3.
UniGene; Hs.49433; -.
PDB; 3K2I; X-ray; 2.40 A; A/B=1-421.
PDBsum; 3K2I; -.
ProteinModelPortal; Q8N9L9; -.
SMR; Q8N9L9; -.
BioGrid; 125809; 1.
STRING; 9606.ENSP00000323071; -.
SwissLipids; SLP:000000592; -.
ESTHER; human-ACOT4; Acyl-CoA_Thioesterase.
MEROPS; S09.943; -.
PhosphoSitePlus; Q8N9L9; -.
BioMuta; ACOT4; -.
DMDM; 50401071; -.
EPD; Q8N9L9; -.
MaxQB; Q8N9L9; -.
PaxDb; Q8N9L9; -.
PeptideAtlas; Q8N9L9; -.
PRIDE; Q8N9L9; -.
DNASU; 122970; -.
Ensembl; ENST00000326303; ENSP00000323071; ENSG00000177465.
GeneID; 122970; -.
KEGG; hsa:122970; -.
UCSC; uc001xoo.4; human.
CTD; 122970; -.
DisGeNET; 122970; -.
EuPathDB; HostDB:ENSG00000177465.4; -.
GeneCards; ACOT4; -.
H-InvDB; HIX0202062; -.
HGNC; HGNC:19748; ACOT4.
HPA; HPA000779; -.
MIM; 614314; gene.
neXtProt; NX_Q8N9L9; -.
OpenTargets; ENSG00000177465; -.
PharmGKB; PA142672654; -.
eggNOG; ENOG410II3X; Eukaryota.
eggNOG; COG1073; LUCA.
GeneTree; ENSGT00390000001046; -.
HOGENOM; HOG000116219; -.
HOVERGEN; HBG000331; -.
InParanoid; Q8N9L9; -.
KO; K01068; -.
OMA; SMIPIEK; -.
OrthoDB; EOG091G08KU; -.
PhylomeDB; Q8N9L9; -.
TreeFam; TF314911; -.
BioCyc; MetaCyc:HS16863-MONOMER; -.
Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
SABIO-RK; Q8N9L9; -.
EvolutionaryTrace; Q8N9L9; -.
GeneWiki; ACOT4; -.
GenomeRNAi; 122970; -.
PRO; PR:Q8N9L9; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000177465; -.
CleanEx; HS_ACOT4; -.
Genevisible; Q8N9L9; HS.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004778; F:succinyl-CoA hydrolase activity; IDA:UniProtKB.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC.
GO; GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
GO; GO:0043648; P:dicarboxylic acid metabolic process; IDA:HGNC.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC.
GO; GO:0032788; P:saturated monocarboxylic acid metabolic process; IDA:HGNC.
GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA:HGNC.
GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:HGNC.
GO; GO:0032789; P:unsaturated monocarboxylic acid metabolic process; IDA:HGNC.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
InterPro; IPR014940; BAAT_C.
InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
Pfam; PF08840; BAAT_C; 1.
Pfam; PF04775; Bile_Hydr_Trans; 1.
PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
SUPFAM; SSF53474; SSF53474; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Hydrolase; Peroxisome;
Polymorphism; Reference proteome; Serine esterase.
CHAIN 1 421 Acyl-coenzyme A thioesterase 4.
/FTId=PRO_0000202149.
MOTIF 419 421 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 232 232 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
ACT_SITE 326 326 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
ACT_SITE 360 360 Charge relay system.
{ECO:0000250|UniProtKB:P49753}.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9QYR9}.
MOD_RES 313 313 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BWN8}.
MOD_RES 408 408 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QYR9}.
VARIANT 57 57 R -> C (in dbSNP:rs3742819).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_052300.
VARIANT 187 187 A -> D (in dbSNP:rs35724886).
/FTId=VAR_052301.
CONFLICT 130 130 L -> P (in Ref. 1; BAC04313).
{ECO:0000305}.
CONFLICT 187 190 ALAY -> DLQS (in Ref. 1; BAC04313).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:3K2I}.
STRAND 20 25 {ECO:0000244|PDB:3K2I}.
STRAND 31 39 {ECO:0000244|PDB:3K2I}.
STRAND 45 53 {ECO:0000244|PDB:3K2I}.
TURN 62 64 {ECO:0000244|PDB:3K2I}.
STRAND 69 72 {ECO:0000244|PDB:3K2I}.
HELIX 79 82 {ECO:0000244|PDB:3K2I}.
STRAND 85 88 {ECO:0000244|PDB:3K2I}.
STRAND 102 112 {ECO:0000244|PDB:3K2I}.
STRAND 119 130 {ECO:0000244|PDB:3K2I}.
STRAND 135 141 {ECO:0000244|PDB:3K2I}.
STRAND 144 150 {ECO:0000244|PDB:3K2I}.
STRAND 152 154 {ECO:0000244|PDB:3K2I}.
STRAND 159 163 {ECO:0000244|PDB:3K2I}.
HELIX 173 179 {ECO:0000244|PDB:3K2I}.
TURN 180 182 {ECO:0000244|PDB:3K2I}.
STRAND 184 189 {ECO:0000244|PDB:3K2I}.
STRAND 191 193 {ECO:0000244|PDB:3K2I}.
HELIX 206 216 {ECO:0000244|PDB:3K2I}.
STRAND 224 231 {ECO:0000244|PDB:3K2I}.
HELIX 233 244 {ECO:0000244|PDB:3K2I}.
STRAND 246 255 {ECO:0000244|PDB:3K2I}.
STRAND 265 267 {ECO:0000244|PDB:3K2I}.
STRAND 270 272 {ECO:0000244|PDB:3K2I}.
HELIX 279 281 {ECO:0000244|PDB:3K2I}.
HELIX 302 304 {ECO:0000244|PDB:3K2I}.
HELIX 311 313 {ECO:0000244|PDB:3K2I}.
STRAND 318 323 {ECO:0000244|PDB:3K2I}.
STRAND 327 329 {ECO:0000244|PDB:3K2I}.
HELIX 331 344 {ECO:0000244|PDB:3K2I}.
STRAND 351 355 {ECO:0000244|PDB:3K2I}.
STRAND 372 375 {ECO:0000244|PDB:3K2I}.
TURN 376 379 {ECO:0000244|PDB:3K2I}.
STRAND 380 383 {ECO:0000244|PDB:3K2I}.
HELIX 388 409 {ECO:0000244|PDB:3K2I}.
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


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