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P49753

- ACOT2_HUMAN

UniProt

P49753 - ACOT2_HUMAN

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Protein

Acyl-coenzyme A thioesterase 2, mitochondrial

Gene

ACOT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Displays high levels of activity on medium- and long chain acyl CoAs.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Kineticsi

  1. KM=40.3 µM for C10-acyl-CoA1 Publication
  2. KM=8.9 µM for C12-acyl-CoA1 Publication
  3. KM=1.6 µM for C14-acyl-CoA1 Publication
  4. KM=2.0 µM for C16-acyl-CoA1 Publication
  5. KM=2.8 µM for C18-acyl-CoA1 Publication
  6. KM=4.8 µM for C20-acyl-CoA1 Publication
  7. KM=4.5 µM for C16:1-acyl-CoA1 Publication
  8. KM=6.1 µM for C18:1-acyl-CoA1 Publication
  9. KM=4.3 µM for C18:1-trans-acyl-CoA1 Publication

Vmax=212 nmol/min/mg enzyme toward C10-acyl-CoA1 Publication

Vmax=681 nmol/min/mg enzyme toward C12-acyl-CoA1 Publication

Vmax=766 nmol/min/mg enzyme toward C14-acyl-CoA1 Publication

Vmax=656 nmol/min/mg enzyme toward C16-acyl-CoA1 Publication

Vmax=488 nmol/min/mg enzyme toward C18-acyl-CoA1 Publication

Vmax=408 nmol/min/mg enzyme toward C20-acyl-CoA1 Publication

Vmax=661 nmol/min/mg enzyme toward C16:1-acyl-CoA1 Publication

Vmax=304 nmol/min/mg enzyme toward C18:1-acyl-CoA1 Publication

Vmax=418 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei294 – 2941Charge relay systemBy similarity
Active sitei388 – 3881Charge relay systemBy similarity
Active sitei422 – 4221Charge relay systemBy similarity

GO - Molecular functioni

  1. acyl-CoA hydrolase activity Source: HGNC
  2. carboxylic ester hydrolase activity Source: UniProtKB-KW
  3. palmitoyl-CoA hydrolase activity Source: UniProtKB-EC
  4. receptor binding Source: UniProtKB

GO - Biological processi

  1. acyl-CoA metabolic process Source: HGNC
  2. long-chain fatty acid metabolic process Source: HGNC
  3. very long-chain fatty acid metabolic process Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:HS04318-MONOMER.
BRENDAi3.1.2.2. 2681.
SABIO-RKP49753.

Protein family/group databases

MEROPSiS09.028.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 2, mitochondrial (EC:3.1.2.2)
Short name:
Acyl-CoA thioesterase 2
Alternative name(s):
Acyl-coenzyme A thioester hydrolase 2a
CTE-Ia
Long-chain acyl-CoA thioesterase 2
ZAP128
Gene namesi
Name:ACOT2
Synonyms:PTE2, PTE2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:18431. ACOT2.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 483Acyl-coenzyme A thioesterase 2, mitochondrialPRO_0000202147
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6-acetyllysineBy similarity
Modified residuei470 – 4701N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49753.
PRIDEiP49753.

PTM databases

PhosphoSiteiP49753.

Expressioni

Tissue specificityi

Strongest expression in heart, liver, muscle and kidney. Weak in placenta and pancreas.1 Publication

Gene expression databases

BgeeiP49753.
CleanExiHS_ACOT2.
GenevestigatoriP49753.

Organism-specific databases

HPAiHPA043705.

Interactioni

Protein-protein interaction databases

BioGridi116164. 6 interactions.
MINTiMINT-5004303.
STRINGi9606.ENSP00000238651.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 716Combined sources
Beta strandi82 – 876Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi107 – 1159Combined sources
Turni124 – 1263Combined sources
Beta strandi131 – 1333Combined sources
Helixi141 – 1444Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi164 – 17411Combined sources
Beta strandi181 – 19212Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi221 – 2255Combined sources
Helixi235 – 2417Combined sources
Turni242 – 2443Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi263 – 2664Combined sources
Helixi267 – 27812Combined sources
Beta strandi286 – 2938Combined sources
Helixi295 – 30612Combined sources
Beta strandi310 – 3178Combined sources
Beta strandi324 – 3296Combined sources
Beta strandi332 – 3343Combined sources
Helixi341 – 3433Combined sources
Beta strandi348 – 3503Combined sources
Helixi364 – 3696Combined sources
Helixi373 – 3753Combined sources
Beta strandi378 – 3858Combined sources
Helixi393 – 40614Combined sources
Beta strandi413 – 4175Combined sources
Helixi450 – 47122Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HLKX-ray2.10A/B46-483[»]
ProteinModelPortaliP49753.
SMRiP49753. Positions 57-472.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49753.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi481 – 4833Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000001046.
HOGENOMiHOG000116219.
HOVERGENiHBG000331.
InParanoidiP49753.
KOiK01068.
OMAiQWSLKSS.
PhylomeDBiP49753.
TreeFamiTF314911.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view]
PfamiPF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view]
PIRSFiPIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49753) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSNKLLSPHP HSVVLRSEFK MASSPAVLRA SRLYQWSLKS SAQFLGSPQL
60 70 80 90 100
RQVGQIIRVP ARMAATLILE PAGRCCWDEP VRIAVRGLAP EQPVTLRASL
110 120 130 140 150
RDEKGALFQA HARYRADTLG ELDLERAPAL GGSFAGLEPM GLLWALEPEK
160 170 180 190 200
PLVRLVKRDV RTPLAVELEV LDGHDPDPGR LLCQTRHERY FLPPGVRREP
210 220 230 240 250
VRVGRVRGTL FLPPEPGPFP GIVDMFGTGG GLLEYRASLL AGKGFAVMAL
260 270 280 290 300
AYYNYEDLPK TMETLHLEYF EEAMNYLLSH PEVKGPGVGL LGISKGGELC
310 320 330 340 350
LSMASFLKGI TAAVVINGSV ANVGGTLHYK GETLPPVGVN RNRIKVTKDG
360 370 380 390 400
YADIVDVLNS PLEGPDQKSF IPVERAESTF LFLVGQDDHN WKSEFYANEA
410 420 430 440 450
CKRLQAHGRR KPQIICYPET GHYIEPPYFP LCRASLHALV GSPIIWGGEP
460 470 480
RAHAMAQVDA WKQLQTFFHK HLGGHEGTIP SKV
Length:483
Mass (Da):53,218
Last modified:November 24, 2009 - v6
Checksum:iFAEDD42BBBD935E4
GO
Isoform 2 (identifier: P49753-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.
     53-214: Missing.

Show »
Length:301
Mass (Da):32,959
Checksum:iD157DF13EAF26EC6
GO

Sequence cautioni

The sequence AAC42007.1 differs from that shown. Reason: Frameshift at positions 215 and 226.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671E → V in AAZ31237. (PubMed:16940157)Curated
Sequence conflicti167 – 1671E → V in BAA91989. (PubMed:14702039)Curated
Sequence conflicti328 – 3281H → R in AAZ31237. (PubMed:16940157)Curated
Sequence conflicti328 – 3281H → R in BAA91989. (PubMed:14702039)Curated
Sequence conflicti328 – 3281H → R in BAD97355. 1 PublicationCurated
Sequence conflicti328 – 3281H → R in AAH04436. (PubMed:15489334)Curated
Sequence conflicti328 – 3281H → R in AAH06335. (PubMed:15489334)Curated
Sequence conflicti328 – 3281H → R in AAH06500. (PubMed:15489334)Curated
Sequence conflicti328 – 3281H → R in AAF97985. (PubMed:10944470)Curated
Sequence conflicti454 – 4541A → V in AAH06335. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161R → S.
Corresponds to variant rs11545741 [ dbSNP | Ensembl ].
VAR_057271
Natural varianti475 – 4751H → R.4 Publications
Corresponds to variant rs7494 [ dbSNP | Ensembl ].
VAR_016136

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform 2. 1 PublicationVSP_012225Add
BLAST
Alternative sequencei53 – 214162Missing in isoform 2. 1 PublicationVSP_012226Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40401 mRNA. Translation: AAC42007.1. Frameshift.
DQ082755 mRNA. Translation: AAZ31237.1.
AK001939 mRNA. Translation: BAA91989.1.
AK223635 mRNA. Translation: BAD97355.1.
BC004436 mRNA. Translation: AAH04436.2.
BC006335 mRNA. Translation: AAH06335.1.
BC006500 mRNA. Translation: AAH06500.4.
AY005822 mRNA. Translation: AAF97985.1.
CCDSiCCDS9816.1. [P49753-1]
PIRiJC7367.
RefSeqiNP_006812.3. NM_006821.5. [P49753-1]
UniGeneiHs.446685.

Genome annotation databases

EnsembliENST00000238651; ENSP00000238651; ENSG00000119673. [P49753-1]
ENST00000615585; ENSP00000482671; ENSG00000119673. [P49753-1]
GeneIDi10965.
KEGGihsa:10965.
UCSCiuc001xon.5. human. [P49753-1]

Polymorphism databases

DMDMi269849771.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40401 mRNA. Translation: AAC42007.1 . Frameshift.
DQ082755 mRNA. Translation: AAZ31237.1 .
AK001939 mRNA. Translation: BAA91989.1 .
AK223635 mRNA. Translation: BAD97355.1 .
BC004436 mRNA. Translation: AAH04436.2 .
BC006335 mRNA. Translation: AAH06335.1 .
BC006500 mRNA. Translation: AAH06500.4 .
AY005822 mRNA. Translation: AAF97985.1 .
CCDSi CCDS9816.1. [P49753-1 ]
PIRi JC7367.
RefSeqi NP_006812.3. NM_006821.5. [P49753-1 ]
UniGenei Hs.446685.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HLK X-ray 2.10 A/B 46-483 [» ]
ProteinModelPortali P49753.
SMRi P49753. Positions 57-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116164. 6 interactions.
MINTi MINT-5004303.
STRINGi 9606.ENSP00000238651.

Chemistry

ChEMBLi CHEMBL2189135.

Protein family/group databases

MEROPSi S09.028.

PTM databases

PhosphoSitei P49753.

Polymorphism databases

DMDMi 269849771.

Proteomic databases

MaxQBi P49753.
PRIDEi P49753.

Protocols and materials databases

DNASUi 10965.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000238651 ; ENSP00000238651 ; ENSG00000119673 . [P49753-1 ]
ENST00000615585 ; ENSP00000482671 ; ENSG00000119673 . [P49753-1 ]
GeneIDi 10965.
KEGGi hsa:10965.
UCSCi uc001xon.5. human. [P49753-1 ]

Organism-specific databases

CTDi 10965.
GeneCardsi GC14P074036.
H-InvDB HIX0011795.
HIX0172385.
HGNCi HGNC:18431. ACOT2.
HPAi HPA043705.
MIMi 609972. gene.
neXtProti NX_P49753.
PharmGKBi PA142672653.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00390000001046.
HOGENOMi HOG000116219.
HOVERGENi HBG000331.
InParanoidi P49753.
KOi K01068.
OMAi QWSLKSS.
PhylomeDBi P49753.
TreeFami TF314911.

Enzyme and pathway databases

BioCyci MetaCyc:HS04318-MONOMER.
BRENDAi 3.1.2.2. 2681.
SABIO-RK P49753.

Miscellaneous databases

EvolutionaryTracei P49753.
GeneWikii ACOT2.
GenomeRNAii 10965.
NextBioi 41670.
PROi P49753.
SOURCEi Search...

Gene expression databases

Bgeei P49753.
CleanExi HS_ACOT2.
Genevestigatori P49753.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR016662. Acyl-CoA_thioEstase_long-chain.
IPR014940. BAAT_C.
IPR006862. Thio_Ohase/aa_AcTrfase.
[Graphical view ]
Pfami PF08840. BAAT_C. 1 hit.
PF04775. Bile_Hydr_Trans. 1 hit.
[Graphical view ]
PIRSFi PIRSF016521. Acyl-CoA_hydro. 1 hit.
SUPFAMi SSF53474. SSF53474. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "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."
    Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.
    FASEB J. 20:1855-1864(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
    Tissue: Placenta.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
    Tissue: Spleen.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-475.
    Tissue: Lung and Uterus.
  6. "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase."
    Jones J.M., Gould S.J.
    Biochem. Biophys. Res. Commun. 275:233-240(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-483 (ISOFORM 1), FUNCTION, VARIANT ARG-475.

Entry informationi

Entry nameiACOT2_HUMAN
AccessioniPrimary (citable) accession number: P49753
Secondary accession number(s): Q3I5F8, Q53EK4, Q9NUX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 24, 2009
Last modified: October 29, 2014
This is version 142 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was originally (PubMed:10944470) thought to be peroxisomal but was later shown (PubMed:16940157) to be mitochondrial.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3