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Q8WXI4 (ACO11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A thioesterase 11

Short name=Acyl-CoA thioesterase 11
EC=3.1.2.-
Alternative name(s):
Acyl-CoA thioester hydrolase 11
Adipose-associated thioesterase
Brown fat-inducible thioesterase
Short name=BFIT
Gene names
Name:ACOT11
Synonyms:BFIT, KIAA0707, THEA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.

Subcellular location

Cytoplasm.

Tissue specificity

Isoform 1 is predominantly expressed in skeletal muscle, liver, testis, stomach, spleen, lung and brain. Isoform 2 is predominantly expressed in kidney, uterus, hibernoma and white adipose tissue.

Induction

By cold exposure and repressed by heat exposure.

Sequence similarities

Contains 2 acyl coenzyme A hydrolase domains.

Contains 1 START domain.

Sequence caution

The sequence BAA31682.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WXI4-1)

Also known as: BFIT1;

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.
Isoform 2 (identifier: Q8WXI4-2)

Also known as: BFIT2;

The sequence of this isoform differs from the canonical sequence as follows:
     544-607: CCWVRVSLTE...NSRFGYLQDT → VSYYNQATPG...NDLAPSLQTL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Acyl-coenzyme A thioesterase 11
PRO_0000053813

Regions

Domain29 – 164136Acyl coenzyme A hydrolase 1
Domain205 – 336132Acyl coenzyme A hydrolase 2
Domain375 – 585211START
Region91 – 933Coenzyme A binding By similarity
Region120 – 1223Coenzyme A binding By similarity
Region271 – 2733Coenzyme A binding By similarity

Sites

Binding site1811Coenzyme A By similarity

Natural variations

Alternative sequence544 – 60764CCWVR…YLQDT → VSYYNQATPGVLNYVTTNVA GLSSEFYTTFKACEQFLLDN RNDLAPSLQTL in isoform 2.
VSP_000160
Natural variant111R → W.
Corresponds to variant rs34630746 [ dbSNP | Ensembl ].
VAR_048190
Natural variant1651P → L.
Corresponds to variant rs2304306 [ dbSNP | Ensembl ].
VAR_022119
Natural variant2021G → D. Ref.4
Corresponds to variant rs1702003 [ dbSNP | Ensembl ].
VAR_022120
Natural variant2121M → I.
Corresponds to variant rs2304305 [ dbSNP | Ensembl ].
VAR_022121
Natural variant5361R → H.
Corresponds to variant rs12403630 [ dbSNP | Ensembl ].
VAR_048191

Experimental info

Sequence conflict2551S → R in AAH01517. Ref.7
Sequence conflict3481R → W in BAD97290. Ref.4

Secondary structure

.................................. 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BFIT1) [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 12F2BCAB8AAC18EC

FASTA60768,492
        10         20         30         40         50         60 
MIQNVGNHLR RGLASVFSNR TSRKSALRAG NDSAMADGEG YRNPTEVQMS QLVLPCHTNQ 

        70         80         90        100        110        120 
RGELSVGQLL KWIDTTACLS AERHAGCPCV TASMDDIYFE HTISVGQVVN IKAKVNRAFN 

       130        140        150        160        170        180 
SSMEVGIQVA SEDLCSEKQW NVCKALATFV ARREITKVKL KQITPRTEEE KMEHSVAAER 

       190        200        210        220        230        240 
RRMRLVYADT IKDLLANCAI QGDLESRDCS RMVPAEKTRV ESVELVLPPH ANHQGNTFGG 

       250        260        270        280        290        300 
QIMAWMENVA TIAASRLCRA HPTLKAIEMF HFRGPSQVGD RLVLKAIVNN AFKHSMEVGV 

       310        320        330        340        350        360 
CVEAYRQEAE THRRHINSAF MTFVVLDADD QPQLLPWIRP QPGDGERRYR EASARKKIRL 

       370        380        390        400        410        420 
DRKYIVSCKQ TEVPLSVPWD PSNQVYLSYN NVSSLKMLVA KDNWVLSSEI SQVRLYTLED 

       430        440        450        460        470        480 
DKFLSFHMEM VVHVDAAQAF LLLSDLRQRP EWDKHYRSVE LVQQVDEDDA IYHVTSPALG 

       490        500        510        520        530        540 
GHTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHRETP EYRRGETLCS GFCLWREGDQ 

       550        560        570        580        590        600 
LTKCCWVRVS LTELVSASGF YSWGLESRSK GRRSDGWNGK LAGGHLSTLK AIPVAKINSR 


FGYLQDT 

« Hide

Isoform 2 (BFIT2) [UniParc].

Checksum: C9CD42FB285A8B53
Show »

FASTA59467,152

References

« Hide 'large scale' references
[1]"BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity."
Adams S.H., Chui C., Schilbach S.L., Yu X.X., Goddard A.D., Grimaldi J.C., Lee J., Dowd P., Colman S., Lewin D.A.
Biochem. J. 360:135-142(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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 2).
Tissue: Thyroid.
[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 2), VARIANT ASP-202.
Tissue: Heart.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 2).
Tissue: Brain and Skin.
[8]"Comparative structural analysis of lipid binding START domains."
Thorsell A.G., Lee W.H., Persson C., Siponen M.I., Nilsson M., Busam R.D., Kotenyova T., Schuler H., Lehtio L.
PLoS ONE 6:E19521-E19521(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 339-543.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF416921 mRNA. Translation: AAL40937.1.
AF416922 mRNA. Translation: AAL40938.1.
AB014607 mRNA. Translation: BAA31682.1. Different initiation.
AK023937 mRNA. Translation: BAB14734.1.
AK223570 mRNA. Translation: BAD97290.1.
AL590093, AC099796 Genomic DNA. Translation: CAH71611.1.
AL590093, AC099796 Genomic DNA. Translation: CAH71612.1.
CH471059 Genomic DNA. Translation: EAX06682.1.
CH471059 Genomic DNA. Translation: EAX06683.1.
CH471059 Genomic DNA. Translation: EAX06684.1.
BC001517 mRNA. Translation: AAH01517.1.
BC093844 mRNA. Translation: AAH93844.1.
BC093846 mRNA. Translation: AAH93846.1.
PIRT00351.
RefSeqNP_056362.1. NM_015547.3.
NP_671517.1. NM_147161.3.
UniGeneHs.745173.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FO5X-ray2.00A/B339-543[»]
ProteinModelPortalQ8WXI4.
SMRQ8WXI4. Positions 46-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117495. 1 interaction.
STRING9606.ENSP00000360366.

PTM databases

PhosphoSiteQ8WXI4.

Polymorphism databases

DMDM21363000.

Proteomic databases

PaxDbQ8WXI4.
PRIDEQ8WXI4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343744; ENSP00000340260; ENSG00000162390. [Q8WXI4-2]
ENST00000371316; ENSP00000360366; ENSG00000162390. [Q8WXI4-1]
GeneID26027.
KEGGhsa:26027.
UCSCuc001cxj.2. human. [Q8WXI4-2]
uc001cxm.2. human. [Q8WXI4-1]

Organism-specific databases

CTD26027.
GeneCardsGC01P055007.
HGNCHGNC:18156. ACOT11.
HPAHPA035309.
MIM606803. gene.
neXtProtNX_Q8WXI4.
PharmGKBPA38303.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1607.
HOVERGENHBG023847.
InParanoidQ8WXI4.
KOK12417.
OMAQLTKVSY.
OrthoDBEOG70CR6C.
PhylomeDBQ8WXI4.
TreeFamTF328368.

Gene expression databases

BgeeQ8WXI4.
CleanExHS_ACOT11.
GenevestigatorQ8WXI4.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
SMARTSM00234. START. 1 hit.
[Graphical view]
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8WXI4.
GeneWikiACOT11.
GenomeRNAi26027.
NextBio47814.
PROQ8WXI4.
SOURCESearch...

Entry information

Entry nameACO11_HUMAN
AccessionPrimary (citable) accession number: Q8WXI4
Secondary accession number(s): B1AQ22 expand/collapse secondary AC list , D3DQ50, O75187, Q52LP1, Q53ER9, Q96DI1, Q9H883
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM