Reviewed, UniProtKB/Swiss-Prot Q8WXI4 (ACO11_HUMAN)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A thioesterase 11
      Short name=Acyl-CoA thioesterase 11
    EC=3.1.2.-
Alternative name(s):
    Acyl-CoA thioester hydrolase 11
    Brown fat-inducible thioesterase
      Short name=BFIT
    Adipose-associated thioesterase

Gene names

Name:	ACOT11
Synonyms:	BFIT, KIAA0707, THEA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Hydrolase Serine esterase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Ref.1 Non-traceable author statement. Source: UniProtKB intracellular signaling cascade Ref.1 Non-traceable author statement. Source: UniProtKB response to cold Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	acyl-CoA thioesterase activity Ref.1 Traceable author statement. Source: UniProtKB carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 607

607

Acyl-coenzyme A thioesterase 11

PRO_0000053813

Regions

Domain

29 – 164

136

Acyl coenzyme A hydrolase 1

Domain

205 – 336

132

Acyl coenzyme A hydrolase 2

Domain

375 – 585

211

START

Region

91 – 93

3

Coenzyme A binding By similarity

Region

120 – 122

3

Coenzyme A binding By similarity

Region

271 – 273

3

Coenzyme A binding By similarity

Sites

Binding site

181

1

Coenzyme A By similarity

Amino acid modifications

Modified residue

367

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

544 – 607

64

CCWVR…YLQDT → VSYYNQATPGVLNYVTTNVA GLSSEFYTTFKACEQFLLDN RNDLAPSLQTL in isoform 2.

VSP_000160

Natural variant

11

1

R → W: dbSNP rs34630746.

VAR_048190

Natural variant

165

1

P → L: dbSNP rs2304306.

VAR_022119

Natural variant

202

1

G → D: dbSNP rs1702003. Ref.4

VAR_022120

Natural variant

212

1

M → I: dbSNP rs2304305.

VAR_022121

Natural variant

536

1

R → H: dbSNP rs12403630.

VAR_048191

Experimental info

Sequence conflict

255

1

S → R in AAH01517. Ref.7

Sequence conflict

348

1

R → W in BAD97290. Ref.4

Secondary structure

1

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607

Helix Strand Turn

Details...

Helix

347 – 363

17

Turn

370 – 372

3

Beta strand

375 – 378

4

Helix

381 – 383

3

Helix

384 – 399

16

Beta strand

405 – 410

6

Beta strand

413 – 419

7

Beta strand

424 – 434

11

Helix

436 – 444

9

Helix

446 – 451

6

Beta strand

458 – 466

9

Beta strand

469 – 476

8

Beta strand

486 – 495

10

Beta strand

504 – 512

9

Beta strand

532 – 536

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BFIT1) [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 12F2BCAB8AAC18EC	FASTA	607	68,492
	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
	Isoform 2 (BFIT2). Checksum: C9CD42FB285A8B53	FASTA	594	67,152
	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 LTKVSYYNQA TPGVLNYVTT NVAGLSSEFY TTFKACEQFL LDNRNDLAPS LQTL

References

	« Hide 'large scale' referencesShow '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: 11696000] [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: 9734811] [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. , 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: 14702039] [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. , 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: 16710414] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Skin.
[8]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, MASS SPECTROMETRY.
[9]	"Human start domain of acyl-coenzyme a thioesterase 11 (acot11)." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 339-543.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC001517 mRNA. Translation: AAH01517.1.
BC093844 mRNA. Translation: AAH93844.1.
BC093846 mRNA. Translation: AAH93846.1.

IPI

IPI00220903.
IPI00305894.

PIR

T00351.

RefSeq

NP_056362.1.
NP_671517.1.

UniGene

Hs.234786

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FO5	X-ray	2.00	A/B	339-543	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q8WXI4.

Proteomic databases

PRIDE

Q8WXI4.

Genome annotation databases

Ensembl

ENST00000371316; ENSP00000360366; ENSG00000162390; Homo sapiens. [Genome view]

GeneID

26027.

KEGG

hsa:26027.

UCSC

uc001cxl.1. human.
uc001cxm.1. human.

Organism-specific databases

CTD

26027.

GeneCards

GC01P054786.

HGNC

HGNC:18156. ACOT11.

MIM

606803. gene.

PharmGKB

PA38303.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q8WXI4.

HOVERGEN

Q8WXI4.

OMA

VSCKQTE

OrthoDB

EOG9CJZ2N

Gene expression databases

ArrayExpress

Q8WXI4.

Bgee

Q8WXI4.

CleanEx

HS_ACOT11.

Genevestigator

Q8WXI4.

GermOnline

ENSG00000162390. Homo sapiens.

Family and domain databases

InterPro

IPR002913. START_lipid_bd.
IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]

SMART

SM00234. START. 1 hit.
[Graphical view]

PROSITE

PS50848. START. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

47814.

SOURCE

Search...

Entry information

Entry name

ACO11_HUMAN

Accession

Primary (citable) accession number: Q8WXI4
Secondary accession number(s): B1AQ22 , O75187, Q52LP1, Q53ER9, Q96DI1, Q9H883

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	November 24, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.