Q8WXI4 (ACO11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
Adipose-associated thioesterase
Brown fat-inducible thioesterase
Short name=BFIT

Gene names

Name:	ACOT11
Synonyms:	BFIT, KIAA0707, THEA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	607 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence BAA31682.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid metabolic process Non-traceable author statement Ref.1. Source: UniProtKB intracellular signal transduction Non-traceable author statement Ref.1. Source: UniProtKB response to cold Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL
Cellular_component	cytoplasm Inferred by curator Ref.1. Source: UniProtKB
Molecular_function	acyl-CoA hydrolase activity Traceable author statement Ref.1. 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

Natural variations

Alternative sequence

544 – 607

64

CCWVR…YLQDT → VSYYNQATPGVLNYVTTNVA GLSSEFYTTFKACEQFLLDN RNDLAPSLQTL in isoform 2.

VSP_000160

Natural variant

11

1

R → W.
Corresponds to variant rs34630746 [ dbSNP | Ensembl ].

VAR_048190

Natural variant

165

1

P → L.
Corresponds to variant rs2304306 [ dbSNP | Ensembl ].

VAR_022119

Natural variant

202

1

G → D. Ref.4
Corresponds to variant rs1702003 [ dbSNP | Ensembl ].

VAR_022120

Natural variant

212

1

M → I.
Corresponds to variant rs2304305 [ dbSNP | Ensembl ].

VAR_022121

Natural variant

536

1

R → H.
Corresponds to variant rs12403630 [ dbSNP | Ensembl ].

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

522 – 524

3

Beta strand

528 – 538

11

Beta strand

541 – 543

3

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) [UniParc]. 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] [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. , 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. , 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. , 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.

IPI

IPI00220903.
IPI00305894.

PIR

T00351.

RefSeq

NP_056362.1. NM_015547.3.
NP_671517.1. NM_147161.3.

UniGene

Hs.234786.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q8WXI4.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000360366.

PTM databases

PhosphoSite

Q8WXI4.

Polymorphism databases

DMDM

21363000.

Proteomic databases

PaxDb

Q8WXI4.

PRIDE

Q8WXI4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343744; ENSP00000340260; ENSG00000162390.
ENST00000371316; ENSP00000360366; ENSG00000162390.

GeneID

26027.

KEGG

hsa:26027.

UCSC

uc001cxj.2. human.
uc001cxm.2. human.

Organism-specific databases

CTD

26027.

GeneCards

GC01P055007.

HGNC

HGNC:18156. ACOT11.

HPA

HPA035309.

MIM

606803. gene.

neXtProt

NX_Q8WXI4.

PharmGKB

PA38303.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1607.

HOVERGEN

HBG023847.

InParanoid

Q8WXI4.

KO

K12417.

OMA

LKQITPR.

OrthoDB

EOG45QHCX.

PhylomeDB

Q8WXI4.

Gene expression databases

Bgee

Q8WXI4.

CleanEx

HS_ACOT11.

Genevestigator

Q8WXI4.

GermOnline

ENSG00000162390. Homo sapiens.

Family and domain databases

Gene3D

3.30.530.20. 1 hit.

InterPro

IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
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

EvolutionaryTrace

Q8WXI4.

GenomeRNAi

26027.

NextBio

47814.

SOURCE

Search...

Entry information

Entry name

ACO11_HUMAN

Accession

Primary (citable) accession number: Q8WXI4
Secondary accession number(s): B1AQ22 , D3DQ50, O75187, Q52LP1, Q53ER9, Q96DI1, Q9H883

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.