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Protein

S-acyl fatty acid synthase thioesterase, medium chain

Gene

OLAH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In fatty acid biosynthesis chain termination and release of the free fatty acid product is achieved by hydrolysis of the thio ester by a thioesterase I, a component of the fatty acid synthetase complex. The chain length of the released fatty acid is usually C16. However, in the mammary glands of non-ruminant mammals, and in the uropygial gland of certain waterfowl there exists a second thioesterase which releases medium-chain length fatty acids (C8 to C2) (By similarity).By similarity

Catalytic activityi

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011By similarity
Active sitei237 – 2371By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Protein family/group databases

ESTHERihuman-OLAH. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
S-acyl fatty acid synthase thioesterase, medium chain (EC:3.1.2.14)
Alternative name(s):
Augmented in rheumatoid arthritis 1
Short name:
AURA1
Oleoyl-ACP hydrolase
Thioesterase II
Thioesterase domain-containing protein 1
Gene namesi
Name:OLAH
Synonyms:THEDC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:25625. OLAH.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134955731.

Polymorphism and mutation databases

BioMutaiOLAH.
DMDMi52783423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265S-acyl fatty acid synthase thioesterase, medium chainPRO_0000180358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NV23.
PRIDEiQ9NV23.

PTM databases

PhosphoSiteiQ9NV23.

Expressioni

Tissue specificityi

Isoform 2 is up-regulated in bone marrow-derived mononuclear cells of rheumatoid arthritis patients.1 Publication

Gene expression databases

BgeeiQ9NV23.
CleanExiHS_OLAH.
ExpressionAtlasiQ9NV23. baseline and differential.
GenevisibleiQ9NV23. HS.

Organism-specific databases

HPAiHPA037947.
HPA037948.

Structurei

Secondary structure

1
265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 326Combined sources
Beta strandi47 – 515Combined sources
Helixi79 – 835Combined sources
Helixi87 – 904Combined sources
Beta strandi95 – 1006Combined sources
Helixi102 – 11615Combined sources
Beta strandi123 – 1297Combined sources
Beta strandi133 – 1353Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 1579Combined sources
Helixi173 – 19018Combined sources
Beta strandi202 – 2098Combined sources
Helixi217 – 2237Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi228 – 2369Combined sources
Helixi239 – 2413Combined sources
Helixi243 – 25917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XJVX-ray2.80A1-265[»]
ProteinModelPortaliQ9NV23.
SMRiQ9NV23. Positions 21-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thioesterase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000015518.
HOGENOMiHOG000131891.
HOVERGENiHBG015455.
InParanoidiQ9NV23.
KOiK01071.
OMAiCDLTCFV.
PhylomeDBiQ9NV23.
TreeFamiTF331555.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR012223. TEII.
IPR001031. Thioesterase.
[Graphical view]
PANTHERiPTHR11487. PTHR11487. 1 hit.
PfamiPF00975. Thioesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NV23-1) [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
MERGDQPKRT RNENIFNCLY KNPEATFKLI CFPWMGGGST HFAKWGQDTH
60 70 80 90 100
DLLEVHSLRL PGRESRVEEP LENDISQLVD EVVCALQPVI QDKPFAFFGH
110 120 130 140 150
SMGSYIAFRT ALGLKENNQP EPLHLFLSSA TPVHSKAWHR IPKDDELSEE
160 170 180 190 200
QISHYLMEFG GTPKHFAEAK EFVKQCSPII RADLNIVRSC TSNVPSKAVL
210 220 230 240 250
SCDLTCFVGS EDIAKDMEAW KDVTSGNAKI YQLPGGHFYL LDPANEKLIK
260
NYIIKCLEVS SISNF
Length:265
Mass (Da):29,931
Last modified:October 1, 2000 - v1
Checksum:iC67722F3CAD2D2C7
GO
Isoform 2 (identifier: Q9NV23-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-55: V → ETASHHVAKAGLKLRRSSDPPASAYPCAGVSHRRREPPCLAKILGLFWILIFFM

Show »
Length:318
Mass (Da):35,818
Checksum:iC7DB0DFEBCB0823F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 551V → ETASHHVAKAGLKLRRSSDP PASAYPCAGVSHRRREPPCL AKILGLFWILIFFM in isoform 2. 1 PublicationVSP_040022

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001844 mRNA. Translation: BAA91937.1.
AK001968 mRNA. Translation: BAA92007.1.
AL590365 Genomic DNA. Translation: CAH73961.1.
AL590365 Genomic DNA. Translation: CAH73962.1.
CH471072 Genomic DNA. Translation: EAW86244.1.
CH471072 Genomic DNA. Translation: EAW86245.1.
BC050372 mRNA. Translation: AAH50372.1.
BR000403 mRNA. Translation: FAA00320.1.
CCDSiCCDS31152.1. [Q9NV23-1]
CCDS7106.1. [Q9NV23-2]
RefSeqiNP_001034791.1. NM_001039702.2. [Q9NV23-1]
NP_060794.1. NM_018324.2. [Q9NV23-2]
XP_006717519.1. XM_006717456.2. [Q9NV23-1]
UniGeneiHs.24309.

Genome annotation databases

EnsembliENST00000378217; ENSP00000367462; ENSG00000152463. [Q9NV23-2]
ENST00000378228; ENSP00000367473; ENSG00000152463. [Q9NV23-1]
GeneIDi55301.
KEGGihsa:55301.
UCSCiuc001int.3. human. [Q9NV23-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001844 mRNA. Translation: BAA91937.1.
AK001968 mRNA. Translation: BAA92007.1.
AL590365 Genomic DNA. Translation: CAH73961.1.
AL590365 Genomic DNA. Translation: CAH73962.1.
CH471072 Genomic DNA. Translation: EAW86244.1.
CH471072 Genomic DNA. Translation: EAW86245.1.
BC050372 mRNA. Translation: AAH50372.1.
BR000403 mRNA. Translation: FAA00320.1.
CCDSiCCDS31152.1. [Q9NV23-1]
CCDS7106.1. [Q9NV23-2]
RefSeqiNP_001034791.1. NM_001039702.2. [Q9NV23-1]
NP_060794.1. NM_018324.2. [Q9NV23-2]
XP_006717519.1. XM_006717456.2. [Q9NV23-1]
UniGeneiHs.24309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XJVX-ray2.80A1-265[»]
ProteinModelPortaliQ9NV23.
SMRiQ9NV23. Positions 21-244.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERihuman-OLAH. Thioesterase.

PTM databases

PhosphoSiteiQ9NV23.

Polymorphism and mutation databases

BioMutaiOLAH.
DMDMi52783423.

Proteomic databases

MaxQBiQ9NV23.
PRIDEiQ9NV23.

Protocols and materials databases

DNASUi55301.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378217; ENSP00000367462; ENSG00000152463. [Q9NV23-2]
ENST00000378228; ENSP00000367473; ENSG00000152463. [Q9NV23-1]
GeneIDi55301.
KEGGihsa:55301.
UCSCiuc001int.3. human. [Q9NV23-1]

Organism-specific databases

CTDi55301.
GeneCardsiOLAH.
HGNCiHGNC:25625. OLAH.
HPAiHPA037947.
HPA037948.
neXtProtiNX_Q9NV23.
PharmGKBiPA134955731.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000015518.
HOGENOMiHOG000131891.
HOVERGENiHBG015455.
InParanoidiQ9NV23.
KOiK01071.
OMAiCDLTCFV.
PhylomeDBiQ9NV23.
TreeFamiTF331555.

Enzyme and pathway databases

ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

GenomeRNAii55301.
NextBioi59524.
PROiQ9NV23.

Gene expression databases

BgeeiQ9NV23.
CleanExiHS_OLAH.
ExpressionAtlasiQ9NV23. baseline and differential.
GenevisibleiQ9NV23. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR012223. TEII.
IPR001031. Thioesterase.
[Graphical view]
PANTHERiPTHR11487. PTHR11487. 1 hit.
PfamiPF00975. Thioesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Brain.
  5. "Isolation and expression profiling of genes upregulated in bone marrow-derived mononuclear cells of rheumatoid arthritis patients."
    Nakamura N., Shimaoka Y., Tougan T., Onda H., Okuzaki D., Zhao H., Fujimori A., Yabuta N., Nagamori I., Tanigawa A., Sato J., Oda T., Hayashida K., Suzuki R., Yukioka M., Nojima H., Ochi T.
    DNA Res. 13:169-183(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION AND UP-REGULATION OF ISOFORM 2, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSAST_HUMAN
AccessioniPrimary (citable) accession number: Q9NV23
Secondary accession number(s): Q5VUB6, Q9NUW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 107 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.