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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)DescriptionActionsGraphical viewLength
Active sitei101By similarity1
Active sitei237By similarity1

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

BioCyciZFISH:HS07821-MONOMER.
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

OpenTargetsiENSG00000152463.
PharmGKBiPA134955731.

Polymorphism and mutation databases

BioMutaiOLAH.
DMDMi52783423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803581 – 265S-acyl fatty acid synthase thioesterase, medium chainAdd BLAST265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NV23.
PeptideAtlasiQ9NV23.
PRIDEiQ9NV23.

PTM databases

iPTMnetiQ9NV23.
PhosphoSitePlusiQ9NV23.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000152463.
CleanExiHS_OLAH.
ExpressionAtlasiQ9NV23. baseline and differential.
GenevisibleiQ9NV23. HS.

Organism-specific databases

HPAiHPA037947.
HPA037948.

Structurei

Secondary structure

1265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 32Combined sources6
Beta strandi47 – 51Combined sources5
Helixi79 – 83Combined sources5
Helixi87 – 90Combined sources4
Beta strandi95 – 100Combined sources6
Helixi102 – 116Combined sources15
Beta strandi123 – 129Combined sources7
Beta strandi133 – 135Combined sources3
Helixi144 – 146Combined sources3
Helixi149 – 157Combined sources9
Helixi173 – 190Combined sources18
Beta strandi202 – 209Combined sources8
Helixi217 – 223Combined sources7
Beta strandi224 – 226Combined sources3
Beta strandi228 – 236Combined sources9
Helixi239 – 241Combined sources3
Helixi243 – 259Combined sources17

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the thioesterase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000015518.
HOGENOMiHOG000131891.
HOVERGENiHBG015455.
InParanoidiQ9NV23.
KOiK01071.
OMAiCDLTCFV.
OrthoDBiEOG091G0EQZ.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04002255V → ETASHHVAKAGLKLRRSSDP PASAYPCAGVSHRRREPPCL AKILGLFWILIFFM in isoform 2. 1 Publication1

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_016871865.1. XM_017016376.1. [Q9NV23-2]
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_016871865.1. XM_017016376.1. [Q9NV23-2]
UniGeneiHs.24309.

3D structure databases

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

Protein family/group databases

ESTHERihuman-OLAH. Thioesterase.

PTM databases

iPTMnetiQ9NV23.
PhosphoSitePlusiQ9NV23.

Polymorphism and mutation databases

BioMutaiOLAH.
DMDMi52783423.

Proteomic databases

MaxQBiQ9NV23.
PeptideAtlasiQ9NV23.
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.
OpenTargetsiENSG00000152463.
PharmGKBiPA134955731.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000015518.
HOGENOMiHOG000131891.
HOVERGENiHBG015455.
InParanoidiQ9NV23.
KOiK01071.
OMAiCDLTCFV.
OrthoDBiEOG091G0EQZ.
PhylomeDBiQ9NV23.
TreeFamiTF331555.

Enzyme and pathway databases

BioCyciZFISH:HS07821-MONOMER.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

GenomeRNAii55301.
PROiQ9NV23.

Gene expression databases

BgeeiENSG00000152463.
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...

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: November 2, 2016
This is version 112 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.