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Reviewed, UniProtKB/Swiss-Prot Q9NV23 (SAST_HUMAN)

Last modified October 13, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-acyl fatty acid synthase thioesterase, medium chain
    EC=3.1.2.14
Alternative name(s):
    Oleoyl-ACP hydrolase
    Thioesterase II
    Thioesterase domain-containing protein 1
Gene names
Name: OLAH
Synonyms: THEDC1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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.

Catalytic activity

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

Sequence similarities

Belongs to the thioesterase family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265S-acyl fatty acid synthase thioesterase, medium chain
PRO_0000180358

Sites

Active site1011 By similarity
Active site2371 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9NV23-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C67722F3CAD2D2C7

FASTA26529,931
        10         20         30         40         50         60 
MERGDQPKRT RNENIFNCLY KNPEATFKLI CFPWMGGGST HFAKWGQDTH DLLEVHSLRL 

        70         80         90        100        110        120 
PGRESRVEEP LENDISQLVD EVVCALQPVI QDKPFAFFGH SMGSYIAFRT ALGLKENNQP 

       130        140        150        160        170        180 
EPLHLFLSSA TPVHSKAWHR IPKDDELSEE QISHYLMEFG GTPKHFAEAK EFVKQCSPII 

       190        200        210        220        230        240 
RADLNIVRSC TSNVPSKAVL SCDLTCFVGS EDIAKDMEAW KDVTSGNAKI YQLPGGHFYL 

       250        260 
LDPANEKLIK NYIIKCLEVS SISNF 

« Hide

References

[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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[2]"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].
Tissue: Brain.

Cross-references

Sequence databases

AK001844 mRNA. Translation: BAA91937.1.
BC050372 mRNA. Translation: AAH50372.1.
IPIIPI00030167.
RefSeqNP_001034791.1.
UniGeneHs.24309

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NV23.

Genome annotation databases

EnsemblENST00000378217; ENSP00000367462; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000378225; ENSP00000367470; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000378228; ENSP00000367473; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000413672; ENSP00000399449; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000416462; ENSP00000413732; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000428897; ENSP00000399290; ENSG00000152463; Homo sapiens. [Genome view]
ENST00000429028; ENSP00000399663; ENSG00000152463; Homo sapiens. [Genome view]
GeneID55301.
KEGGhsa:55301.
UCSCuc001inu.1. human.

Organism-specific databases

CTD55301.
GeneCardsGC10P015126.
HGNCHGNC:25625. OLAH.
HPACAB015417.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9NV23.

Enzyme and pathway databases

BRENDA3.1.2.14. 247.

Gene expression databases

ArrayExpressQ9NV23.
BgeeQ9NV23.
CleanExHS_OLAH.
GenevestigatorQ9NV23.
GermOnlineENSG00000152463. Homo sapiens.

Family and domain databases

InterProIPR012223. TEII.
IPR001031. Thioesterase.
[Graphical view]
PANTHERPTHR11487. TEII. 1 hit.
PfamPF00975. Thioesterase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio59524.

Entry information

Entry nameSAST_HUMAN
AccessionPrimary (citable) accession number: Q9NV23
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2000
Last modified: October 13, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents