Q9NV23 (SAST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	OLAH
Synonyms:	THEDC1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	265 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Tissue specificity	Isoform 2: Up-regulated in bone marrow-derived mononuclear cells of rheumatoid arthritis patients. Ref.5
Sequence similarities	Belongs to the thioesterase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	myristoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC palmitoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NV23-1)

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: Q9NV23-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 265	265	S-acyl fatty acid synthase thioesterase, medium chain		PRO_0000180358
Sites
	Active site	101	1	By similarity
	Active site	237	1	By similarity
Natural variations
	Alternative sequence	55	1	V → ETASHHVAKAGLKLRRSSDP PASAYPCAGVSHRRREPPCL AKILGLFWILIFFM in isoform 2.		VSP_040022

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C67722F3CAD2D2C7	FASTA	265	29,931
	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
	Isoform 2 [UniParc]. Checksum: C7DB0DFEBCB0823F	FASTA	318	35,818
	10 20 30 40 50 60 MERGDQPKRT RNENIFNCLY KNPEATFKLI CFPWMGGGST HFAKWGQDTH DLLEETASHH 70 80 90 100 110 120 VAKAGLKLRR SSDPPASAYP CAGVSHRRRE PPCLAKILGL FWILIFFMHS LRLPGRESRV 130 140 150 160 170 180 EEPLENDISQ LVDEVVCALQ PVIQDKPFAF FGHSMGSYIA FRTALGLKEN NQPEPLHLFL 190 200 210 220 230 240 SSATPVHSKA WHRIPKDDEL SEEQISHYLM EFGGTPKHFA EAKEFVKQCS PIIRADLNIV 250 260 270 280 290 300 RSCTSNVPSK AVLSCDLTCF VGSEDIAKDM EAWKDVTSGN AKIYQLPGGH FYLLDPANEK 310 LIKNYIIKCL EVSSISNF

References

	« Hide 'large scale' referencesShow 'large scale' 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. , 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] (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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[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: 15489334] [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: 17082220] [Abstract] Cited for: EXPRESSION AND UP-REGULATION OF ISOFORM 2, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00019562. IPI00030167.
RefSeq	NP_001034791.1. NM_001039702.2. NP_060794.1. NM_018324.2.
UniGene	Hs.24309.
3D structure databases
ProteinModelPortal	Q9NV23.
SMR	Q9NV23. Positions 10-257.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NV23.
Polymorphism databases
DMDM	52783423.
Proteomic databases
PRIDE	Q9NV23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378228; ENSP00000367473; ENSG00000152463.
GeneID	55301.
KEGG	hsa:55301.
UCSC	uc001inu.1. human.
Organism-specific databases
CTD	55301.
GeneCards	GC10P015074.
HGNC	HGNC:25625. OLAH.
HPA	HPA037947. HPA037948.
neXtProt	NX_Q9NV23.
PharmGKB	PA134955731.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000015518.
HOVERGEN	HBG015455.
OMA	SCDLTCF.
PhylomeDB	Q9NV23.
Gene expression databases
ArrayExpress	Q9NV23.
Bgee	Q9NV23.
CleanEx	HS_OLAH.
Genevestigator	Q9NV23.
GermOnline	ENSG00000152463. Homo sapiens.
Family and domain databases
InterPro	IPR012223. TEII. IPR001031. Thioesterase. [Graphical view]
KO	K01071.
PANTHER	PTHR11487. TEII. 1 hit.
Pfam	PF00975. Thioesterase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	59524.

Entry information

Entry name

SAST_HUMAN

Accession

Primary (citable) accession number: Q9NV23
Secondary accession number(s): Q5VUB6, Q9NUW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 74 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.