P08635 (SAST_RAT) 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):
Oleoyl-ACP hydrolase
Thioesterase II
Thioesterase domain-containing protein 1

Gene names

Name:	Olah
Synonyms:	Mch, Thedc1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Evidence 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).
Catalytic activity	Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.
Subunit structure	Monomer.
Sequence similarities	Belongs to the thioesterase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 263	263	S-acyl fatty acid synthase thioesterase, medium chain		PRO_0000180360
Sites
	Active site	101	1	Ref.4
	Active site	237	1	By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine

Sequences

	Sequence		Length	Mass (Da)
	P08635 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 6AB3681E639D7E02	FASTA	263	29,471
	10 20 30 40 50 60 METAVNAKSP RNEKVLNCLY QNPDAVFKLI CFPWAGGGSI HFAKWGQKIN DSLEVHAVRL 70 80 90 100 110 120 AGRETRLGEP FANDIYQIAD EIVTALLPII QDKAFAFFGH SFGSYIALIT ALLLKEKYKM 130 140 150 160 170 180 EPLHIFVSGA SAPHSTSRPQ VPDLNELTEE QVRHHLLDFG GTPKHLIEDQ DVLRMFIPLL 190 200 210 220 230 240 KADAGVVKKF IFDKPSKALL SLDITGFLGS EDTIKDIEGW QDLTSGKFDV HMLPGDHFYL 250 260 MKPDNENFIK NYIAKCLELS SLT

References

[1]	"Molecular cloning and sequence analysis of complementary DNA encoding rat mammary gland medium-chain S-acyl fatty acid synthetase thio ester hydrolase." Safford R., de Silva J., Lucas C., Windust J.H.C., Shedden J., James C.M., Sidebottom C.M., Slabas A.R., Tombs M.P., Hughes S.G. Biochemistry 26:1358-1364(1987) [PubMed: 3105579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	"Cloning and sequencing of the medium-chain S-acyl fatty acid synthetase thioester hydrolase cDNA from rat mammary gland." Naggert J., Williams B., Caslhman D.P., Smith S. Biochem. J. 243:597-601(1987) [PubMed: 3632637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[3]	"Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thio ester hydrolase from rat mammary gland." Randhawa Z.I., Smith S. Biochemistry 26:1365-1373(1987) [PubMed: 3567174] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Mammary gland.
[4]	"Amino acid sequence of the serine active-site region of the medium-chain S-acyl fatty acid synthetase thioester hydrolase from rat mammary gland." Randhawa Z.I., Naggert J., Blacher R.W., Smith S. Eur. J. Biochem. 162:577-581(1987) [PubMed: 3104035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-121, PROTEIN SEQUENCE OF 65-121, ACTIVE SITE. Tissue: Mammary gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M16200 mRNA. Translation: AAA41578.1. Y00311 mRNA. Translation: CAA68411.1.
IPI	IPI00212989.
PIR	A26625.
RefSeq	NP_073196.1. NM_022705.1.
UniGene	Rn.9674.
3D structure databases
ProteinModelPortal	P08635.
ModBase	Search...
Protein-protein interaction databases
STRING	P08635.
Proteomic databases
PRIDE	P08635.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000022043; ENSRNOP00000022043; ENSRNOG00000016403.
GeneID	64669.
KEGG	rno:64669.
UCSC	NM_022705. rat.
Organism-specific databases
CTD	55301.
RGD	621115. Olah.
Phylogenomic databases
eggNOG	roNOG17940.
GeneTree	ENSGT00390000015518.
HOVERGEN	HBG015455.
InParanoid	P08635.
OMA	SCDLTCF.
OrthoDB	EOG4F1X42.
PhylomeDB	P08635.
Gene expression databases
ArrayExpress	P08635.
Genevestigator	P08635.
GermOnline	ENSRNOG00000016403. Rattus norvegicus.
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	613661.

Entry information

Entry name

SAST_RAT

Accession

Primary (citable) accession number: P08635

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 16, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program