P80250 (PMCH_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Palmitoyl-CoA hydrolase EC=3.1.2.2 Alternative name(s): Long-chain fatty-acyl-CoA hydrolase
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	64 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolysis of a variety of CoA thioesters of long-chain fatty acids.
Catalytic activity	Palmitoyl-CoA + H2O = CoA + palmitate.
Subunit structure	Monomer and homotrimer.
Subcellular location	Microsome. Endoplasmic reticulum.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Microsome
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	palmitoyl-CoA 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 – ›64	›64	Palmitoyl-CoA hydrolase		PRO_0000070294
Experimental info
	Non-terminal residue	64	1

Sequences

	Sequence		Length	Mass (Da)
	P80250 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: E9FA5D7CD7870559	FASTA	64	6,919
	10 20 30 40 50 60 NPSSPPVVDT TNTTSYPPMC SQDAVGGQVL ENIPLQEDCL YNFNTVPYIV GIIPEDIIPV AIEK

References

[1]

"Isolation and characterization of microsomal acyl-CoA thioesterase. A member of the rat liver microsomal carboxylesterase multi-gene family." Alexson S.E.H., Mentlein R., Wernstedt C., Hellman U. Eur. J. Biochem. 214:719-727(1993) [PubMed: 8100522] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver.

Cross-references

Sequence databases
IPI	IPI00195608.
3D structure databases
ProteinModelPortal	P80250.
SMR	P80250. Positions 12-41.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.1.2.2. 5301.
Gene expression databases
Genevestigator	P80250.
Family and domain databases
PROSITE	PS00122. CARBOXYLESTERASE_B_1. Partial match. PS00941. CARBOXYLESTERASE_B_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMCH_RAT

Accession

Primary (citable) accession number: P80250

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 21, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program