Reviewed, UniProtKB/Swiss-Prot Q9WUR2 (PECI_MOUSE)

Names and origin

Protein names

Recommended name:
    Peroxisomal 3,2-trans-enoyl-CoA isomerase
    EC=5.3.3.8
Alternative name(s):
    Dodecenoyl-CoA isomerase
    Delta(3),delta(2)-enoyl-CoA isomerase
      Short name=D3,D2-enoyl-CoA isomerase

Gene names

Name:

Peci

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates By similarity.
Catalytic activity	(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
Subcellular location	Isoform 1: Mitochondrion By similarity. Isoform 2: Peroxisome matrix By similarity.
Post-translational modification	Acetylation of Lys-60 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. Contains 1 ACB (acyl-CoA-binding) domain.

Ontologies

Keywords
Cellular component	Mitochondrion Peroxisome
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Molecular function	Isomerase
PTM	Acetylation
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from direct assay. Source: MGI peroxisomal matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl-CoA binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase 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: Q9WUR2-1)

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: Q9WUR2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 36	36	Mitochondrion Potential
	Chain	37 – 391	355	Peroxisomal 3,2-trans-enoyl-CoA isomerase		PRO_0000214028
Regions
	Domain	37 – 122	86	ACB
	Region	149 – 319	171	ECH-like
	Motif	389 – 391	3	Microbody targeting signal Potential
Amino acid modifications
	Modified residue	49	1	N6-acetyllysine By similarity
	Modified residue	60	1	N6-acetyllysine Ref.4
	Modified residue	90	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 33	33	Missing in isoform 2.		VSP_037855
Experimental info
	Sequence conflict	35	1	R → K in BAB26315. Ref.2
	Sequence conflict	128	1	R → C in AAH01983. Ref.3
	Sequence conflict	135	1	R → Q in AAH01983. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 1, 2009. Version 2. Checksum: 0B93D3908DF77AF8	FASTA	391	43,268
	10 20 30 40 50 60 MAAVTWSRAR CWCPSVLQVF RLQVAKLHLG RPTMRASQQD FENALNQVKL LKKDPGNEVK 70 80 90 100 110 120 LRLYALYKQA TEGPCNMPKP GMLDFVNKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS 130 140 150 160 170 180 EAPSQGKRGA DEKARESKDI LVTSEDGITK ITFNRPTKKN AISFQMYRDI ILALKNASTD 190 200 210 220 230 240 NTVMAVFTGT GDYYCSGNDL TNFTSATGGI EEAASNGAVL LRDFVNSFID FPKPLVAVVN 250 260 270 280 290 300 GPAVGISVTL LGLFDAVFAS DRATFHTPFS QLGQSPEACS SYTFPKMMGS AKAAEMLLFG 310 320 330 340 350 360 KKLTAREAWA QGLVTEVFPE STFETEVWTR LKTYAKLPPN AMRISKELIR KNEKEKLYAV 370 380 390 NAEECTTLQA RWLSEECMNA IMSFVSRKPK L
	Isoform 2. Checksum: 2E22207290123AE5	FASTA	358	39,503
	10 20 30 40 50 60 MRASQQDFEN ALNQVKLLKK DPGNEVKLRL YALYKQATEG PCNMPKPGML DFVNKAKWDA 70 80 90 100 110 120 WNALGSLPKE TARQNYVDLV SSLSSSSEAP SQGKRGADEK ARESKDILVT SEDGITKITF 130 140 150 160 170 180 NRPTKKNAIS FQMYRDIILA LKNASTDNTV MAVFTGTGDY YCSGNDLTNF TSATGGIEEA 190 200 210 220 230 240 ASNGAVLLRD FVNSFIDFPK PLVAVVNGPA VGISVTLLGL FDAVFASDRA TFHTPFSQLG 250 260 270 280 290 300 QSPEACSSYT FPKMMGSAKA AEMLLFGKKL TAREAWAQGL VTEVFPESTF ETEVWTRLKT 310 320 330 340 350 YAKLPPNAMR ISKELIRKNE KEKLYAVNAE ECTTLQARWL SEECMNAIMS FVSRKPKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase of mammalian peroxisomes." Geisbrecht B.V., Zhang D., Schulz H., Gould S.J. J. Biol. Chem. 274:21797-21803(1999) [PubMed: 10419495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Tongue.
[3]	"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] OF 8-391 (ISOFORM 1). Strain: Czech II. Tissue: Mammary tumor.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF153613 mRNA. Translation: AAD34174.1. AK009478 mRNA. Translation: BAB26315.2. BC001983 mRNA. Translation: AAH01983.1. Different initiation.
IPI	IPI00322931. IPI00877214.
RefSeq	NP_001103801.1. NP_001103802.1. NP_035998.2.
UniGene	Mm.28883
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WUR2.
PTM databases
PhosphoSite	Q9WUR2.
Proteomic databases
PRIDE	Q9WUR2.
Genome annotation databases
Ensembl	ENSMUST00000021854; ENSMUSP00000021854; ENSMUSG00000021417; Mus musculus. [Genome view] ENSMUST00000110251; ENSMUSP00000105880; ENSMUSG00000021417; Mus musculus. [Genome view]
GeneID	23986.
KEGG	mmu:23986.
UCSC	uc007qbx.1. mouse.
Organism-specific databases
CTD	23986.
MGI	MGI:1346064. Peci.
Phylogenomic databases
HOGENOM	HBG748731.
HOVERGEN	Q9WUR2.
InParanoid	Q9WUR2.
OMA	RWLSDEC.
Enzyme and pathway databases
BRENDA	5.3.3.8. 244.
Gene expression databases
ArrayExpress	Q9WUR2.
Bgee	Q9WUR2.
Genevestigator	Q9WUR2.
GermOnline	ENSMUSG00000021417. Mus musculus.
Family and domain databases
InterPro	IPR000582. Acyl-CoA-binding_protein. IPR001753. Crotonase_core. IPR014352. FERM/acyl-CoA_bd_prot_3-hlx. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 1 hit.
Pfam	PF00887. ACBP. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
PRINTS	PR00689. ACOABINDINGP.
PROSITE	PS00880. ACB_1. 1 hit. PS51228. ACB_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	303881.
SOURCE	Search...

Entry information

Entry name

PECI_MOUSE

Accession

Primary (citable) accession number: Q9WUR2
Secondary accession number(s): Q99M61, Q9D785

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	September 1, 2009
Last modified:	February 9, 2010
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)