[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/19.22.6333; PubMed=1956798 [NCBI, ExPASy, EBI, Israel, Japan] Philpott C.C., Rouault T.A., Klausner R.D.; "Sequence and expression of the murine iron-responsive element binding protein."; Nucleic Acids Res. 19:6333-6333(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA. This protein also expresses aconitase activity.
CATALYTIC ACTIVITY: Citrate = isocitrate.
COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the aconitase/IPM isomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X61147; CAA43455.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005454; AAH05454.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S18720; S18720.

UniGene

Mm.331547

3D structure databases

P28271; 3-889.

PTM databases

P28271; -.

2D gel databases

SWISS-2DPAGE

P28271; -.

REPRODUCTION-2DPAGE

P28271; -.

Organism-specific databases

MGI

MGI:87879; Aco1.

Gene expression databases

ArrayExpress

P28271; -.

CleanEx

MM_ACO1; -.

GermOnline

ENSMUSG00000028405; Mus musculus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from MGI).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0003994;	Molecular function: aconitate hydratase activity (inferred from direct assay from MGI).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030350;	Molecular function: iron-responsive element binding (inferred from direct assay from MGI).
GO:0006879;	Biological process: cellular iron ion homeostasis (inferred from genetic interaction from MGI).
GO:0050892;	Biological process: intestinal absorption (inferred from genetic interaction from MGI).
GO:0009791;	Biological process: post-embryonic development (inferred from genetic interaction from MGI).
GO:0006417;	Biological process: regulation of translation (inferred from mutant phenotype from MGI).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030; Acoase/IPM_deHydtase_lsu_aba.
IPR015937; Aconitase-like_core.
IPR015928; Aconitase/3IPM_dehydase_swvl.
IPR006249; Aconitase/Fe_reg_prot_2.
IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1.
G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.

PANTHER

PTHR11670; Aconitase-like_core; 1.
PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1.

Pfam

PF00330; Aconitase; 1.
PF00694; Aconitase_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00415; ACONITASE.

ProDom

PD000511; Aconitase_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01341; aconitase_1; 1.

PROSITE

PS00450; ACONITASE_1; 1.
PS01244; ACONITASE_2; 1.

Genome annotation databases

Ensembl

ENSMUSG00000028405; Mus musculus. [Contig view]

Phylogenomic databases

HOVERGEN

P28271; -.

Other

SOURCE

Aco1; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 889`	`889`	`Cytoplasmic aconitate hydratase.`	`PRO_0000076681`
`METAL`	`437 437`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`503 503`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`506 506`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CONFLICT`	`406 406`		`P -> S (in Ref. 2; AAH05454).`
`CONFLICT`	`418 418`		`N -> S (in Ref. 1; CAA43455).`
`CONFLICT`	`436 436`		`S -> T (in Ref. 1; CAA43455).`
`CONFLICT`	`603 603`		`Y -> H (in Ref. 1; CAA43455).`

Sequence information

Length: 889 AA [This is the length of the unprocessed precursor]

Molecular weight: 98179 Da [This is the MW of the unprocessed precursor]

CRC64: 04F0B3968B1FA7BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKNPFAHLAE PLDAAQPGKR FFNLNKLEDS RYGRLPFSIR VLLEAAVRNC DEFLVKKNDI 

        70         80         90        100        110        120 
ENILNWNVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGN PEKINPVCPA 

       130        140        150        160        170        180 
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN KERFEFLKWG SQAFCNMRII PPGSGIIHQV 

       190        200        210        220        230        240 
NLEYLARVVF DQDGCYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP 

       250        260        270        280        290        300 
QVIGYKLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 

       310        320        330        340        350        360 
PEYGATAAFF PVDEVSIAYL LQTGREEDKV KHIQKYLQAV GMFRDFNDTS QDPDFTQVVE 

       370        380        390        400        410        420 
LDLKTVVPCC SGPKRPQDKV AVSEMKKDFE SCLGAKQGFK GFQVAPDRHN DRKTFLYNNS 

       430        440        450        460        470        480 
EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEAG LSVKPYIKTS LSPGSGVVTY 

       490        500        510        520        530        540 
YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG 

       550        560        570        580        590        600 
RVHPNTRANY LASPPLVIAY AIAGTVRIDF EKEPLGVNAQ GRQVFLKDIW PTRDEIQAVE 

       610        620        630        640        650        660 
RQYVIPGMFK EVYQKIETVN KSWNALAAPS EKLYAWNPKS TYIKSPPFFE SLTLDLQPPK 

       670        680        690        700        710        720 
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA 

       730        740        750        760        770        780 
RGTFANIRLL NKFLNKQAPQ TVHLPSGETL DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR 

       790        800        810        820        830        840 
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GETADSLGLT GRERYTINIP 

       850        860        870        880 
EDLKPRMTVQ IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMAQ

P28271 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools