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Q01059 (ACOC_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic aconitate hydratase
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Ferritin repressor protein
Iron regulatory protein 1
Short name=IRP1
Iron-responsive element-binding protein 1
Short name=IRE-BP 1
Gene names
Name:ACO1
Synonyms:FRP, IREB1, IREBP
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length889 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding By similarity. Ref.3

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity. Ref.3

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Subunit structure

Interacts (when associated with the 4Fe-4S) with FBXL5 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 889889Cytoplasmic aconitate hydratase
PRO_0000076682

Regions

Region205 – 2073Substrate binding By similarity
Region779 – 7802Substrate binding By similarity

Sites

Metal binding4371Iron-sulfur (4Fe-4S) By similarity
Metal binding5031Iron-sulfur (4Fe-4S) By similarity
Metal binding5061Iron-sulfur (4Fe-4S) By similarity
Binding site861Substrate By similarity
Binding site5361Substrate By similarity
Binding site5411Substrate By similarity
Binding site6991Substrate By similarity

Secondary structure

1 ........................................................................................................................................................................... 889
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01059 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 970C4DF4DD7A61D7

FASTA88998,505
        10         20         30         40         50         60 
MSNPFAYLAE PLDPAQPGKK FFNLNKLDYS RYGRLPFSIR VLLEAAVRNC DKFLVKKEDI 

        70         80         90        100        110        120 
ENILNWNVTQ HMNIEVPFKP ARVILQDFTG VPSVVDFAAM RDAVKKLGGD PEKINPICPV 

       130        140        150        160        170        180 
DLVIDHSIQV DFNRRADSLQ KNQDLEFERN RERFEFLKWG SKAFRNMRII PPGSGIIHQV 

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

       250        260        270        280        290        300 
QVIGYRLMGK PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGLGVAQLSI ADRATIANMC 

       310        320        330        340        350        360 
PEYGATATFF PVDEVSIKYL VQTGRDESKV KQIRKYLQAV GMFRDYSDPS QDPDFTQVVE 

       370        380        390        400        410        420 
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPDHHN DHKTFIYNDS 

       430        440        450        460        470        480 
EFTLSHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVKPYVKTS LSPGSGVVTY 

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

       550        560        570        580        590        600 
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGTNAK GQQVFLRDIW PTREEIQAVE 

       610        620        630        640        650        660 
RQYVIPGMFT EVYQKIETVN ASWNALAAPS DKLYLWNPKS TYIKSPPFFE NLTLDLQPPK 

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

       730        740        750        760        770        780 
RGTFANIRLL NRFLNKQAPQ TIHLPSGETL DVFDAAERYQ QEGHPLIVLA GKEYGSGSSR 

       790        800        810        820        830        840 
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADSLGLT GRERYTIIIP 

       850        860        870        880 
ENLTPRMHVQ VKLDTGKTFQ AVIRFDTDVE LTYLHNGGIL NYMIRKMAK

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References

[1]"Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein. Demonstration of a tissue-specific pattern of expression."
Patino M.M., Walden W.E.
J. Biol. Chem. 267:19011-19016(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Localization of an RNA binding element of the iron responsive element binding protein within a proteolytic fragment containing iron coordination ligands."
Swenson G.R., Walden W.E.
Nucleic Acids Res. 22:2627-2633(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 133-146 AND 624-638.
[3]"Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA."
Walden W.E., Selezneva A.I., Dupuy J., Volbeda A., Fontecilla-Camps J.C., Theil E.C., Volz K.
Science 314:1903-1908(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH TARGET MRNA, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M95815 mRNA. Translation: AAA31255.1.
PIRA44153.
RefSeqNP_001075784.1. NM_001082315.1.
UniGeneOcu.1880.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SN2X-ray2.99A2-889[»]
3SNPX-ray2.80A/B2-889[»]
ProteinModelPortalQ01059.
SMRQ01059. Positions 2-889.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000013749.

Proteomic databases

PRIDEQ01059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009154.

Organism-specific databases

CTD100009154.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000025704.
HOVERGENHBG052147.
OrthoDBEOG4C2H8W.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_prot_2.
IPR015934. Aconitase/Fe_reg_prot_2/AcnD.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOC_RABIT
AccessionPrimary (citable) accession number: Q01059
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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