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Reviewed, UniProtKB/Swiss-Prot P21399 (ACOC_HUMAN)

Last modified June 16, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cytoplasmic aconitate hydratase
      Short name=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase
    Iron-responsive element-binding protein 1
      Short name=IRE-BP 1
    Iron regulatory protein 1
      Short name=IRP1
    Ferritin repressor protein
Gene names
Name: ACO1
Synonyms: IREB1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length889 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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. Ref.5

Catalytic activity

Citrate = isocitrate.

Cofactor

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 889889Cytoplasmic aconitate hydratase
PRO_0000076680

Sites

Metal binding4371Iron-sulfur (4Fe-4S) By similarity
Metal binding5031Iron-sulfur (4Fe-4S) By similarity
Metal binding5061Iron-sulfur (4Fe-4S) By similarity

Natural variations

Natural variant3951A → D: dbSNP rs3814519.
VAR_048180
Natural variant4861G → R: dbSNP rs34630459.
VAR_048181

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21399-1 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: E1A05AF701D46DCB

FASTA88998,399
        10         20         30         40         50         60 
MSNPFAHLAE PLDPVQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAIRNC DEFLVKKQDI 

        70         80         90        100        110        120 
ENILHWNVTQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPVCPA 

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

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

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

       310        320        330        340        350        360 
PEYGATAAFF PVDEVSITYL VQTGRDEEKL KYIKKYLQAV GMFRDFNDPS QDPDFTQVVE 

       370        380        390        400        410        420 
LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQVAPEHHN DHKTFIYDNT 

       430        440        450        460        470        480 
EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LNVMPYIKTS LSPGSGVVTY 

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

       550        560        570        580        590        600 
RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PTRDEIQAVE 

       610        620        630        640        650        660 
RQYVIPGMFK EVYQKIETVN ESWNALATPS DKLFFWNSKS TYIKSPPFFE NLTLDLQPPK 

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

       730        740        750        760        770        780 
RGTFANIRLL NRFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIVLA GKEYGAGSSR 

       790        800        810        820        830        840 
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENADALGLT GQERYTIIIP 

       850        860        870        880 
ENLKPQMKVQ VKLDTGKTFQ AVMRFDTDVE LTYFLNGGIL NYMIRKMAK

« Hide

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References

« Hide 'large scale' references
[1]"Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation."
Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C., Kuehn L.
Nucleic Acids Res. 20:33-39(1992) [PubMed: 1738601] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Uterus.
[3]"Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein."
Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J., Samaniego F., McBride O.W., Harford J.B., Klausner R.D.
Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990) [PubMed: 2172968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, PARTIAL PROTEIN SEQUENCE.
[4]"Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase."
Hentze M.W., Argos P.
Nucleic Acids Res. 19:1739-1740(1991) [PubMed: 1903202] [Abstract]
Cited for: SIMILARITY TO ACONITASES AND IPM ISOMERASES.
[5]"A regulated RNA binding protein also possesses aconitase activity."
Kaptain S., Downey W.E., Tang C.K., Philpott C., Haile D.J., Orloff D.G., Harford J.B., Rouault T.A., Klausner R.D.
Proc. Natl. Acad. Sci. U.S.A. 88:10109-10113(1991) [PubMed: 1946430] [Abstract]
Cited for: FUNCTION AS AN ACONITASE.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Web resources

Wikipedia

Aconitase entry

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Cross-references

Sequence databases

Z11559 mRNA. Translation: CAA77651.1.
BC018103 mRNA. Translation: AAH18103.1.
M58510 mRNA. Translation: AAA69900.1.
IPIIPI00008485.
PIRS26403.
RefSeqNP_002188.1.
UniGeneHs.567229

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2B3XX-ray2.54A2-889[»]
2B3YX-ray1.85A/B2-889[»]
ModBaseSearch...

PTM databases

PhosphoSiteP21399.

2-D gel databases

REPRODUCTION-2DPAGEIPI00008485.

Proteomic databases

PeptideAtlasP21399.
PRIDEP21399.

Genome annotation databases

EnsemblENSG00000122729. Homo sapiens. [Contig view]
GeneID48.
KEGGhsa:48.

Organism-specific databases

GeneCardsGC09P032374.
H-InvDBHIX0007969.
HGNCHGNC:117. ACO1.
MIM100880. gene.
Orphanet43115. Aconitase deficiency.
PharmGKBPA24442.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP21399.
HOVERGENP21399.
OMAP21399. DFTQVVE.

Enzyme and pathway databases

BRENDA4.2.1.3. 247.

Gene expression databases

ArrayExpressP21399.
BgeeP21399.
CleanExHS_ACO1.
GermOnlineENSG00000122729. Homo sapiens.

Family and domain databases

InterProIPR015931. 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.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
ProDomPD000511. Aconitase_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio187.
SOURCESearch...

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Entry information

Entry nameACOC_HUMAN
AccessionPrimary (citable) accession number: P21399
Secondary accession number(s): Q14652
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents