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P28271 (ACOC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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
Iron regulatory protein 1
Short name=IRP1
Iron-responsive element-binding protein 1
Short name=IRE-BP 1
Gene names
Name:Aco1
Synonyms:Ireb1, Irebp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.1

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity. Ref.1

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.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
RNA-binding
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular iron ion homeostasis

Inferred from mutant phenotype. Source: MGI

citrate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

intestinal absorption

Inferred from genetic interaction. Source: MGI

post-embryonic development

Inferred from genetic interaction. Source: MGI

regulation of translation

Inferred from mutant phenotype. Source: MGI

response to iron(II) ion

Inferred from sequence or structural similarity. Source: UniProtKB

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: MGI

mitochondrion

Inferred from direct assay. Source: MGI

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

aconitate hydratase activity

Inferred from sequence or structural similarity. Source: UniProtKB

citrate hydro-lyase (cis-aconitate-forming) activity

Inferred from electronic annotation. Source: EC

iron-responsive element binding

Inferred from sequence or structural similarity. Source: UniProtKB

isocitrate hydro-lyase (cis-aconitate-forming) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 889889Cytoplasmic aconitate hydratase
PRO_0000076681

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

Experimental info

Sequence conflict4061P → S in AAH05454. Ref.5
Sequence conflict4181S → N in AAH05454. Ref.5
Sequence conflict4361S → T in CAA43455. Ref.1
Sequence conflict6031H → Y in AAH05454. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P28271 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 704B8A018EAC6B4C

FASTA88998,126
        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 DRKTFLYSNS 

       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 
RQHVIPGMFK 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

« Hide

References

« Hide 'large scale' references
[1]"Sequence and expression of the murine iron-responsive element binding protein."
Philpott C.C., Rouault T.A., Klausner R.D.
Nucleic Acids Res. 19:6333-6333(1991) [PubMed: 1956798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[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. expand/collapse author list , 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].
Strain: C57BL/6J.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X61147 mRNA. Translation: CAA43455.1.
AK163985 mRNA. Translation: BAE37570.1.
AL831793 Genomic DNA. Translation: CAM27573.1.
CH466538 Genomic DNA. Translation: EDL05446.1.
BC005454 mRNA. Translation: AAH05454.1.
IPIIPI00875325.
PIRS18720.
RefSeqNP_031412.2. NM_007386.2.
UniGeneMm.331547.

3D structure databases

ProteinModelPortalP28271.
SMRP28271. Positions 3-889.
ModBaseSearch...

Protein-protein interaction databases

STRINGP28271.

PTM databases

PhosphoSiteP28271.

2D gel databases

SWISS-2DPAGEP28271.
REPRODUCTION-2DPAGEP28271.

Proteomic databases

PRIDEP28271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102973; ENSMUSP00000100038; ENSMUSG00000028405.
GeneID11428.
KEGGmmu:11428.

Organism-specific databases

CTD48.
MGIMGI:87879. Aco1.

Phylogenomic databases

eggNOGroNOG06028.
GeneTreeENSGT00530000063060.
HOVERGENHBG052147.
OrthoDBEOG4C2H8W.

Gene expression databases

ArrayExpressP28271.
BgeeP28271.
CleanExMM_ACO1.
GenevestigatorP28271.
GermOnlineENSMUSG00000028405. Mus musculus.

Family and domain databases

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]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 3 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KOK01681.
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.
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...

Other

NextBio278700.
SOURCESearch...

Entry information

Entry nameACOC_MOUSE
AccessionPrimary (citable) accession number: P28271
Secondary accession number(s): Q3TQ15, Q99K54
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents