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Q63270

- ACOC_RAT

UniProt

Q63270 - ACOC_RAT

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Protein

Cytoplasmic aconitate hydratase

Gene
Aco1, Ireb1, Irebp
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Citrate = isocitrate.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861Substrate By similarity
Metal bindingi437 – 4371Iron-sulfur (4Fe-4S) By similarity
Metal bindingi503 – 5031Iron-sulfur (4Fe-4S) By similarity
Metal bindingi506 – 5061Iron-sulfur (4Fe-4S) By similarity
Binding sitei536 – 5361Substrate By similarity
Binding sitei541 – 5411Substrate By similarity
Binding sitei699 – 6991Substrate By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  2. aconitate hydratase activity Source: UniProtKB
  3. iron-responsive element binding Source: UniProtKB
  4. iron-sulfur cluster binding Source: RGD
  5. metal ion binding Source: UniProtKB-KW
  6. mRNA 5'-UTR binding Source: RGD
  7. mRNA binding Source: RGD

GO - Biological processi

  1. cellular iron ion homeostasis Source: RGD
  2. citrate metabolic process Source: UniProtKB
  3. regulation of translation Source: RGD
  4. response to iron(II) ion Source: UniProtKB
  5. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic aconitate hydratase (EC:4.2.1.3)
Short name:
Aconitase
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 namesi
Name:Aco1
Synonyms:Ireb1, Irebp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2019. Aco1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. cytosol Source: RGD
  3. endoplasmic reticulum Source: RGD
  4. Golgi apparatus Source: MGI
  5. intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 889889Cytoplasmic aconitate hydratasePRO_0000076683Add
BLAST

Proteomic databases

PaxDbiQ63270.
PRIDEiQ63270.

PTM databases

PhosphoSiteiQ63270.

Expressioni

Gene expression databases

GenevestigatoriQ63270.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi248407. 1 interaction.
MINTiMINT-4569119.
STRINGi10116.ENSRNOP00000057501.

Structurei

3D structure databases

ProteinModelPortaliQ63270.
SMRiQ63270. Positions 3-889.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 2073Substrate binding By similarity
Regioni779 – 7802Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1048.
HOGENOMiHOG000025704.
HOVERGENiHBG052147.
KOiK01681.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. 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_2.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63270-1 [UniParc]FASTAAdd to Basket

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MKNPFAHLAE PLDPAQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAVRNC    50
DEFLVKKNDI ENILNWSIMQ HKSIEVPFKP ARVILQDFTG VPAVVDFAAM 100
RDAVKKLGGN PEKINPVCPA DLVIDHSIQV HFNRRADSLQ KNQDLEFERN 150
RERFEFLKWG SQAFCNMRII PPGSGIIHQV NLEYLARVVF DQDGCYYPDS 200
LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP QVIGYKLMGK 250
PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 300
PEYGATAAFF PVDDVSIAYL VQTGREEDKV KHIKRYLQAV GMFRDFSDSS 350
QDPDFTQVVE LDLKTVVPCC SGPKRPQDKV AVSEIEKDFE SCLGAKQGFK 400
GFQVAPDHHN DHKTFIYNDS EFTLAHGSVV IAAITSCTNT SNPSVMLGAG 450
LLAKKAVEAG LNVKPYVKTS LSPGSGVVTY YLRESGVMPY LSQLGFDVVG 500
YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG RVHPNTRANY 550
LASPPLVIAY AIAGTVRIDF EKEPLGVNAQ GQQVFLKDIW PTRDEIQEVE 600
RKYVIPGMFK EVYQKIETVN KSWNALAAPS EKLYAWNPKS TYIKSPPFFE 650
SLTLDLQPPK SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG 700
LTPRDFNSYG SRRGNDAIMA RGTFANIRLL NKFLNKQAPQ TVHLPSGETL 750
DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR DWAAKGPFLL GIKAVLAESY 800
ERTHCSNLVG MGVIPLEYLP GETADSLGLT GRERYTIHIP EHLKPRMKVQ 850
IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMAQ 889
Length:889
Mass (Da):98,128
Last modified:November 1, 1996 - v1
Checksum:i610486302B4362CD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311H → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23874 mRNA. Translation: AAA41449.1.
PIRiA44154.
RefSeqiNP_059017.1. NM_017321.1.
UniGeneiRn.35934.

Genome annotation databases

GeneIDi50655.
KEGGirno:50655.
UCSCiRGD:2019. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23874 mRNA. Translation: AAA41449.1 .
PIRi A44154.
RefSeqi NP_059017.1. NM_017321.1.
UniGenei Rn.35934.

3D structure databases

ProteinModelPortali Q63270.
SMRi Q63270. Positions 3-889.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248407. 1 interaction.
MINTi MINT-4569119.
STRINGi 10116.ENSRNOP00000057501.

PTM databases

PhosphoSitei Q63270.

Proteomic databases

PaxDbi Q63270.
PRIDEi Q63270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 50655.
KEGGi rno:50655.
UCSCi RGD:2019. rat.

Organism-specific databases

CTDi 48.
RGDi 2019. Aco1.

Phylogenomic databases

eggNOGi COG1048.
HOGENOMi HOG000025704.
HOVERGENi HBG052147.
KOi K01681.

Miscellaneous databases

NextBioi 610466.
PROi Q63270.

Gene expression databases

Genevestigatori Q63270.

Family and domain databases

Gene3Di 3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProi IPR015931. 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_2.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
Pfami PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view ]
PRINTSi PR00415. ACONITASE.
SUPFAMi SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsi TIGR01341. aconitase_1. 1 hit.
PROSITEi PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The iron-responsive element binding protein. Purification, cloning, and regulation in rat liver."
    Yu Y., Radisky E.S., Leibold E.A.
    J. Biol. Chem. 267:19005-19010(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 114-134 AND 277-293, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiACOC_RAT
AccessioniPrimary (citable) accession number: Q63270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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