Reviewed, UniProtKB/Swiss-Prot Q63270 (ACOC_RAT)

Names and origin

Protein names

Recommended 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

Gene names

Name:	Aco1
Synonyms:	Ireb1, Irebp

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	889 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding RNA-binding
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular iron ion homeostasis Inferred from direct assay. Source: RGD regulation of translation Ref.1 Traceable author statement. Source: RGD tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: MGI cytosol Inferred from direct assay. Source: RGD endoplasmic reticulum Inferred from direct assay. Source: RGD microsome Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from direct assay. Source: RGD iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron-responsive element binding Ref.1 Inferred from direct assay. Source: RGD mRNA 5'-UTR binding Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 889	889	Cytoplasmic aconitate hydratase		PRO_0000076683
Sites
	Metal binding	437	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	503	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	506	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	131	1	H → D AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q63270-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 610486302B4362CD	FASTA	889	98,128
	10 20 30 40 50 60 MKNPFAHLAE PLDPAQPGKK FFNLNKLEDS RYGRLPFSIR VLLEAAVRNC DEFLVKKNDI 70 80 90 100 110 120 ENILNWSIMQ HKSIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGN PEKINPVCPA 130 140 150 160 170 180 DLVIDHSIQV HFNRRADSLQ KNQDLEFERN RERFEFLKWG 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 PVDDVSIAYL VQTGREEDKV KHIKRYLQAV GMFRDFSDSS QDPDFTQVVE 370 380 390 400 410 420 LDLKTVVPCC SGPKRPQDKV AVSEIEKDFE SCLGAKQGFK GFQVAPDHHN DHKTFIYNDS 430 440 450 460 470 480 EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEAG LNVKPYVKTS LSPGSGVVTY 490 500 510 520 530 540 YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG 550 560 570 580 590 600 RVHPNTRANY LASPPLVIAY AIAGTVRIDF EKEPLGVNAQ GQQVFLKDIW PTRDEIQEVE 610 620 630 640 650 660 RKYVIPGMFK EVYQKIETVN KSWNALAAPS EKLYAWNPKS TYIKSPPFFE SLTLDLQPPK 670 680 690 700 710 720 SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPRDFNSYG SRRGNDAIMA 730 740 750 760 770 780 RGTFANIRLL NKFLNKQAPQ TVHLPSGETL DVFDAAERYQ QAGLPLIVLA GKEYGSGSSR 790 800 810 820 830 840 DWAAKGPFLL GIKAVLAESY ERTHCSNLVG MGVIPLEYLP GETADSLGLT GRERYTIHIP 850 860 870 880 EHLKPRMKVQ IKLDTGKTFQ AVMRFDTDVE LTYFHNGGIL NYMIRKMAQ

References

[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: 1527027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L23874 mRNA. Translation: AAA41449.1.
IPI	IPI00207003.
PIR	A44154.
RefSeq	NP_059017.1.
UniGene	Rn.35934
3D structure databases
SMR	Q63270. Positions 3-889.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63270.
PTM databases
PhosphoSite	Q63270.
Proteomic databases
PRIDE	Q63270.
Genome annotation databases
Ensembl	ENSRNOT00000008337; ENSRNOP00000008337; ENSRNOG00000005849; Rattus norvegicus. [Genome view] ENSRNOT00000060773; ENSRNOP00000057501; ENSRNOG00000005849; Rattus norvegicus. [Genome view]
GeneID	50655.
KEGG	rno:50655.
UCSC	NM_017321. rat.
Organism-specific databases
CTD	50655.
RGD	2019. Aco1.
Phylogenomic databases
HOVERGEN	Q63270.
Enzyme and pathway databases
BRENDA	4.2.1.3. 248.
Gene expression databases
ArrayExpress	Q63270.
Genevestigator	Q63270.
GermOnline	ENSRNOG00000005849. Rattus norvegicus.
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. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
Gene3D	G3DSA: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.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01341. aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	610466.

Entry information

Entry name

ACOC_RAT

Accession

Primary (citable) accession number: Q63270

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)