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UniProtKB/Swiss-Prot entry P21399


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACOC_HUMAN
Primary accession number P21399
Secondary accession number Q14652
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on July 15, 1998 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 98)
Name and origin of the protein
Protein name Cytoplasmic aconitate hydratase
Synonyms Aconitase
EC 4.2.1.3
Citrate hydro-lyase
Iron-responsive element-binding protein 1
IRE-BP 1
Iron regulatory protein 1
IRP1
Ferritin repressor protein
Gene name
Name: ACO1
Synonyms: IREB1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/20.1.33; PubMed=1738601 [NCBI, ExPASy, EBI, Israel, Japan]
Hirling H., Emery-Goodman A., Thompson N., Neupert B., Seiser C., Kuehn L.;
"Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation.";
Nucleic Acids Res. 20:33-39(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-889, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2172968 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990).
[4]
SIMILARITY TO ACONITASES AND IPM ISOMERASES.
DOI=10.1093/nar/19.8.1739; PubMed=1903202 [NCBI, ExPASy, EBI, Israel, Japan]
Hentze M.W., Argos P.;
"Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase.";
Nucleic Acids Res. 19:1739-1740(1991).
[5]
FUNCTION AS AN ACONITASE.
PubMed=1946430 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A regulated RNA binding protein also possesses aconitase activity.";
Proc. Natl. Acad. Sci. U.S.A. 88:10109-10113(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z11559; CAA77651.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018103; AAH18103.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M58510; AAA69900.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S26403; S26403.
RefSeq NP_002188.1; -.
UniGene Hs.699191
3D structure databases
PDB
2B3X; X-ray; 2.54 A; A=2-889.[ExPASy / RCSB / EBI]
2B3Y; X-ray; 1.85 A; A/B=2-889.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2B3X; -.
2B3Y; -.
ModBase P21399.
PTM databases
PhosphoSite P21399; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00008485; -.
Organism-specific databases
H-InvDB HIX0007969; -.
HGNC HGNC:117; ACO1.
GenAtlas ACO1.
MIM 100880; gene. [NCBI / EBI]
Orphanet 43115; Aconitase deficiency.
PharmGKB PA24442; -.
GeneCards P21399.
Gene expression databases
ArrayExpress P21399; -.
CleanEx HS_ACO1; -.
GermOnline ENSG00000122729; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from HGNC).
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from MGI).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from MGI).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0003994; Molecular function: aconitate hydratase activity (inferred from direct assay from UniProtKB).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0006101; Biological process: citrate metabolic process (inferred from direct assay from HGNC).
GO:0006099; Biological process: tricarboxylic acid cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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.
IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
Graphical view of domain structure.
Gene3D G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1.
G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.
PANTHER PTHR11670; Aconitase-like_core; 1.
PTHR11670:SF1; Aconitase/Fe_reg_prot_2/AcnD; 1.
Pfam PF00330; Aconitase; 1.
PF00694; Aconitase_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00415; ACONITASE.
ProDom PD000511; Aconitase_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01341; aconitase_1; 1.
PROSITE PS00450; ACONITASE_1; 1.
PS01244; ACONITASE_2; 1.
ProtoNet P21399.
Proteomic databases
PeptideAtlas P21399; -.
Genome annotation databases
Ensembl ENSG00000122729; Homo sapiens. [Contig view]
GeneID 48; -.
KEGG hsa:48; -.
Phylogenomic databases
HOGENOM P21399; -.
HOVERGEN P21399; -.
Other
NextBio 187; -.
SOURCE ACO1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur; Lyase; Metal-binding; RNA-binding; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   889  889     Cytoplasmic aconitate hydratase. PRO_0000076680
METAL   437   437        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   503   503        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   506   506        Iron-sulfur (4Fe-4S) (By similarity). 
HELIX   6     8  3      
STRAND   9    12  4      
STRAND   20    22  3      
HELIX   24    27  4      
HELIX   32    34  3      
HELIX   37    48  12      
STRAND   52    55  4      
HELIX   57    64  8      
HELIX   66    69  4      
TURN   70    73  4      
STRAND   75    78  4      
STRAND   81    86  6      
HELIX   87   106  20      
HELIX   111   113  3      
STRAND   120   123  4      
HELIX   138   163  26      
STRAND   167   170  4      
HELIX   177   183  7      
STRAND   188   192  5      
STRAND   195   198  4      
STRAND   200   205  6      
HELIX   206   214  9      
STRAND   217   220  4      
HELIX   223   230  8      
STRAND   235   238  4      
STRAND   242   249  8      
HELIX   257   271  15      
STRAND   277   282  6      
HELIX   283   285  3      
HELIX   290   298  9      
HELIX   300   303  4      
STRAND   306   309  4      
HELIX   314   322  9      
HELIX   327   340  14      
HELIX   349   351  3      
STRAND   356   362  7      
HELIX   363   365  3      
STRAND   368   371  4      
STRAND   379   381  3      
HELIX   382   384  3      
HELIX   385   394  10      
HELIX   406   408  3      
STRAND   412   417  6      
STRAND   420   425  6      
STRAND   428   434  7      
HELIX   437   440  4      
HELIX   443   458  16      
STRAND   467   471  5      
HELIX   476   484  9      
HELIX   488   493  6      
HELIX   504   507  4      
HELIX   515   524  10      
STRAND   529   535  7      
STRAND   547   551  5      
HELIX   554   563  10      
TURN   570   572  3      
STRAND   575   578  4      
TURN   579   581  3      
STRAND   582   584  3      
HELIX   586   589  4      
HELIX   593   603  11      
HELIX   606   613  8      
TURN   614   618  5      
HELIX   621   625  5      
HELIX   647   649  3      
STRAND   662   671  10      
HELIX   677   680  4      
STRAND   688   690  3      
HELIX   691   698  8      
HELIX   703   705  3      
HELIX   710   712  3      
HELIX   716   721  6      
TURN   722   724  3      
TURN   732   734  3      
STRAND   735   737  3      
STRAND   739   742  4      
TURN   744   746  3      
STRAND   749   751  3      
HELIX   752   761  10      
STRAND   766   769  4      
STRAND   772   774  3      
HELIX   782   789  8      
STRAND   792   798  7      
HELIX   802   810  9      
STRAND   814   818  5      
HELIX   824   827  4      
STRAND   835   837  3      
STRAND   848   853  6      
STRAND   858   863  6      
HELIX   868   876  9      
HELIX   879   888  10      
Sequence information
Length: 889 AA [This is the length of the unprocessed precursor] Molecular weight: 98399 Da [This is the MW of the unprocessed precursor] CRC64: E1A05AF701D46DCB [This is a checksum on the sequence]
        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 

P21399 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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