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9.B.21.1.1
Frataxin (Fxn; FrdA) of 210 aas. Defective in the inherited neuro- and cardio-degenerative disease, Friedreich's ataxia (FA), caused by the deficient expression of frataxin that leads to deleterious alterations in iron metabolism (Chiang et al. 2016).

Accession Number:Q16595
Protein Name:Frataxin, mitochondrial precursor aka Friedreich's ataxia protein aka Fxn
Length:210
Molecular Weight:23135.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Mitochondrion1
Substrate Unknown

Cross database links:

Genevestigator: Q16595
eggNOG: prNOG11242
HEGENOM: HBG125781
RefSeq: NP_000135.2    NP_001155178.1    NP_852090.1   
Entrez Gene ID: 2395   
Pfam: PF01491   
OMIM: 229300  phenotype
606829  gene
KEGG: hsa:2395   

Gene Ontology

GO:0005829 C:cytosol
GO:0005759 C:mitochondrial matrix
GO:0051537 F:2 iron, 2 sulfur cluster binding
GO:0008199 F:ferric iron binding
GO:0008198 F:ferrous iron binding
GO:0034986 F:iron chaperone activity
GO:0005515 F:protein binding
GO:0006879 P:cellular iron ion homeostasis
GO:0006783 P:heme biosynthetic process
GO:0018283 P:iron incorporation into metallo-sulfur cluster
GO:0030307 P:positive regulation of cell growth
GO:0008284 P:positive regulation of cell proliferation
GO:0051349 P:positive regulation of lyase activity
GO:0048554 P:positive regulation of metalloenzyme activity
GO:0051353 P:positive regulation of oxidoreductase activity
GO:0051347 P:positive regulation of transferase activity
GO:0016540 P:protein autoprocessing
GO:0010722 P:regulation of ferrochelatase activity
GO:0010039 P:response to iron ion

References (18)

[1] “Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.”  Campuzano V.et.al.   8596916
[2] “DNA sequence and analysis of human chromosome 9.”  Humphray S.J.et.al.   15164053
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “In vivo maturation of human frataxin.”  Condo I.et.al.   17468497
[5] “Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes.”  Campuzano V.et.al.   9302253
[6] “Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin.”  Koutnikova H.et.al.   9241270
[7] “Maturation of frataxin within mammalian and yeast mitochondria: one-step processing by matrix processing peptidase.”  Gordon D.M.et.al.   10545606
[8] “Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase.”  Branda S.S.et.al.   10428860
[9] “Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates.”  Cavadini P.et.al.   11020385
[10] “A pool of extramitochondrial frataxin that promotes cell survival.”  Condo I.et.al.   16608849
[11] “Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones.”  Shan Y.et.al.   17331979
[12] “Crystal structure of human frataxin.”  Dhe-Paganon S.et.al.   10900192
[13] “Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin.”  Musco G.et.al.   10903947
[14] “Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion.”  Bidichandani S.I.et.al.   9150176
[15] “Identification of a missense mutation in a Friedreich's ataxia patient: implications for diagnosis and carrier studies.”  Bartolo C.et.al.   9779809
[16] “The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene.”  Forrest S.M.et.al.   10732799
[17] “Friedreich's ataxia: point mutations and clinical presentation of compound heterozygotes.”  Cossee M.et.al.   9989622
[18] “A novel missense mutation (L198R) in the Friedreich's ataxia gene.”  Al-Mahdawi S.et.al.   10874325
Structure:
1EKG   1LY7   3S4M   3S5D   3S5E   3S5F   3T3J   3T3K   3T3L   3T3T   [...more]

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FASTA formatted sequence
1:	MWTLGRRAVA GLLASPSPAQ AQTLTRVPRP AELAPLCGRR GLRTDIDATC TPRRASSNQR 
61:	GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF 
121:	EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV 
181:	SLHELLAAEL TKALKTKLDL SSLAYSGKDA