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Protein

Adrenodoxin-like protein, mitochondrial

Gene

Fdx1l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential for heme A and Fe/S protein biosynthesis.By similarity

Cofactori

[2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi102 – 1021Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi105 – 1051Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi142 – 1421Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-MMU-196108. Pregnenolone biosynthesis.
R-MMU-211976. Endogenous sterols.
R-MMU-2395516. Electron transport from NADPH to Ferredoxin.

Names & Taxonomyi

Protein namesi
Recommended name:
Adrenodoxin-like protein, mitochondrial
Alternative name(s):
Ferredoxin-1-like protein
Gene namesi
Name:Fdx1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915415. Fdx1l.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionSequence analysisAdd
BLAST
Chaini44 – 174131Adrenodoxin-like protein, mitochondrialPRO_0000325953Add
BLAST

Proteomic databases

EPDiQ9CPW2.
MaxQBiQ9CPW2.
PaxDbiQ9CPW2.
PRIDEiQ9CPW2.

PTM databases

iPTMnetiQ9CPW2.

Expressioni

Gene expression databases

BgeeiQ9CPW2.
CleanExiMM_FDX1L.
GenevisibleiQ9CPW2. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9CPW2. 1 interaction.
MINTiMINT-4124703.
STRINGi10090.ENSMUSP00000010348.

Structurei

3D structure databases

ProteinModelPortaliQ9CPW2.
SMRiQ9CPW2. Positions 57-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 1611032Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG055801.
InParanoidiQ9CPW2.
OMAiVYVSEAH.
OrthoDBiEOG708W1D.
PhylomeDBiQ9CPW2.
TreeFamiTF354319.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9CPW2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASMARGVS ARVLLRAAGG SWGPRAGHAA VTSRTFGTTG ERRAGEEAAD
60 70 80 90 100
SPELPRDVVN VVFVDRSGKR IPVRGKVGDN VLYLAQRHGV DLEGACEASL
110 120 130 140 150
ACSTCHVYVS EAHLDLLPPP EEREDDMLDM APLLQENSRL GCQIVLTPEL
160 170
EGVEFALPKI TRNFYVDGHI PKPH
Length:174
Mass (Da):18,766
Last modified:June 1, 2001 - v1
Checksum:iF0E2506668F7038A
GO
Isoform 2 (identifier: Q9CPW2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.

Note: No experimental confirmation available.
Show »
Length:48
Mass (Da):5,432
Checksum:i2AF65C4C2939060F
GO

Sequence cautioni

The sequence BAB26771.1 differs from that shown. Reason: Frameshift at position 10. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → G in BAB26771 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 126126Missing in isoform 2. 1 PublicationVSP_032498Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008401 mRNA. Translation: BAB25650.1.
AK010211 mRNA. Translation: BAB26771.1. Frameshift.
AK020979 mRNA. Translation: BAB32267.1.
BC061189 mRNA. Translation: AAH61189.1.
CCDSiCCDS22892.1. [Q9CPW2-1]
RefSeqiNP_001034913.1. NM_001039824.2. [Q9CPW2-1]
UniGeneiMm.490294.

Genome annotation databases

EnsembliENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677. [Q9CPW2-1]
GeneIDi68165.
KEGGimmu:68165.
UCSCiuc009okb.1. mouse. [Q9CPW2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008401 mRNA. Translation: BAB25650.1.
AK010211 mRNA. Translation: BAB26771.1. Frameshift.
AK020979 mRNA. Translation: BAB32267.1.
BC061189 mRNA. Translation: AAH61189.1.
CCDSiCCDS22892.1. [Q9CPW2-1]
RefSeqiNP_001034913.1. NM_001039824.2. [Q9CPW2-1]
UniGeneiMm.490294.

3D structure databases

ProteinModelPortaliQ9CPW2.
SMRiQ9CPW2. Positions 57-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CPW2. 1 interaction.
MINTiMINT-4124703.
STRINGi10090.ENSMUSP00000010348.

PTM databases

iPTMnetiQ9CPW2.

Proteomic databases

EPDiQ9CPW2.
MaxQBiQ9CPW2.
PaxDbiQ9CPW2.
PRIDEiQ9CPW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677. [Q9CPW2-1]
GeneIDi68165.
KEGGimmu:68165.
UCSCiuc009okb.1. mouse. [Q9CPW2-1]

Organism-specific databases

CTDi112812.
MGIiMGI:1915415. Fdx1l.

Phylogenomic databases

eggNOGiKOG3309. Eukaryota.
COG0633. LUCA.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG055801.
InParanoidiQ9CPW2.
OMAiVYVSEAH.
OrthoDBiEOG708W1D.
PhylomeDBiQ9CPW2.
TreeFamiTF354319.

Enzyme and pathway databases

ReactomeiR-MMU-1362409. Mitochondrial iron-sulfur cluster biogenesis.
R-MMU-196108. Pregnenolone biosynthesis.
R-MMU-211976. Endogenous sterols.
R-MMU-2395516. Electron transport from NADPH to Ferredoxin.

Miscellaneous databases

ChiTaRSiFdx1l. mouse.
PROiQ9CPW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPW2.
CleanExiMM_FDX1L.
GenevisibleiQ9CPW2. MM.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Small intestine.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Pancreas and Testis.

Entry informationi

Entry nameiADXL_MOUSE
AccessioniPrimary (citable) accession number: Q9CPW2
Secondary accession number(s): Q6P8M0, Q9CV00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 114 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.