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Reviewed, UniProtKB/Swiss-Prot Q9CPW2 (ADXL_MOUSE)

Last modified November 24, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adrenodoxin-like protein, mitochondrial
Alternative name(s):
    Ferredoxin-1-like protein
Gene names
Name: Fdx1l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Cofactor

Binds 1 2Fe-2S cluster By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the adrenodoxin/putidaredoxin family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence caution

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

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Ligand2Fe-2S
Iron
Iron-sulfur
Metal-binding
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9CPW2-1)

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.
Isoform 2 (identifier: Q9CPW2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Potential
Chain44 – 174131Adrenodoxin-like protein, mitochondrial
PRO_0000325953

Regions

Domain59 – 1611032Fe-2S ferredoxin-type

Sites

Metal binding961Iron-sulfur (2Fe-2S) By similarity
Metal binding1021Iron-sulfur (2Fe-2S) By similarity
Metal binding1051Iron-sulfur (2Fe-2S) By similarity
Metal binding1421Iron-sulfur (2Fe-2S) By similarity

Natural variations

Alternative sequence1 – 126126Missing in isoform 2.
VSP_032498

Experimental info

Sequence conflict111A → G in BAB26771. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F0E2506668F7038A

FASTA17418,766
        10         20         30         40         50         60 
MAASMARGVS ARVLLRAAGG SWGPRAGHAA VTSRTFGTTG ERRAGEEAAD SPELPRDVVN 

        70         80         90        100        110        120 
VVFVDRSGKR IPVRGKVGDN VLYLAQRHGV DLEGACEASL ACSTCHVYVS EAHLDLLPPP 

       130        140        150        160        170 
EEREDDMLDM APLLQENSRL GCQIVLTPEL EGVEFALPKI TRNFYVDGHI PKPH 

« Hide

Isoform 2.

Checksum: 2AF65C4C2939060F
Show »

FASTA485,432

References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK008401 mRNA. Translation: BAB25650.1.
AK010211 mRNA. Translation: BAB26771.1. Frameshift.
AK020979 mRNA. Translation: BAB32267.1.
BC061189 mRNA. Translation: AAH61189.1.
IPIIPI00132087.
IPI00889305.
RefSeqNP_001034913.1.
UniGeneMm.196137

3D structure databases

HSSPHSSP built from PDB template 1XLQ based on UniProtKB P00259.
ModBaseSearch...

Proteomic databases

PRIDEQ9CPW2.

Genome annotation databases

EnsemblENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677; Mus musculus. [Genome view]
GeneID68165.
KEGGmmu:68165.
NMPDRfig|10090.3.peg.19710.
UCSCuc009okb.1. mouse.

Organism-specific databases

CTD68165.
MGIMGI:1915415. Fdx1l.

Phylogenomic databases

HOVERGENQ9CPW2.
OMADMAPALK
OrthoDBEOG9SFCRM

Gene expression databases

CleanExMM_FDX1L.
GenevestigatorQ9CPW2.

Family and domain databases

InterProIPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSPR00355. ADRENODOXIN.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio326570.
SOURCESearch...

Entry information

Entry nameADXL_MOUSE
AccessionPrimary (citable) accession number: Q9CPW2
Secondary accession number(s): Q6P8M0, Q9CV00
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2001
Last modified: November 24, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents