Q9CPW2 (ADXL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adrenodoxin-like protein, mitochondrial

Alternative name(s):
Ferredoxin-1-like protein

Gene names

Name:

Fdx1l

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Electron transport Transport
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 43	43	Mitochondrion Potential
	Chain	44 – 174	131	Adrenodoxin-like protein, mitochondrial		PRO_0000325953
Regions
	Domain	59 – 161	103	2Fe-2S ferredoxin-type
Sites
	Metal binding	96	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	102	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	105	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	142	1	Iron-sulfur (2Fe-2S) By similarity
Natural variations
	Alternative sequence	1 – 126	126	Missing in isoform 2.		VSP_032498
Experimental info
	Sequence conflict	11	1	A → G in BAB26771. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: F0E2506668F7038A	FASTA	174	18,766
	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
	Isoform 2 [UniParc]. Checksum: 2AF65C4C2939060F	FASTA	48	5,432
	10 20 30 40 MLDMAPLLQE NSRLGCQIVL TPELEGVEFA LPKITRNFYV DGHIPKPH

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. , 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
EMBL GenBank DDBJ	AK008401 mRNA. Translation: BAB25650.1. AK010211 mRNA. Translation: BAB26771.1. Frameshift. AK020979 mRNA. Translation: BAB32267.1. BC061189 mRNA. Translation: AAH61189.1.
IPI	IPI00132087. IPI00889305.
RefSeq	NP_001034913.1. NM_001039824.2.
UniGene	Mm.196137.
3D structure databases
HSSP	HSSP built from PDB template 1XLQ based on UniProtKB P00259.
ProteinModelPortal	Q9CPW2.
SMR	Q9CPW2. Positions 56-158.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CPW2.
Proteomic databases
PRIDE	Q9CPW2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677.
GeneID	68165.
KEGG	mmu:68165.
NMPDR	fig|10090.3.peg.19710.
UCSC	uc009okb.1. mouse.
Organism-specific databases
CTD	112812.
MGI	MGI:1915415. Fdx1l.
Phylogenomic databases
GeneTree	ENSGT00530000063577.
HOGENOM	HBG524254.
HOVERGEN	HBG055801.
InParanoid	Q9CPW2.
OMA	EIVNITY.
OrthoDB	EOG4MKNHB.
PhylomeDB	Q9CPW2.
Gene expression databases
Bgee	Q9CPW2.
CleanEx	MM_FDX1L.
Genevestigator	Q9CPW2.
Family and domain databases
InterPro	IPR001055. Adrenodoxin. IPR018298. Adrenodoxin_Fe-S_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
PRINTS	PR00355. ADRENODOXIN.
SUPFAM	SSF54292. Ferredoxin. 1 hit.
PROSITE	PS51085. 2FE2S_FER_2. 1 hit. PS00814. ADX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	326570.
SOURCE	Search...

Entry information

Entry name

ADXL_MOUSE

Accession

Primary (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:	September 21, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program