P13216 (ADX_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adrenodoxin, mitochondrial

Alternative name(s):
Adrenal ferredoxin

Gene names

Name:

FDX1

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	143 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adrenodoxin transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450.
Cofactor	Binds 1 2Fe-2S cluster.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the adrenodoxin/putidaredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Mitochondrion
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 19	›19	Mitochondrion
	Chain	20 – 143	124	Adrenodoxin, mitochondrial		PRO_0000000992
Regions
	Domain	26 – 130	105	2Fe-2S ferredoxin-type
Sites
	Metal binding	65	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	71	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	74	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	111	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	4	1	V → P in AAA82597. Ref.2
	Sequence conflict	16	1	A → S in AAA82597. Ref.2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P13216 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 15BC3DA3067914B7	FASTA	143	15,483
	10 20 30 40 50 60 CSAVAVRTLR PLSLSARAAC SSEDKITVHF INRDGDKLTA KGKPGDSLLD VVVENNLDID 70 80 90 100 110 120 GFGACEGTLA CSTCHLIFED HIFEKLDAIT DEEMDMLDLA YGLTETSRLG CQICLKKSMD 130 140 NMTVRVPEAV ADARQSVDLS KNS

References

[1]	"Deduced amino acid sequence of mature chicken testis ferredoxin." Kagimoto K., McCarthy J.L., Waterman M.R., Kagimoto M. Biochem. Biophys. Res. Commun. 155:379-383(1988) [PubMed: 3415692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	Blanchard R.K., Henry H.L. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-143. Tissue: Kidney.
[3]	"1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins." Skjeldal L., Markley J.L., Coghlan V.M., Vickery L.E. Biochemistry 30:9078-9083(1991) [PubMed: 1909889] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21275 mRNA. Translation: AAA48576.1. U25823 mRNA. Translation: AAA82597.1.
IPI	IPI00821250.
PIR	A31574.
RefSeq	NP_001185597.1. NM_001198668.1.
UniGene	Gga.891.
3D structure databases
ProteinModelPortal	P13216.
SMR	P13216. Positions 24-136.
ModBase	Search...
Protein-protein interaction databases
STRING	P13216.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000027702; ENSGALP00000027649; ENSGALG00000017152.
GeneID	373947.
KEGG	gga:373947.
Organism-specific databases
CTD	2230.
Phylogenomic databases
eggNOG	veNOG19520.
GeneTree	ENSGT00530000063577.
HOGENOM	HBG524254.
HOVERGEN	HBG105056.
InParanoid	P13216.
OrthoDB	EOG4DNF5T.
PhylomeDB	P13216.
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...

Entry information

Entry name

ADX_CHICK

Accession

Primary (citable) accession number: P13216

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	September 21, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program