P81459 (CYC_THUAA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c

Gene names

Name:

cyc

Organism

Thunnus alalunga (Albacore)

Taxonomic identifier

8235 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Neognathi › Neoteleostei › Eurypterygii › Ctenosquamata › Acanthomorpha › Euacanthomorpha › Holacanthopterygii › Acanthopterygii › Euacanthopterygii › Percomorpha › Perciformes › Scombroidei › Scombridae › Scombrinae › Thunnini › Thunnus

Protein attributes

Sequence length	103 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular location	Mitochondrion intermembrane space. Note: Loosely associated with the inner membrane.
Post-translational modification	Binds 1 heme group per subunit.
Sequence similarities	Belongs to the cytochrome c family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 103

103

Cytochrome c

PRO_0000108255

Sites

Metal binding

18

1

Iron (heme axial ligand)

Metal binding

80

1

Iron (heme axial ligand)

Binding site

14

1

Heme (covalent)

Binding site

17

1

Heme (covalent)

Amino acid modifications

Modified residue

1

1

N-acetylglycine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

103

Helix Strand Turn

Details...

Helix

3 – 13

11

Turn

14 – 17

4

Beta strand

27 – 29

3

Helix

50 – 54

5

Helix

61 – 69

9

Helix

71 – 74

4

Helix

88 – 101

14

Sequences

	Sequence		Length	Mass (Da)
	P81459 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 1CBC776EF34A8677	FASTA	103	11,370
	10 20 30 40 50 60 GDVAKGKKTF VQKCAQCHTV ENGGKHKVGP NLWGLFGRKT GQAEGYSYTD ANKSKGIVWN 70 80 90 100 NDTLMEYLEN PKKYIPGTKM IFAGIKKKGE RQDLVAYLKS ATS

References

[1]	"The structure of ferrocytochrome c at 2.45 A resolution." Takano T., Kallai O.B., Swanson R., Dickerson R.E. J. Biol. Chem. 248:5234-5255(1973) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). Tissue: Heart.
[2]	"Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution." Takano T., Dickerson R.E. J. Mol. Biol. 153:79-94(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM. Tissue: Heart.
[3]	"Internal mobility of ferrocytochrome c." Northrup S.H., Pear M.R., McCammon J.A., Karplus M., Takano T. Nature 287:659-660(1980) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF REDUCED FORM. Tissue: Heart.
[4]	"Tuna cytochrome c at 2.0 A resolution. I. Ferricytochrome structure analysis." Swanson R., Trus B.L., Mandel N., Mandel G., Kallai O.B., Dickerson R.E. J. Biol. Chem. 252:759-775(1977) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM. Tissue: Heart.
[5]	"Tuna cytochrome c at 2.0 A resolution. II. Ferrocytochrome structure analysis." Takano T., Trus B.L., Mandel N., Mandel G., Kallai O.B., Swanson R., Dickerson R.E. J. Biol. Chem. 252:776-785(1977) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF REDUCED FORM. Tissue: Heart.
[6]	"Tuna cytochrome c at 2.0-A resolution. III. Coordinate optimization and comparison of structures." Mandel N., Mandel G., Trus B.L., Rosenburg J., Carlson G., Dickerson R.E. J. Biol. Chem. 252:4619-4636(1977) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS.
[7]	"Redox conformation changes in refined tuna cytochrome c." Takano T., Dickerson R.E. Proc. Natl. Acad. Sci. U.S.A. 77:6371-6375(1980) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF OXIDIZED AND REDUCED FORMS. Tissue: Heart.
[8]	"Electron tunneling in protein crystals." Tezcan F.A., Crane B.R., Winkler J.R., Gray H.B. Proc. Natl. Acad. Sci. U.S.A. 98:5002-5006(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ZN-SUBSTITUTED FORMS. Tissue: Heart.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Life shuttle - Issue 76 of November 2006

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I54	X-ray	1.50	A/B	1-103	[»]
1I55	X-ray	2.00	A/B	1-103	[»]
1LFM	X-ray	1.50	A/B	1-103	[»]
3CYT	X-ray	1.80	I/O	1-103	[»]
5CYT	X-ray	1.50	R	1-103	[»]

ProteinModelPortal

P81459.

SMR

P81459. Positions 1-103.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG003023.

Family and domain databases

InterPro

IPR002327. Cyt_c_1A/1B.
IPR009056. Cyt_c_dom.
IPR003088. Cyt_c_I.
[Graphical view]

PANTHER

PTHR11961. PTHR11961. 1 hit.

Pfam

PF00034. Cytochrom_C. 1 hit.
[Graphical view]

PRINTS

PR00604. CYTCHRMECIAB.

SUPFAM

SSF46626. Cytochrome_c. 1 hit.

PROSITE

PS51007. CYTC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P81459.

Entry information

Entry name

CYC_THUAA

Accession

Primary (citable) accession number: P81459

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program