P R O T E I N S E Q U E N C E D A T A B A S E
of PIR-International
Release 70.03, November 09, 2001
262525 sequences, 89717977 residues
Protein Information Resource (PIR)*
National Biomedical Research Foundation
3900 Reservoir Road, N.W.,
Washington, DC 20007, USA
Japan International Protein Munich Information Center for
Information Database (JIPID) Protein Sequences (MIPS)
Amakubo 1-16-1 GSF-Forschungszentrum f. Umwelt und Gesundheit
Tsukuba 305-0005, Japan am Max-Planck-Instut f. Biochemie
Am Klopferspitz 18, D-82152 Martinsried, FRG
This database may be redistributed without prior consent, provided that
this notice be given to each user and that the words "Derived from" shall
precede this notice if the database has been altered by the redistributor.
Copyright 2000, PIR-International.
*PIR is a registered mark of NBRF.
CCHU
A31764
A05676
I55192
A00001
24-Apr-1984
30-Sep-1991
28-Jul-2000
cytochrome c [validated]
man
Homo sapiens
Evans, M.J.
Scarpulla, R.C.
Proc. Natl. Acad. Sci. U.S.A.
85
1988
9625-9629
The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution.
MUID
89071748
A31764
DNA
1-105
GB
M22877
NID
g181241
PIDN
AAA35732.1
PID
g181242
Matsubara, H.
Smith, E.L.
J. Biol. Chem.
238
1963
2732-2753
Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence.
A05676
protein
2-28;29-46;47-100;101-105
Matsubara, H.
Smith, E.L.
J. Biol. Chem.
237
1962
3575-3576
The amino acid sequence of human heart cytochrome c.
annotation
66-Leu is found in 10% of the molecules in pooled protein
Tanaka, Y.
Ashikari, T.
Shibano, Y.
Amachi, T.
Yoshizumi, H.
Matsubara, H.
J. Biochem.
103
1988
954-961
Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae.
MUID
89008207
I55192
translated from GB/EMBL/DDBJ
mRNA
78-105
GB
D00265
NID
g2897691
PIDN
BAA00187.1
PID
g219557
57/1
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
polymorphism
respiratory chain
product
cytochrome c
2-105
experimental
domain
cytochrome c homology
5-99
modified-site
acetylated amino end (Gly) (in mature form)
2
experimental
binding-site
heme (Cys) (covalent)
15,18
experimental
binding-site
heme iron (His, Met) (axial ligands)
19,81
predicted
105
complete
MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIW
GEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCCZ
A00002
17-Mar-1987
17-Mar-1987
03-Mar-2000
cytochrome c
chimpanzee
Pan troglodytes
Needleman, S.B.
submitted to the Atlas
October
1968
A00002
protein
1-104
Needleman, S.B.
Margoliash, E.
unpublished results, 1966, cited by Margoliash, E., and Fitch, W.M., Ann. N.Y. Acad. Sci. 151, 359-381
1968
annotation
compositions of chymotryptic peptides
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
predicted
binding-site
heme (Cys) (covalent)
14,17
predicted
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
tentative
GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWG
EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMQR
A00003
17-Mar-1987
17-Mar-1987
03-Mar-2000
cytochrome c
rhesus macaque
Macaca mulatta
Rothfus, J.A.
Smith, E.L.
J. Biol. Chem.
240
1965
4277-4283
Amino acid sequence of rhesus monkey heart cytochrome c.
MUID
66045191
compositions of chymotryptic peptides
sequences of residues 55-61 and 68-70
A00003
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
predicted
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
tentative
GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGITWG
EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMKP
A00004
17-Dec-1982
17-Dec-1982
03-Mar-2000
cytochrome c
spider monkey
Ateles sp.
Margoliash, E.
unpublished results, cited by Shelnutt, J.A., Rousseau, D.L., Dethmers, J.K., and Margoliash, E., Biochemistry 20, 6485-6497
1981
A00004
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
predicted
binding-site
heme (Cys) (covalent)
14,17
predicted
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVFKGKRIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQASGFTYTEANKNKGIIWG
EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMS
A23057
A04604
A00009
31-Dec-1990
30-Sep-1991
28-Jul-2000
cytochrome c [validated]
house mouse
Mus musculus
Limbach, K.J.
Wu, R.
Nucleic Acids Res.
13
1985
617-630
Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes.
MUID
85215501
A23057
DNA
1-105
EMBL
X01756
NID
g50618
PIDN
CAA25899.1
PID
g50619
strain BALB/c
Carlson, S.S.
Mross, G.A.
Wilson, A.C.
Mead, R.T.
Wolin, L.D.
Bowers, S.F.
Foley, N.T.
Muijsers, A.O.
Margoliash, E.
Biochemistry
16
1977
1437-1442
Primary structure of mouse, rat, and guinea pig cytochrome c.
MUID
77134768
A04604
protein
2-105
strain BALB/c
57/1
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
product
cytochrome c
2-105
experimental
domain
cytochrome c homology
5-99
modified-site
acetylated amino end (Gly) (in mature form)
2
experimental
binding-site
heme (Cys) (covalent)
15,18
experimental
binding-site
heme iron (His, Met) (axial ligands)
19,81
predicted
105
complete
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW
GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRT
A04605
C28160
A00009
31-Dec-1990
30-Sep-1991
28-Jul-2000
cytochrome c [validated]
Norway rat
Rattus norvegicus
Scarpulla, R.C.
Agne, K.M.
Wu, R.
J. Biol. Chem.
256
1981
6480-6486
Isolation and structure of a rat cytochrome c gene.
MUID
81215609
A04605
DNA
1-105
GB
K00750
GB
M28216
NID
g550511
PIDN
AAA21711.1
PID
g203699
Virbasius, J.V.
Scarpulla, R.C.
J. Biol. Chem.
263
1988
6791-6796
Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants.
MUID
88198250
C28160
mRNA
1-105
GB
M20622
NID
g203722
PIDN
AAA41014.1
PID
g203723
Carlson, S.S.
Mross, G.A.
Wilson, A.C.
Mead, R.T.
Wolin, L.D.
Bowers, S.F.
Foley, N.T.
Muijsers, A.O.
Margoliash, E.
Biochemistry
16
1977
1437-1442
Primary structure of mouse, rat, and guinea pig cytochrome c.
MUID
77134768
annotation
peptide mapping, compositional analysis, and partial sequencing indicate that rat cytochrome c is identical with that of mouse
57/1
cytochrome c
cytochrome c homology
blocked amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
product
cytochrome c
2-105
experimental
domain
cytochrome c homology
5-99
modified-site
blocked amino end (Gly) (in mature form) (probably acetylated)
2
experimental
binding-site
heme (Cys) (covalent)
15,18
experimental
binding-site
heme iron (His, Met) (axial ligands)
19,81
predicted
105
complete
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW
GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRB
A00009
13-Jul-1981
13-Jul-1981
28-Jul-2000
cytochrome c [validated]
domestic rabbit
Oryctolagus cuniculus
Needleman, S.B.
Margoliash, E.
J. Biol. Chem.
241
1966
853-863
Rabbit heart cytochrome c.
MUID
66093127
A00009
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
experimental
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG
EDTLMEYLENPKKYIPGTKMIFAGIKKKDERADLIAYLKKATNE
CCGW
A04608
A00009
31-Dec-1990
31-Dec-1990
28-Jul-2000
cytochrome c [validated]
guanaco
Lama guanicoe
Niece, R.L.
Margoliash, E.
Fitch, W.M.
Biochemistry
16
1977
68-72
Complete amino acid sequence of guanaco (Lama guanicoe) cytochrome c.
MUID
77087753
A04608
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
experimental
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG
EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCCM
A04607
A00009
31-Dec-1990
31-Dec-1990
03-Mar-2000
cytochrome c
Arabian camel
Camelus dromedarius
Sokolovsky, M.
Moldovan, M.
Biochemistry
11
1972
145-149
Primary structure of cytochrome c from the camel, Camelus dromedarius.
MUID
72096652
A04607
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
predicted
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG
EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCWHC
A04606
A00009
31-Dec-1990
31-Dec-1990
03-Mar-2000
cytochrome c
California gray whale
Eschrichtius robustus, Eschrichtius gibbosus
Goldstone, A.
Smith, E.L.
J. Biol. Chem.
241
1966
4480-4486
Amino acid sequence of whale heart cytochrome c.
MUID
67041932
A04606
protein
1-104
cytochrome c
cytochrome c homology
blocked amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
blocked amino end (Gly) (probably acetylated)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
predicted
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG
EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCPG
A00007
17-Mar-1987
17-Mar-1987
28-Jul-2000
cytochrome c [validated]
domestic pig
Sus scrofa domestica
Stewart, J.W.
Margoliash, E.
Can. J. Biochem.
43
1965
1187-1206
The primary structure of the cytochrome c from various organs of the hog.
MUID
66072936
A00007
protein
1-104
cytochrome c
cytochrome c homology
acetylated amino end
chromoprotein
electron transfer
heme
iron
metalloprotein
mitochondrion
oxidative phosphorylation
respiratory chain
domain
cytochrome c homology
4-98
modified-site
acetylated amino end (Gly)
1
experimental
binding-site
heme (Cys) (covalent)
14,17
experimental
binding-site
heme iron (His, Met) (axial ligands)
18,80
predicted
104
complete
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG
EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCBO
A92022
A00007
31-Mar-1992
31-Mar-1992
03-Mar-2000
cytochrome c
cattle
Bos primigenius taurus
Nakashima, T.
Higa, H.
Matsubara, H.
Benson, A.
Yasunobu, K.T.
J. Biol. Chem.
241
1966
1166-1177
The amino acid sequence of bovine heart cytochrome c.
MUID
66132521
A92022
protein
1-104
Tsunasawa, S.
Narita, K.
J. Biochem.
92
1982
607-613 ALERT: data truncated here for web previewing.