k.) 1990 Oxford University Press
4246 Nucleic Acids Research, Vol. 18, No. 14
The cDNA
of chicken annexin 11
sequence
V.Gerke* and W.Koch Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, D-3400 G6ttingen, FRG Submitted June 19, 1990
EMBL accession
We thank Dr.K.Weber for his support and Dr.R.Hynes for
providing the CEF cDNA library. This work was supported by the Bundesministerium fiir Forschung und Technologie.
REFERENCES 1. Gerke,V. (1989) Cell Motil. Cytsoskeleton 14, 449-454. 2. Johnsson,N., Johnsson,K. and Weber,K. (1988) FEBS Lett. 236, 201 -204. 3. Huang,K., Wallner,B.P., Mattaliano,R.J., Tizard,R., Burne,C., Frey,A., Hession,C., McGray,P., Sinclair,L.K., Chow,E.P., Browning,J.L., Ramachandran,K.L., Tang,J. Smart,J.E. and Pepinsky,R.B. (1986) Cell (Cambridge, Mass.) 46, 191-199. 4. Saris,C.J.M., Tack,B.F., Kristensen,T., Glenney,J.R. and Hunter,T. (1986) Cell (Cambridge, Mass) 46, 201-212. 5. Kristensen,T., Saris,C.J.M., Hunter,T., Hicks,L.J., Noonan,D.J., Glenney,J.R. and Tack,B.F. (1986) Biochemistry 25, 4497-4503.
I
!gTCTACTGTCCATGAAATTTTAAGCAAGCTC M S T V H E L S K L
81
AGTCTGGAAGGAGATCATTCTCTCCCTCCAAGTGCATATGCCACAGTTAAGGCTTACTCAAACTTTGATGCTGACCGGGA
12 161 39 241
CCCGCCGCCAGAGCAGCCTTGCCCGCCCCGGCCAGCATTCTGCCAAC S
L
E
G
D
H
S
92 401
119 481
P
S
A
A
Y
T
V
K
A
S
Y
N
F
A
D
D
R
D
TGCTGCAGCCCTGGAAGCAGCCATCAAGACCAAAGGTGTGGATGAAGTTACCATCATCAACATCCTGACAAACCGCAGCA A A A L
E
A
A
K
T
G
K
D
V
E
V
T
I
I
N
L
I
T
N
S
R
ATGAACAGAGGCAGGATATTGCCTTTGCCTATCAGAGGAGAACCAAAAAGGAACTTTCTGCAGCACTTAAGTCTGCTCTG V E Q R 0 D
65 N 321
P
L
A
F
A
Y
R
R
T
K
E
K
S
L
A
A
S A
K
L
L
TCAGGTCATTTAGAGGCAGTGATCTTGGGCTTGCTGAAGACACCATCACAGTATGATGCGTCTGAACTGAAAGCTGCCAT S G H L E A V I
G
L
L
K
L
T
P
0
S
D
Y
A
S
E
L
K
A
A
M
GAAGGGCCTGGGAACTGATGAAGACACACTTATCGAAATCATTTGCTCACGGACAAATCAGGAGCTTAATGAAATTAATA K G L G T D E D T L I E I 0 C
S
R
T
N
E
L
N
E
I
N
145
GAGTCTATAGGGAAATGTACAAAACAGAACTGGAAAAGGACATTATATCAGACACATCTGGTGACTTCCGCAAGCTAATG R V Y R E M Y K T
561 172
GTTGCCCTGGCCAAGGGCAAAAGGTGTGAAGATACTTCTGTGATTGACTATGAACTGATTGACCAAGACGCTAGGGAGCT V A L A K G K R C E D T S V I E I
641
CTATGATGCTGGTGTCAAGAGAAAGGGAACAGATGTTCCCAAGTGGATCAACATTATGACTGAAAGAAGTGTTCCACATC Y D A G V K R K G T D
199
E
L
E
D
K
S
I
D
V
P
K
W
D
Y
I
S
T
G
D
L
N
I
D
M
T
F
0
E
R
D
R
K
A
S
L
R
V
M
E
P
L
H
225
TGCAGAAAGTGTTTGAAAGGTACAAGAGCTACAGCCCATATGATATGTTGGAGAGCATCAAGAAGGAAGTTAAGGGAGAT 0 K V F E R Y K S Y S P Y D M L E S I K K E V K G D L
801 252
CTGGAGAATGCCTTCCTTAATCTTGTTCAGTGCATTCAGAACAAGCAGCTATACTTTGCAGACAGACTCTATGATTCCAT L E N A F 0 C
881 279
GAAGGGCAAGGGAACCCGTGACAAGGTCCTGATTAGGATTATGGTCTCCCGCTGTGAGGTTGACATGCTGAAAATTAAGA K G K G T R D K
961
GTGAATTCAAGAGGAAATACGGAAAATCCCTCTATTATTTCATCCAGCAAGACACAAAAGGTGATTACCAGAGGGCGCTG O R A L E F K R K Y G K S L Y Y F I 0 0 D T K G D Y
721
L
N
L
0
V
V
L
R
N
I
M
0
K
V
L
S
F
Y
R
C
A
E
D
V
R
D
L
M
D
Y
L
K
S
M
K
304 S
1041 332
1121 1201
1281 1361
CTGAACCTGTGTGGTGGAGAGGACTGAAAGCTGTGATGTGGGAAATGGAAACGCAGAGACATGCCTATCTGCTCTTCGTT L N L C G G E D *
TTACTCCAACCCCCGACAAAATCGAGCCGCCATGCAAACCCTTCCCTGCCCCAATACCTGCCACACCACCACGCCGTGT GCTTCTGGTGCTGCCTGCACTTCTCAGCAGCAGCGCTCTGCTTGGTTCTGCCAAACTTCCTAACAGCGTAAAGCCAGAGA AACTAACATTCCCCAGAGATAAAGGTTAAACGTGCTTGTTGAGGATGCCTCCTTGTGTAATGTTTCTAATAAAACATAAA TAAAACAGAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
* To whom correspondence should be addressed
X53334
ACKNOWLEDGEMENTS
Annexin II (also known as p36, calpactin I, or lipocortin II) is member of the recently described annexin family of calciumand phospholipid-binding proteins. It was originally identified as a major cellular substrate for retroviral tyrosine kinases (for review see 1). We have now cloned the full-length cDNA encoding chicken annexin II. Clones were identified in a Xgtl 1 cDNA library made from chicken embryo fibroblast mRNA (kindly provided by Dr. R.Hynes, MIT, Cambridge, USA) using mouse annexin II cDNA fragments as hybridization probes. Isolated cDNA clones were sequenced and shown to encode the correct protein by comparing the deduced amino acid sequence to the N-terminal sequence of chicken annexin II which had been determined by direct protein sequencing (2). The deduced amino acid sequence of chicken annexin H shows a high degree of similarity to annexin II from other species sharing 90% sequence identity with human (3), murine (4), and bovine (5) annexin II. Species variations cluster in the region between amino acids 24 and 43. a
1
no.
4246 Nucleic Acids Research, Vol. 18, No. 14
The cDNA
of chicken annexin 11
sequence
V.Gerke* and W.Koch Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, D-3400 G6ttingen, FRG Submitted June 19, 1990
EMBL accession
We thank Dr.K.Weber for his support and Dr.R.Hynes for
providing the CEF cDNA library. This work was supported by the Bundesministerium fiir Forschung und Technologie.
REFERENCES 1. Gerke,V. (1989) Cell Motil. Cytsoskeleton 14, 449-454. 2. Johnsson,N., Johnsson,K. and Weber,K. (1988) FEBS Lett. 236, 201 -204. 3. Huang,K., Wallner,B.P., Mattaliano,R.J., Tizard,R., Burne,C., Frey,A., Hession,C., McGray,P., Sinclair,L.K., Chow,E.P., Browning,J.L., Ramachandran,K.L., Tang,J. Smart,J.E. and Pepinsky,R.B. (1986) Cell (Cambridge, Mass.) 46, 191-199. 4. Saris,C.J.M., Tack,B.F., Kristensen,T., Glenney,J.R. and Hunter,T. (1986) Cell (Cambridge, Mass) 46, 201-212. 5. Kristensen,T., Saris,C.J.M., Hunter,T., Hicks,L.J., Noonan,D.J., Glenney,J.R. and Tack,B.F. (1986) Biochemistry 25, 4497-4503.
I
!gTCTACTGTCCATGAAATTTTAAGCAAGCTC M S T V H E L S K L
81
AGTCTGGAAGGAGATCATTCTCTCCCTCCAAGTGCATATGCCACAGTTAAGGCTTACTCAAACTTTGATGCTGACCGGGA
12 161 39 241
CCCGCCGCCAGAGCAGCCTTGCCCGCCCCGGCCAGCATTCTGCCAAC S
L
E
G
D
H
S
92 401
119 481
P
S
A
A
Y
T
V
K
A
S
Y
N
F
A
D
D
R
D
TGCTGCAGCCCTGGAAGCAGCCATCAAGACCAAAGGTGTGGATGAAGTTACCATCATCAACATCCTGACAAACCGCAGCA A A A L
E
A
A
K
T
G
K
D
V
E
V
T
I
I
N
L
I
T
N
S
R
ATGAACAGAGGCAGGATATTGCCTTTGCCTATCAGAGGAGAACCAAAAAGGAACTTTCTGCAGCACTTAAGTCTGCTCTG V E Q R 0 D
65 N 321
P
L
A
F
A
Y
R
R
T
K
E
K
S
L
A
A
S A
K
L
L
TCAGGTCATTTAGAGGCAGTGATCTTGGGCTTGCTGAAGACACCATCACAGTATGATGCGTCTGAACTGAAAGCTGCCAT S G H L E A V I
G
L
L
K
L
T
P
0
S
D
Y
A
S
E
L
K
A
A
M
GAAGGGCCTGGGAACTGATGAAGACACACTTATCGAAATCATTTGCTCACGGACAAATCAGGAGCTTAATGAAATTAATA K G L G T D E D T L I E I 0 C
S
R
T
N
E
L
N
E
I
N
145
GAGTCTATAGGGAAATGTACAAAACAGAACTGGAAAAGGACATTATATCAGACACATCTGGTGACTTCCGCAAGCTAATG R V Y R E M Y K T
561 172
GTTGCCCTGGCCAAGGGCAAAAGGTGTGAAGATACTTCTGTGATTGACTATGAACTGATTGACCAAGACGCTAGGGAGCT V A L A K G K R C E D T S V I E I
641
CTATGATGCTGGTGTCAAGAGAAAGGGAACAGATGTTCCCAAGTGGATCAACATTATGACTGAAAGAAGTGTTCCACATC Y D A G V K R K G T D
199
E
L
E
D
K
S
I
D
V
P
K
W
D
Y
I
S
T
G
D
L
N
I
D
M
T
F
0
E
R
D
R
K
A
S
L
R
V
M
E
P
L
H
225
TGCAGAAAGTGTTTGAAAGGTACAAGAGCTACAGCCCATATGATATGTTGGAGAGCATCAAGAAGGAAGTTAAGGGAGAT 0 K V F E R Y K S Y S P Y D M L E S I K K E V K G D L
801 252
CTGGAGAATGCCTTCCTTAATCTTGTTCAGTGCATTCAGAACAAGCAGCTATACTTTGCAGACAGACTCTATGATTCCAT L E N A F 0 C
881 279
GAAGGGCAAGGGAACCCGTGACAAGGTCCTGATTAGGATTATGGTCTCCCGCTGTGAGGTTGACATGCTGAAAATTAAGA K G K G T R D K
961
GTGAATTCAAGAGGAAATACGGAAAATCCCTCTATTATTTCATCCAGCAAGACACAAAAGGTGATTACCAGAGGGCGCTG O R A L E F K R K Y G K S L Y Y F I 0 0 D T K G D Y
721
L
N
L
0
V
V
L
R
N
I
M
0
K
V
L
S
F
Y
R
C
A
E
D
V
R
D
L
M
D
Y
L
K
S
M
K
304 S
1041 332
1121 1201
1281 1361
CTGAACCTGTGTGGTGGAGAGGACTGAAAGCTGTGATGTGGGAAATGGAAACGCAGAGACATGCCTATCTGCTCTTCGTT L N L C G G E D *
TTACTCCAACCCCCGACAAAATCGAGCCGCCATGCAAACCCTTCCCTGCCCCAATACCTGCCACACCACCACGCCGTGT GCTTCTGGTGCTGCCTGCACTTCTCAGCAGCAGCGCTCTGCTTGGTTCTGCCAAACTTCCTAACAGCGTAAAGCCAGAGA AACTAACATTCCCCAGAGATAAAGGTTAAACGTGCTTGTTGAGGATGCCTCCTTGTGTAATGTTTCTAATAAAACATAAA TAAAACAGAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
* To whom correspondence should be addressed
X53334
ACKNOWLEDGEMENTS
Annexin II (also known as p36, calpactin I, or lipocortin II) is member of the recently described annexin family of calciumand phospholipid-binding proteins. It was originally identified as a major cellular substrate for retroviral tyrosine kinases (for review see 1). We have now cloned the full-length cDNA encoding chicken annexin II. Clones were identified in a Xgtl 1 cDNA library made from chicken embryo fibroblast mRNA (kindly provided by Dr. R.Hynes, MIT, Cambridge, USA) using mouse annexin II cDNA fragments as hybridization probes. Isolated cDNA clones were sequenced and shown to encode the correct protein by comparing the deduced amino acid sequence to the N-terminal sequence of chicken annexin II which had been determined by direct protein sequencing (2). The deduced amino acid sequence of chicken annexin H shows a high degree of similarity to annexin II from other species sharing 90% sequence identity with human (3), murine (4), and bovine (5) annexin II. Species variations cluster in the region between amino acids 24 and 43. a
1
no.
