XSB2879 : spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) isoform 2 [Homo sapiens]
[ CaMP Format ]
This entry is computationally expanded from SB0061
* Basic Information
| Organism | Homo sapiens (human) |
| Protein Names | Spectrin alpha chain, brain; Spectrin, non-erythroid alpha chain; Alpha-II spectrin; Fodrin alpha chain; spectrin; alpha; non-erythrocytic 1 (alpha-fodrin) isoform 2; non-erythrocytic spectrin alpha |
| Gene Names | SPTAN1; SPTA2; spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) |
| Gene Locus | 9q33-q34; chromosome 9 |
| GO Function | Not available |
* Information From OMIM
Text: The spectrins are a family of widely-distributed filamentous cytoskeletal proteins which have a highly conserved 106-amino acid repeat structure. Spectrins are heterodimers of a constant alpha-chain and variable, tissue-specific beta-chains. Functions of these proteins include regulation of receptor binding and actin crosslinking. Barton et al. (1987) and Leto et al. (1988) used a probe for nonerythroid alpha-spectrin derived from a rat brain cDNA library to map the corresponding gene in man. The findings of somatic cell hybrid studies and in situ hybridization indicated localization in the region 9q33-q34. The cDNA that they used encodes a protein also known as alpha-fodrin. McMahon et al. (1987) cloned the alpha-fodrin gene from a human lung fibroblast cDNA library. From this, they compared the structure of alpha-spectrin and alpha-fodrin with deductions as to their evolution. Birkenmeier et al. (1988) showed that the brain alpha-spectrin gene is located on the centromeric end of mouse chromosome 2 and is not closely linked to any known erythroid or neurologic mutation. They symbolized this gene in the mouse as Spna-2. Leto et al. (1988) found close similarities of sequence in diverse species.
* Structure Information
1. Primary Information
Length: 2472 aa
Average Mass: 284.539 kDa
Monoisotopic Mass: 284.364 kDa
2. Domain Information
Annotated Domains: interpro / pfam / smart / prosite
Computationally Assigned Domains (Pfam+HMMER):
| domain name | begin | end | score | e-value |
|---|---|---|---|---|
| Spectrin 1. | 44 | 147 | 128.0 | 3.1e-35 |
| Spectrin 2. | 149 | 253 | 139.8 | 8.3e-39 |
| Spectrin 3. | 255 | 359 | 139.5 | 1e-38 |
| Spectrin 4. | 361 | 465 | 115.0 | 2.5e-31 |
| Spectrin 5. | 467 | 571 | 131.3 | 3e-36 |
| Spectrin 6. | 573 | 676 | 125.4 | 1.9e-34 |
| Spectrin 7. | 678 | 782 | 146.3 | 9.3e-41 |
| Spectrin 8. | 784 | 888 | 153.3 | 7.5e-43 |
| SH3_1 1. | 970 | 1024 | 78.9 | 1.8e-20 |
| Spectrin 9. | 1091 | 1231 | 71.6 | 2.9e-18 |
| --- cleavage 1176 (inside Spectrin 1091..1231) --- | ||||
| Spectrin 10. | 1233 | 1337 | 149.2 | 1.3e-41 |
| Spectrin 11. | 1339 | 1443 | 119.7 | 9.5e-33 |
| Spectrin 12. | 1445 | 1549 | 127.9 | 3.3e-35 |
| Spectrin 13. | 1551 | 1656 | 100.8 | 4.6e-27 |
| Spectrin 14. | 1658 | 1762 | 135.1 | 2.3e-37 |
| Spectrin 15. | 1764 | 1868 | 146.8 | 6.5e-41 |
| Spectrin 16. | 1870 | 1974 | 130.9 | 4e-36 |
| Spectrin 17. | 1976 | 2081 | 121.0 | 3.8e-33 |
| Spectrin 18. | 2091 | 2195 | 72.2 | 1.9e-18 |
| Spectrin 19. | 2205 | 2310 | 68.7 | 2.1e-17 |
| efhand 1. | 2327 | 2355 | 36.5 | 1e-07 |
| efhand 2. | 2370 | 2398 | 23.4 | 0.00096 |
| efhand_Ca_insen 1. | 2402 | 2471 | 44.6 | 3.8e-10 |
3. Sequence Information
Fasta Sequence: XSB2879.fasta
Amino Acid Sequence and Secondary Structures (PsiPred):
* Cleavage Information
1 [sites]
Cleavage sites (±10aa)
[Site 1] VQAVQQQEVY1176-GMMPRDETDS
Tyr1176 
Gly
 |
|||||||||
| P10 | P9 | P8 | P7 | P6 | P5 | P4 | P3 | P2 | P1 |
|---|---|---|---|---|---|---|---|---|---|
| Val1167 | Gln1168 | Ala1169 | Val1170 | Gln1171 | Gln1172 | Gln1173 | Glu1174 | Val1175 | Tyr1176 |
 |
|||||||||
| P1' | P2' | P3' | P4' | P5' | P6' | P7' | P8' | P9' | P10' |
| Gly1177 | Met1178 | Met1179 | Pro1180 | Arg1181 | Asp1182 | Glu1183 | Thr1184 | Asp1185 | Ser1186 |
Sequence conservation (by blast)
* References
[PubMed ID: 19217883] McMahon LW, Zhang P, Sridharan DM, Lefferts JA, Lambert MW, Knockdown of alphaII spectrin in normal human cells by siRNA leads to chromosomal instability and decreased DNA interstrand cross-link repair. Biochem Biophys Res Commun. 2009 Apr 3;381(2):288-93. Epub 2009 Feb 13.