P26039
EV
Gene name |
Tln1 (Tln) |
Protein name |
Talin-1 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:21894 |
EC number |
|
Protein Class |
TALIN (PTHR19981) |
Descriptions
Talin-1, a FERM domain-containing protein, forms a direct link with integrin adhesion receptors and the actin cytoskeleton and plays an important role in regulating integrin-mediated signaling. Talin function is autoinhibited by intramolecular interactions between the integrin-binding F3 domain within the FERM domain and autoinhibitory domain (R9) within the C-terminal rod domain (Talin rod). Both the small GTPase Rap1 and PIP2 activate talin and promote integrin-mediated cell adhesion.
Autoinhibitory domains (AIDs)
Target domain |
314-403 (Talin head, FERM F3 subdomain) |
Relief mechanism |
Ligand binding, Partner binding |
Assay |
Deletion assay, Mutagenesis experiment, Structural analysis |
Accessory elements
No accessory elements
References
- Goult BT et al. (2009) "The structure of an interdomain complex that regulates talin activity", The Journal of biological chemistry, 284, 15097-106
- Haage A et al. (2020) "Precise coordination of cell-ECM adhesion is essential for efficient melanoblast migration during development", Development (Cambridge, England), 147,
- Song X et al. (2012) "A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion", Cell research, 22, 1533-45
- Goksoy E et al. (2008) "Structural basis for the autoinhibition of talin in regulating integrin activation", Molecular cell, 31, 124-33
- Zeng Y et al. (2015) "The conformational states of talin autoinhibition complex and its activation under forces", Science China. Life sciences, 58, 694-703
- Kopp PM et al. (2010) "Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1", European journal of cell biology, 89, 661-73
- Liao Z et al. (2021) "Optogenetics-based localization of talin to the plasma membrane promotes activation of β3 integrins", The Journal of biological chemistry, 296, 100675
- Zhang H et al. (2016) "Structural and Functional Analysis of a Talin Triple-Domain Module Suggests an Alternative Talin Autoinhibitory Configuration", Structure (London, England : 1993), 24, 721-729
Autoinhibited structure
Activated structure
39 structures for P26039
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1SJ7 | X-ray | 250 A | A/B/C | 482-655 | PDB |
| 1SJ8 | X-ray | 260 A | A | 482-789 | PDB |
| 1T01 | X-ray | 206 A | B | 605-628 | PDB |
| 1U89 | NMR | - | A | 755-889 | PDB |
| 1Y19 | X-ray | 260 A | B/D/F/H/J/L | 209-410 | PDB |
| 1ZW3 | X-ray | 330 A | B | 1628-1652 | PDB |
| 2B0H | NMR | - | A | 1843-1973 | PDB |
| 2G35 | NMR | - | A | 305-404 | PDB |
| 2JSW | NMR | - | A | 2300-2482 | PDB |
| 2KBB | NMR | - | A | 1655-1822 | PDB |
| 2KC1 | NMR | - | A | 1-85 | PDB |
| 2KC2 | NMR | - | A | 86-202 | PDB |
| 2KGX | NMR | - | PDB | ||
| 2KMA | NMR | - | A | 1-202 | PDB |
| 2KVP | NMR | - | A | 1815-1973 | PDB |
| 2L10 | NMR | - | A | 1206-1357 | PDB |
| 2L7A | NMR | - | A | 787-911 | PDB |
| 2L7N | NMR | - | A | 1046-1207 | PDB |
| 2LQG | NMR | - | A | 913-1044 | PDB |
| 2QDQ | X-ray | 220 A | A/B | 2494-2541 | PDB |
| 2X0C | X-ray | 200 A | A | 1359-1659 | PDB |
| 3DYJ | X-ray | 185 A | A/B | 1974-2293 | PDB |
| 3IVF | X-ray | 194 A | A | 1-400 | PDB |
| 3S90 | X-ray | 197 A | C/D | 1512-1546 | PDB |
| 4F7G | X-ray | 205 A | PDB | ||
| 4W8P | X-ray | 150 A | A | 1357-1657 | PDB |
| 5FZT | X-ray | 210 A | A | 1359-1659 | PDB |
| 5IC0 | X-ray | 197 A | A | 1357-1822 | PDB |
| 5IC1 | X-ray | 220 A | A | 1357-1822 | PDB |
| 5NL1 | X-ray | 250 A | A/B/C/D/E/F | 480-635 | PDB |
| 6BA6 | NMR | - | A | 1-86 | PDB |
| 6MFS | X-ray | 285 A | PDB | ||
| 6TWN | X-ray | 228 A | A/B | 1359-1659 | PDB |
| 6VGU | X-ray | 278 A | A | 1-430 | PDB |
| 7V1A | X-ray | 184 A | A | 1357-1657 | PDB |
| 7ZW4 | X-ray | 272 A | A | 1358-1659 | PDB |
| 8AS9 | X-ray | 340 A | C | 1359-1659 | PDB |
| 8IVZ | X-ray | 280 A | A/B | 1357-1653 | PDB |
| AF-P26039-F1 | Predicted | AlphaFoldDB |
130 variants for P26039
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388678357 | 57 | K>Q | No | EVA | |
| rs3388681952 | 65 | G>R | No | EVA | |
| rs3388683586 | 106 | K>R | No | EVA | |
| rs3388668405 | 110 | D>N | No | EVA | |
| rs3388683605 | 125 | D>E | No | EVA | |
| rs3388681983 | 133 | L>P | No | EVA | |
| rs3388668348 | 141 | G>E | No | EVA | |
| rs3388677913 | 156 | K>R | No | EVA | |
| rs3388681978 | 171 | L>F | No | EVA | |
| rs3388681624 | 224 | L>V | No | EVA | |
| rs3388680658 | 265 | F>I | No | EVA | |
| rs3388683590 | 269 | E>A | No | EVA | |
| rs3388668328 | 280 | F>L | No | EVA | |
| rs3393897141 | 283 | H>L | No | EVA | |
| rs3394180716 | 284 | K>E | No | EVA | |
| rs3394224034 | 284 | K>N | No | EVA | |
| rs3394223371 | 287 | G>V | No | EVA | |
| rs3388668371 | 291 | E>V | No | EVA | |
| rs3388681683 | 366 | F>Y | No | EVA | |
| rs3388684500 | 374 | Q>* | No | EVA | |
| rs3388678294 | 393 | A>G | No | EVA | |
| rs3388673017 | 405 | S>I | No | EVA | |
| rs3388673017 | 405 | S>N | No | EVA | |
| rs3388684479 | 411 | L>E | No | EVA | |
| rs3388681907 | 411 | L>V | No | EVA | |
| rs3388661260 | 412 | E>D | No | EVA | |
| rs3388681673 | 441 | K>E | No | EVA | |
| rs3388681619 | 454 | R>H | No | EVA | |
| rs250817076 | 465 | V>M | No | EVA | |
| rs3388677920 | 479 | Q>H | No | EVA | |
| rs3388677839 | 541 | H>Q | No | EVA | |
| rs3388681076 | 555 | A>T | No | EVA | |
| rs3388674939 | 557 | V>M | No | EVA | |
| rs3388674991 | 560 | L>P | No | EVA | |
| rs3388673022 | 561 | T>I | No | EVA | |
| rs3388678289 | 575 | C>* | No | EVA | |
| rs3388674989 | 608 | L>I | No | EVA | |
| rs3412938978 | 613 | K>R | No | EVA | |
| rs3388661202 | 614 | G>C | No | EVA | |
| rs3388680538 | 616 | A>T | No | EVA | |
| rs3394232494 | 636 | N>K | No | EVA | |
| rs3394087256 | 637 | L>R | No | EVA | |
| rs3394224041 | 639 | Q>H | No | EVA | |
| rs3394087272 | 639 | Q>H | No | EVA | |
| rs3394175006 | 639 | Q>P | No | EVA | |
| rs3388678275 | 641 | A>V | No | EVA | |
| rs3388674992 | 647 | A>V | No | EVA | |
| rs3388678376 | 656 | G>R | No | EVA | |
| rs3388678405 | 691 | Q>R | No | EVA | |
| rs3388678401 | 694 | E>D | No | EVA | |
| rs3388668910 | 764 | L>V | No | EVA | |
| rs3388677875 | 773 | A>V | No | EVA | |
| rs3388674937 | 811 | N>T | No | EVA | |
| rs3388661212 | 878 | A>T | No | EVA | |
| rs3388674977 | 897 | L>P | No | EVA | |
| rs3388677867 | 903 | A>T | No | EVA | |
| rs248061000 | 944 | A>G | No | EVA | |
| rs3388668973 | 956 | C>R | No | EVA | |
| rs3388678286 | 977 | P>S | No | EVA | |
| rs3394133952 | 980 | P>T | No | EVA | |
| rs3394087266 | 981 | S>R | No | EVA | |
| rs3388673013 | 988 | A>P | No | EVA | |
| rs3388668369 | 996 | P>L | No | EVA | |
| rs3388668323 | 1017 | A>V | No | EVA | |
| rs3393673107 | 1026 | N>S | No | EVA | |
| rs3394019640 | 1032 | A>T | No | EVA | |
| rs3388680719 | 1059 | N>K | No | EVA | |
| rs3388677923 | 1081 | G>W | No | EVA | |
| rs3393918279 | 1086 | K>E | No | EVA | |
| rs3388678316 | 1091 | L>R | No | EVA | |
| rs3388674948 | 1094 | S>G | No | EVA | |
| rs3388681608 | 1099 | S>G | No | EVA | |
| 1105 | L>P | No | |||
| rs3388681701 | 1133 | Q>* | No | EVA | |
| rs3388674958 | 1137 | G>D | No | EVA | |
| rs3388674911 | 1143 | S>L | No | EVA | |
| rs3388684471 | 1176 | P>A | No | EVA | |
| rs3388674936 | 1177 | G>E | No | EVA | |
| rs3388680660 | 1214 | R>* | No | EVA | |
| rs27831179 | 1227 | S>L | No | EVA | |
| rs3388677859 | 1297 | D>V | No | EVA | |
| rs3388684485 | 1299 | A>V | No | EVA | |
| rs3388677891 | 1381 | V>D | No | EVA | |
| rs3388683560 | 1382 | Q>L | No | EVA | |
| rs3388668386 | 1398 | E>G | No | EVA | |
| rs3388681699 | 1451 | D>E | No | EVA | |
| rs3388680521 | 1453 | N>Y | No | EVA | |
| rs3388684492 | 1470 | A>E | No | EVA | |
| rs3388674967 | 1569 | V>M | No | EVA | |
| rs3388674974 | 1572 | L>M | No | EVA | |
| rs3388668975 | 1656 | P>L | No | EVA | |
| rs3388668922 | 1660 | E>K | No | EVA | |
| rs3412695453 | 1665 | I>T | No | EVA | |
| rs3388674606 | 1677 | Q>H | No | EVA | |
| rs3388683618 | 1711 | H>L | No | EVA | |
| rs3393897093 | 1745 | A>GGSGS* | No | EVA | |
| rs3388680641 | 1749 | A>T | No | EVA | |
| rs3388668375 | 1791 | H>Y | No | EVA | |
| rs3388661240 | 1801 | Q>E | No | EVA | |
| rs3388668346 | 1812 | T>M | No | EVA | |
| rs3388677884 | 1815 | N>K | No | EVA | |
| rs3388673038 | 1817 | A>T | No | EVA | |
| rs3388681702 | 1835 | I>V | No | EVA | |
| rs1134009029 | 1879 | P>L | No | EVA | |
| rs3388683616 | 1887 | N>D | No | EVA | |
| rs3388683575 | 1890 | T>S | No | EVA | |
| rs3388672965 | 1956 | R>S | No | EVA | |
| rs3388677855 | 1974 | G>V | No | EVA | |
| rs3388684483 | 1977 | A>S | No | EVA | |
| rs3388668953 | 2010 | E>V | No | EVA | |
| rs3388674941 | 2032 | V>I | No | EVA | |
| rs3388668366 | 2034 | V>L | No | EVA | |
| rs3388674575 | 2044 | L>V | No | EVA | |
| rs3542218618 | 2057 | R>L | No | EVA | |
| rs3388680646 | 2153 | I>T | No | EVA | |
| 2180 | K>M | No | |||
| rs3388661266 | 2181 | G>D | No | EVA | |
| rs3388674564 | 2309 | L>F | No | EVA | |
| rs3388674564 | 2309 | L>I | No | EVA | |
| rs3388677870 | 2312 | A>P | No | EVA | |
| rs3388677871 | 2313 | A>V | No | EVA | |
| rs3388681070 | 2315 | A>V | No | EVA | |
| rs3388674984 | 2327 | K>R | No | EVA | |
| rs3388677889 | 2347 | E>G | No | EVA | |
| rs3388673014 | 2408 | C>* | No | EVA | |
| rs3388679269 | 2436 | A>P | No | EVA | |
| rs3388678273 | 2460 | G>A | No | EVA | |
| rs3388673018 | 2460 | G>S | No | EVA | |
| rs27831204 | 2470 | L>M | No | EVA | |
| rs3388677892 | 2526 | R>Q | No | EVA |
No associated diseases with P26039
13 regional properties for P26039
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 634 - 895 | IPR000719 |
| domain | Ephrin receptor ligand binding domain | 30 - 208 | IPR001090 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 634 - 891 | IPR001245 |
| conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 184 - 204 | IPR001426-1 |
| conserved_site | Tyrosine-protein kinase, receptor class V, conserved site | 246 - 266 | IPR001426-2 |
| domain | Sterile alpha motif domain | 926 - 993 | IPR001660 |
| domain | Fibronectin type III | 327 - 437 | IPR003961-1 |
| domain | Fibronectin type III | 438 - 533 | IPR003961-2 |
| active_site | Tyrosine-protein kinase, active site | 755 - 767 | IPR008266 |
| binding_site | Protein kinase, ATP binding site | 640 - 666 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 634 - 891 | IPR020635 |
| domain | Ephrin receptor, transmembrane domain | 542 - 631 | IPR027936 |
| domain | Ephrin type-A receptor 8, ligand binding domain | 30 - 202 | IPR034287 |
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR19981 | TALIN |
| PANTHER Subfamily | PTHR19981:SF7 | TALIN-1 |
| PANTHER Protein Class | ||
| PANTHER Pathway Category |
Integrin signalling pathway Talin |
|
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| adherens junction | A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules. |
| cell surface | The external part of the cell wall and/or plasma membrane. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
| ruffle membrane | The portion of the plasma membrane surrounding a ruffle. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| integrin binding | Binding to an integrin. |
| LIM domain binding | Binding to a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions. |
| phosphatidylinositol binding | Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives. |
| phosphatidylserine binding | Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine. |
| structural constituent of cytoskeleton | The action of a molecule that contributes to the structural integrity of a cytoskeletal structure. |
| vinculin binding | Binding to vinculin, a protein found in muscle, fibroblasts, and epithelial cells that binds actin and appears to mediate attachment of actin filaments to integral proteins of the plasma membrane. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cell-cell adhesion | The attachment of one cell to another cell via adhesion molecules. |
| cell-substrate junction assembly | The aggregation, arrangement and bonding together of a set of components to form a junction between a cell and its substrate. |
| cortical actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. |
| integrin activation | The aggregation, arrangement and bonding together of an integrin, a heterodimeric adhesion receptor formed by the non-covalent association of particular alpha and beta subunits, that lead to the increased affinity of the integrin for its extracellular ligands. |
| integrin-mediated signaling pathway | The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. |
14 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q32LP0 | FERMT3 | Fermitin family homolog 3 | Bos taurus (Bovine) | SS |
| P54939 | TLN1 | Talin-1 | Gallus gallus (Chicken) | SS |
| Q9VZI3 | Fit1 | Unc-112-related protein | Drosophila melanogaster (Fruit fly) | SS |
| Q9Y490 | TLN1 | Talin-1 | Homo sapiens (Human) | EV |
| Q9Y4G6 | TLN2 | Talin-2 | Homo sapiens (Human) | SS |
| Q96AC1 | FERMT2 | Fermitin family homolog 2 | Homo sapiens (Human) | SS |
| Q86UX7 | FERMT3 | Fermitin family homolog 3 | Homo sapiens (Human) | EV |
| Q9BQL6 | FERMT1 | Fermitin family homolog 1 | Homo sapiens (Human) | SS |
| Q71LX4 | Tln2 | Talin-2 | Mus musculus (Mouse) | SS |
| Q8K1B8 | Fermt3 | Fermitin family homolog 3 | Mus musculus (Mouse) | SS |
| P59113 | Fermt1 | Fermitin family homolog 1 | Mus musculus (Mouse) | SS |
| Q8CIB5 | Fermt2 | Fermitin family homolog 2 | Mus musculus (Mouse) | SS |
| Q18685 | unc-112 | Protein unc-112 | Caenorhabditis elegans | SS |
| F1Q8X5 | fermt2 | Fermitin family homolog 2 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVALSLKISI | GNVVKTMQFE | PSTMVYDACR | MIRERIPEAL | AGPPNDFGLF | LSDDDPKKGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WLEAGKALDY | YMLRNGDTME | YRKKQRPLKI | RMLDGTVKTI | MVDDSKTVTD | MLMTICARIG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ITNHDEYSLV | RELMEEKKDE | GTGTLRKDKT | LLRDEKKMEK | LKQKLHTDDE | LNWLDHGRTL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| REQGVEEHET | LLLRRKFFYS | DQNVDSRDPV | QLNLLYVQAR | DDILNGSHPV | SFDKACEFAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FQCQIQFGPH | NEQKHKAGFL | DLKDFLPKEY | VKQKGERKIF | QAHKNCGQMS | EIEAKVRYVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LARSLKTYGV | SFFLVKEKMK | GKNKLVPRLL | GITKECVMRV | DEKTKEVIQE | WSLTNIKRWA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASPKSFTLDF | GDYQDGYYSV | QTTEGEQIAQ | LIAGYIDIIL | KKKKSKDHFG | LEGDEESTML |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EDSVSPKKST | VLQQQYNRVG | KVEHGSVALP | AIMRSGASGP | ENFQVGSMPP | AQQQITSGQM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HRGHMPPLTS | AQQALTGTIN | SSMQAVQAAQ | ATLDDFETLP | PLGQDAASKA | WRKNKMDESK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HEIHSQVDAI | TAGTASVVNL | TAGDPAETDY | TAVGCAVTTI | SSNLTEMSRG | VKLLAALLED |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EGGNGRPLLQ | AAKGLAGAVS | ELLRSAQPAS | AEPRQNLLQA | AGNVGQASGE | LLQQIGESDT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DPHFQDVLMQ | LAKAVASAAA | ALVLKAKSVA | QRTEDSGLQT | QVIAAATQCA | LSTSQLVACT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KVVAPTISSP | VCQEQLVEAG | RLVAKAVEGC | VSASQAATED | GQLLRGVGAA | ATAVTQALNE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| LLQHVKAHAT | GAGPAGRYDQ | ATDTILTVTE | NIFSSMGDAG | EMVRQARILA | QATSDLVNAI |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KADAEGESDL | ENSRKLLSAA | KILADATAKM | VEAAKGAAAH | PDSEEQQQRL | REAAEGLRMA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| TNAAAQNAIK | KKLVQRLEHA | AKQAAASATQ | TIAAAQHAAS | APKASAGPQP | LLVQSCKAVA |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| EQIPLLVQGV | RGSQAQPDSP | SAQLALIAAS | QSFLQPGGKM | VAAAKASVPT | IQDQASAMQL |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| SQCAKNLGTA | LAELRTAAQK | AQEACGPLEM | DSALSVVQNL | EKDLQEIKAA | ARDGKLKPLP |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| GETMEKCTQD | LGNSTKAVSS | AIAKLLGEIA | QGNENYAGIA | ARDVAGGLRS | LAQAARGVAA |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| LTSDPAVQAI | VLDTASDVLD | KASSLIEEAK | KASGHPGDPE | SQQRLAQVAK | AVTQALNRCV |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| SCLPGQRDVD | NALRAVGDAS | KRLLSDSLPP | STGTFQEAQS | RLNEAAAGLN | QAATELVQAS |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| RGTPQDLARA | SGRFGQDFST | FLEAGVEMAG | QAPSQEDRAQ | VVSNLKGISM | SSSKLLLAAK |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| ALSTDPASPN | LKSQLAAAAR | AVTDSINQLI | TMCTQQAPGQ | KECDNALRQL | ETVRELLENP |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| VQPINDMSYF | GCLDSVMENS | KVLGEAMTGI | SQNAKNGNLP | EFGDAIATAS | KALCGFTEAA |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| AQAAYLVGVS | DPNSQAGQQG | LVEPTQFARA | NQAIQMACQS | LGEPGCTQAQ | VLSAATIVAK |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| HTSALCNSCR | LASARTANPT | AKRQFVQSAK | EVANSTANLV | KTIKALDGDF | TEENRAQCRA |
| 1570 | 1580 | 1590 | 1600 | 1610 | 1620 |
| ATAPLLEAVD | NLSAFASNPE | FSSVPAQISP | EGRAAMEPIV | ISAKTMLESA | GGLIQTARAL |
| 1630 | 1640 | 1650 | 1660 | 1670 | 1680 |
| AVNPRDPPRW | SVLAGHSRTV | SDSIKKLITS | MRDKAPGQLE | CETAIAALNS | CLRDLDQASL |
| 1690 | 1700 | 1710 | 1720 | 1730 | 1740 |
| AAVSQQLAPR | EGISQEALHT | QMLTAVQEIS | HLIEPLASAA | RAEASQLGHK | VSQMAQYFEP |
| 1750 | 1760 | 1770 | 1780 | 1790 | 1800 |
| LTLAAVGAAS | KTLSHPQQMA | LLDQTKTLAE | SALQLLYTAK | EAGGNPKQAA | HTQEALEEAV |
| 1810 | 1820 | 1830 | 1840 | 1850 | 1860 |
| QMMTEAVEDL | TTTLNEAASA | AGVVGGMVDS | ITQAINQLDE | GPMGDPEGSF | VDYQTTMVRT |
| 1870 | 1880 | 1890 | 1900 | 1910 | 1920 |
| AKAIAVTVQE | MVTKSNTSPE | ELGPLANQLT | SDYGRLASQA | KPAAVAAENE | EIGAHIKHRV |
| 1930 | 1940 | 1950 | 1960 | 1970 | 1980 |
| QELGHGCSAL | VTKAGALQCS | PSDVYTKKEL | IECARRVSEK | VSHVLAALQA | GNRGTQACIT |
| 1990 | 2000 | 2010 | 2020 | 2030 | 2040 |
| AASAVSGIIA | DLDTTIMFAT | AGTLNREGAE | TFADHREGIL | KTAKVLVEDT | KVLVQNAAGS |
| 2050 | 2060 | 2070 | 2080 | 2090 | 2100 |
| QEKLAQAAQS | SVATITRLAD | VVKLGAASLG | AEDPETQVVL | INAVKDVAKA | LGDLISATKA |
| 2110 | 2120 | 2130 | 2140 | 2150 | 2160 |
| AAGKVGDDPA | VWQLKNSAKV | MVTNVTSLLK | TVKAVEDEAT | KGTRALEATT | EHIRQELAVF |
| 2170 | 2180 | 2190 | 2200 | 2210 | 2220 |
| CSPEPPAKTS | TPEDFIRMTK | GITMATAKAV | AAGNSCRQED | VIATANLSRR | AIADMLRACK |
| 2230 | 2240 | 2250 | 2260 | 2270 | 2280 |
| EAAFHPEVAP | DVRLRALHYG | RECANGYLEL | LDHVLLTLQK | PNPDLKQQLT | GHSKRVAGSV |
| 2290 | 2300 | 2310 | 2320 | 2330 | 2340 |
| TELIQAAEAM | KGTEWVDPED | PTVIAENELL | GAAAAIEAAA | KKLEQLKPRA | KPKEADESLN |
| 2350 | 2360 | 2370 | 2380 | 2390 | 2400 |
| FEEQILEAAK | SIAAATSALV | KAASAAQREL | VAQGKVGAIP | ANALDDGQWS | QGLISAARMV |
| 2410 | 2420 | 2430 | 2440 | 2450 | 2460 |
| AAATNNLCEA | ANAAVQGHAS | QEKLISSAKQ | VAASTAQLLV | ACKVKADQDS | EAMKRLQAAG |
| 2470 | 2480 | 2490 | 2500 | 2510 | 2520 |
| NAVKRASDNL | VKAAQKAAAF | EDQENETVVV | KEKMVGGIAQ | IIAAQEEMLR | KERELEEARK |
| 2530 | 2540 | ||||
| KLAQIRQQQY | KFLPSELRDE | H |