Identifiers and Description

Gene Model Identifier

TTHERM_00348510

Standard Name

BTU1 (Beta TUbulin 1 )

Aliases

PreTt05263 | 36.m00227 | 3703.m00089

Description

BTU1 tubulin; Component of microtubules; forms dimers with alpha-tubulin molecules- which polymerize into filaments and bind microtubule-associated proteins; encoded protein identical to Btu2p

Genome Browser (Macronucleus)

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Genome Browser (Micronucleus)

Full Screen View

External Links

Gene Ontology Annotations

Cellular Component

Molecular Function

Biological Process

Domains

  • ( PF00091 ) Tubulin/FtsZ family, GTPase domain
  • ( PF03953 ) tubulin/FtsZ family, C-terminal domain

Gene Expression Profile

Vegetative Cell Cycle (Zhang et al., 2023)

GeneMania

Tetrahymena Stock Center

  • ( SD01420 )
  • ( SD01833 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with duplicate C-tail"
  • ( SD01834 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with duplicate C-tail"
  • ( SD01839 ) Micronucleus: H4-neo replaces coding of BTU1, heterozygous
  • ( SD01840 ) Micronucleus: H4-neo replaces coding of BTU1, heterozygous
  • ( SD01841 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,432,435D) no WT
  • ( SD01842 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,435D) no WT
  • ( SD01843 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,435D) no WT
  • ( SD01844 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E435D) no WT
  • ( SD01848 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D5 with (E437-442D). Some ATU1 replaced by ATU1 with chimeric α-β hybrid tail."
  • ( SD01913 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,432,433,435D) no WT
  • ( SD01914 ) knockout of btu1 with neo knockout of btu2 with bsr
  • ( SD01915 ) Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,432,433,435D) no WT
  • ( SD01916 ) Macronucleus: ∆BTU1 with H4 driven neo coding
  • ( SD01918 ) ∆BTU1 with H4 driven neo coding
  • ( SD01919 ) Macronucleus: ∆BTU1 with H4 driven neo coding
  • ( SD01942 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: some BTU1::neo1 genes
  • ( SD01943 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: some BTU1::neo1 genes
  • ( SD01998 ) "Micronucleus: BTU1 coding replaced by neo1 BTU2 coding replaced by bsr1 Macronucleus: BTU1 into mac, still btu2 KO with bsr"
  • ( SD02001 )
  • ( SD02009 )
  • ( SD02010 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02011 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02012 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02013 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02014 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02015 ) Micronucleus: BTU1 coding replaced with neo1 cassette; BTU2 is blasticidin KO. Macronucleus: assorted to WT or lost resistance cassettes
  • ( SD02016 ) "Micronucleus: BTU1 coding replaced by neo1 BTU2 coding replaced by bsr1 Macronucleus: BTU1 into mac, still btu2 KO with bsr"
  • ( SD02017 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E437-442 EEEE-E changed to DDDD-D) no WT version; BTU2 is KO"
  • ( SD02018 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E437-442 EEEE-E changed to DDDD-D) no WT version; BTU2 is KO"
  • ( SD02019 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with chimeric α-β hybrid tail."
  • ( SD02020 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with chimeric α-β hybrid tail."
  • ( SD02021 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with chimeric α-β hybrid tail."
  • ( SD02022 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU2 replaced by bsr. BTU1 partially replaced by neo1, some replaced by BTU1-D9 with (E431-442D). Some ATU1 replaced by ATU1 with chimeric α-β hybrid tail."
  • ( SD02122 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,432,433,435D) no WT"
  • ( SD02212 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E431,432,433,435D) no WT BTU2 is KO"
  • ( SD02236 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: HA c-terminal tagged BTU1 into MTT1 locus"
  • ( SD02237 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: HA c-terminal tagged BTU1 into MTT1 locus"
  • ( SD02238 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: HA c-terminal tagged BTU1 into MTT1 locus"
  • ( SD02267 ) Macronucleus: Removed the amino acids REI at positions 2,3,4 ibeta tubulin 1 gene
  • ( SD02268 ) Macronucleus: Removed the amino acids REI at positions 2,3,4 ibeta tubulin 1 gene
  • ( SD02269 ) Macronucleus: Removed the amino acids REI at positions 2,3,4 ibeta tubulin 1 gene
  • ( SD02270 ) Macronucleus: Removed the amino acids REI at positions 2,3,4 ibeta tubulin 1 gene
  • ( SD02481 ) Macronucleus: BTU1 has the REI removed from the MREI at start of protien, BTU2 partically replaced by btu2::neo1
  • ( SD02482 ) Macronucleus: BTU1 has the REI removed from the MREI at start of protien, BTU2 partically replaced by btu2::neo1
  • ( SD02483 ) Macronucleus: BTU1 has the REI removed from the MREI at start of protien, BTU2 partically replaced by btu2::neo1
  • ( SD02484 ) Macronucleus: BTU1 has the REI removed from the MREI at start of protien, BTU2 partically replaced by btu2::neo1
  • ( SD02753 ) Micronucleus: H4-neo replaces coding of BTU1, heterozygous
  • ( SD02964 ) "Micronucleus: knockout of btu1 with neo knockout of btu2 with bsr Macronucleus: BTU1 has only (E437-442 EEEE-E changed to DDDD-D) no WT version; BTU2 is KO."

Homologs

Source Identifier Score
WormBase WBGene00006538 9.997093137033517e-262
Description: locus:tbb-4 Tubulin beta-4 chain status:Partially_confirmed UniProt:P41937 protein_id:CAA86310.1
Tetrahymena borealis EI9_09761.1 9.997093137033517e-262
Description: tubulin/FtsZ family, GTPase domain-containing protein (444 aa)
DictyBase DDB_G0269196 9.997093137033517e-262
Description: tubB on chromosome: 1 position 3261649 to 3263130
Oxytricha Contig8792.0.g74 9.997093137033517e-262
Description: Tubulin/FtsZ family, GTPase domain
SGD YFL037W 9.997093137033517e-262
Description: TUB2 Beta-tubulin; associates with alpha-tubulin (Tub1p and Tub3p) to form tubulin dimer, which polymerizes to form microtubules
Stentor Coeruleus SteCoe_22851 9.997093137033517e-262
Description: None

General Information

No Data fetched for General Information

Associated Literature

  1. Ref:15254268: Thazhath R, Jerka-Dziadosz M, Duan J, Wloga D, Gorovsky MA, Frankel J, Gaertig J (2004) Cell context-specific effects of the beta-tubulin glycylation domain on assembly and size of microtubular organelles. Molecular biology of the cell 15(9):4136-47
  2. Ref:15304567: Smith JJ, Cole ES, Romero DP (2004) Transcriptional control of RAD51 expression in the ciliate Tetrahymena thermophila. Nucleic acids research 32(14):4313-21
  3. Ref:15470250: Smith JJ, Yakisich JS, Kapler GM, Cole ES, Romero DP (2004) A beta-tubulin mutation selectively uncouples nuclear division and cytokinesis in Tetrahymena thermophila. Eukaryotic cell 3(5):1217-26
  4. Ref:11864572: Duan J, Gorovsky MA (2002) Both carboxy-terminal tails of alpha- and beta-tubulin are essential, but either one will suffice. Current biology : CB 12(4):313-6
  5. Ref:11862218: Thazhath R, Liu C, Gaertig J (2002) Polyglycylation domain of beta-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nature cell biology 4(3):256-9
  6. Ref:11891286: Shang Y, Song X, Bowen J, Corstanje R, Gao Y, Gaertig J, Gorovsky MA (2002) A robust inducible-repressible promoter greatly facilitates gene knockouts, conditional expression, and overexpression of homologous and heterologous genes in Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 99(6):3734-9
  7. Ref:10847334: Gaertig J (2000) Molecular mechanisms of microtubular organelle assembly in Tetrahymena. The Journal of eukaryotic microbiology 47(3):185-90
  8. Ref:10831613: Xia L, Hai B, Gao Y, Burnette D, Thazhath R, Duan J, Bré MH, Levilliers N, Gorovsky MA, Gaertig J (2000) Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila. The Journal of cell biology 149(5):1097-106
  9. Ref:10403369: Nakazawa M, Moreira D, Laurent J, Le Guyader H, Fukami Y, Ito K (1999) Biochemical analysis of the interaction between elongation factor 1alpha and alpha/beta-tubulins from a ciliate, Tetrahymena pyriformis. FEBS letters 453(1-2):29-34
  10. Ref:10331805: Gaertig J, Gao Y, Tishgarten T, Clark TG, Dickerson HW (1999) Surface display of a parasite antigen in the ciliate Tetrahymena thermophila. Nature biotechnology 17(5):462-5
  11. Ref:9037049: Hai B, Gorovsky MA (1997) Germ-line knockout heterokaryons of an essential alpha-tubulin gene enable high-frequency gene replacement and a test of gene transfer from somatic to germ-line nuclei in Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 94(4):1310-5
  12. Ref:7804247: Levasseur PJ, Meng Q, Bouck GB (1995) Tubulin genes in the algal protist Euglena gracilis. The Journal of eukaryotic microbiology 41(5):468-77
  13. Ref:7651434: Gu L, Gaertig J, Stargell LA, Gorovsky MA (1995) Gene-specific signal transduction between microtubules and tubulin genes in Tetrahymena thermophila. Molecular and cellular biology 15(9):5173-9
  14. Ref:9072048: Nakamura K, Shigaki Y, Takaya C (1995) Proteolysis of tubulin isotypes within Tetrahymena axonemes. Biological chemistry Hoppe-Seyler 376(12):729-32
  15. Ref:7775576: Gaertig J, Cruz MA, Bowen J, Gu L, Pennock DG, Gorovsky MA (1995) Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila. The Journal of cell biology 129(5):1301-10
  16. Ref:7816630: Gaertig J, Gu L, Hai B, Gorovsky MA (1994) High frequency vector-mediated transformation and gene replacement in Tetrahymena. Nucleic acids research 22(24):5391-8
  17. Ref:7910408: Gaertig J, Thatcher TH, Gu L, Gorovsky MA (1994) Electroporation-mediated replacement of a positively and negatively selectable beta-tubulin gene in Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 91(10):4549-53
  18. Ref:8102497: Mitchison TJ (1993) Localization of an exchangeable GTP binding site at the plus end of microtubules. Science (New York, N.Y.) 261(5124):1044-7
  19. Ref:8102139: Soares H, Galego L, Cóias R, Rodrigues-Pousada C (1993) The mechanisms of tubulin messenger regulation during Tetrahymena pyriformis reciliation. The Journal of biological chemistry 268(22):16623-30
  20. Ref:8221902: Gaertig J, Thatcher TH, McGrath KE, Callahan RC, Gorovsky MA (1993) Perspectives on tubulin isotype function and evolution based on the observation that Tetrahymena thermophila microtubules contain a single alpha- and beta-tubulin. Cell motility and the cytoskeleton 25(3):243-53
  21. Ref:1339345: Dupuis P (1992) The beta-tubulin genes of Paramecium are interrupted by two 27 bp introns. The EMBO journal 11(10):3713-9
  22. Ref:1640053: Nakamura K, Okuya Y, Katahira M, Yoshida S, Wada S, Okuno M (1992) Analysis of tubulin isoforms by two-dimensional gel electrophoresis using SDS-polyacrylamide gel electrophoresis in the first dimension. Journal of biochemical and biophysical methods 24(3-4):195-203
  23. Ref:1902785: Soares H, Cyrne L, Barahona I, Rodrigues-Pousada C (1991) Different patterns of expression of beta-tubulin genes in Tetrahymena pyriformis during reciliation. European journal of biochemistry 197(2):291-9
  24. Ref:1900051: Penque D, Galego L, Rodrigues-Pousada C (1991) Multiple alpha-tubulin isoforms in cilia and cytoskeleton of Tetrahymena pyriformis generated by post-translational modifications. Studies during reciliation. European journal of biochemistry 195(2):487-94
  25. Ref:1689806: Krawczyńska W, Kludkiewicz B (1990) Polyadenylated RNA during DAPI-arrested regeneration of Tetrahymena cilia. Molecular and cellular biochemistry 92(1):53-60
  26. Ref:2470096: Harper DS, Jahn CL (1989) Differential use of termination codons in ciliated protozoa. Proceedings of the National Academy of Sciences of the United States of America 86(9):3252-6
  27. Ref:2768213: Hirano-Ohnishi J, Watanabe Y (1989) Ca2+/calmodulin-dependent phosphorylation of ciliary beta-tubulin in Tetrahymena. Journal of biochemistry 105(6):858-60
  28. Ref:3139885: Barahona I, Soares H, Cyrne L, Penque D, Denoulet P, Rodrigues-Pousada C (1988) Sequence of one alpha- and two beta-tubulin genes of Tetrahymena pyriformis. Structural and functional relationships with other eukaryotic tubulin genes. Journal of molecular biology 202(3):365-82
  29. Ref:3137027: Cóias R, Galego L, Barahona I, Rodrigues-Pousada C (1988) Destabilization of tubulin mRNA during heat shock in Tetrahymena pyriformis. European journal of biochemistry 175(3):467-74
  30. Ref:3901010: Suprenant KA, Hays E, LeCluyse E, Dentler WL (1985) Multiple forms of tubulin in the cilia and cytoplasm of Tetrahymena thermophila. Proceedings of the National Academy of Sciences of the United States of America 82(20):6908-12
  31. Ref:6413210: Little M, Quinlan RA, Hoffman EJ, Ludueña RF (1983) Identification and characterization of axopodial tubulins from Echinosphaerium nucleofilum. European journal of cell biology 31(1):55-61
  32. Ref:6192014: Barahona I, Rodrigues-Pousada C (1983) Site of tubulin synthesis in Tetrahymena pyriformis. FEBS letters 158(2):271-5
  33. Ref:7440655: Gavin RH (1980) The oral apparatus of Tetrahymena. V. Oral apparatus polypeptides and their distribution. Journal of cell science 44( ):317-33
  34. Ref:7458914: Roobol A, Pogson CI, Gull K (1980) Identification and characterization of microtubule proteins from myxamoebae of Physarum polycephalum. The Biochemical journal 189(2):305-12
  35. Ref:111932: Marcaud L, Hayes D (1979) RNA synthesis in starved deciliated Tetrahymena pyriformis. European journal of biochemistry 98(1):267-73
  36. Ref:119852: Fliss ER, Suyama Y (1979) Tetrahymena tubulins and in vitro translation of Tetrahymena RNA. The Journal of protozoology 26(3):505-9

Sequences 

>TTHERM_00348510(coding)
ATGAGAGAAATCGTTCACATCTAGGGTGGTCAATGCGGTAACCAAATTGGTGCTAAGTTC
TGGGAAGTCATTTCCGATGAACACGGTATCGATCCCACTGGTACCTATCATGGTGACTCC
GATTTGCAATTGGAAAGAATCAACGTTTATTACAATGAAGCTACTGGTGGTAGATACGTC
CCCAGAGCTATCTTGATGGACTTAGAACCTGGTACCATGGACTCCGTCAGAGCTGGTCCT
TTCGGTCAACTCTTCAGACCTGATAACTTCGTTTTCGGTCAAACTGGTGCTGGTAACAAC
TGGGCTAAGGGTCACTACACCGAAGGTGCTGAATTAATTGACTCCGTTTTGGATGTTGTC
AGAAAGGAAGCTGAAGGTTGCGATTGCCTCTAAGGTTTCTAAATCACCCACTCCCTCGGT
GGTGGTACTGGTTCTGGTATGGGTACCCTCCTTATTTCCAAGGTCAGAGAAGAATATCCT
GATAGAATCATGGAAACCTTCTCCGTCGTCCCCTCTCCCAAGGTCTCTGATACCGTCGTT
GAACCCTACAATGCCACCCTTTCCGTCCATCAATTGGTCGAAAATGCTGATGAATGTATG
GTCATCGATAACGAAGCTCTTTACGATATCTGCTTCAGAACCCTCAAGCTCACCACCCCC
ACTTATGGTGATCTTAACCACTTGGTCTCTGCTGCCATGTCTGGTGTTACTTGCTGTCTC
AGATTCCCTGGTCAATTGAACTCCGATCTTAGAAAGCTCGCTGTCAACTTGATTCCCTTC
CCTCGTCTCCACTTCTTCATGATTGGTTTCGCTCCCCTTACCTCCAGAGGTTCTCAATAA
TACAGAGCCCTCACTGTTCCTGAATTGACCTAATAAATGTTCGATGCCAAGAATATGATG
TGCGCTGCTGATCCCAGACACGGTAGATATTTGACTGCCTCCGCTCTCTTCAGAGGTAGA
ATGTCCACCAAGGAAGTCGACGAATAAATGCTCAACGTCTAAAACAAGAACTCTTCTTAC
TTCGTTGAATGGATTCCCAACAACATCAAGTCTTCCATTTGTGATATTCCTCCTAAGGGT
CTTAAGATGGCTGTCACCTTCGTTGGTAACTCCACTGCTATCCAAGAAATGTTCAAGAGA
GTCGCTGAATAATTCACTGCTATGTTCAGAAGAAAGGCTTTCTTACATTGGTACACTGGT
GAAGGTATGGACGAAATGGAATTCACTGAAGCTGAATCCAACATGAACGATCTCGTCTCC
GAATATCAACAATATCAAGATGCCACCGCTGAAGAAGAAGGTGAATTCGAAGAAGAAGAA
GGTGAAAACTGA


>TTHERM_00348510(gene)
ATGAGAGAAATCGTTCACATCTAGGGTGGTCAATGCGGTAACCAAATTGGTGCTAAGTTC
TGGGAAGTCATTTCCGATGAACACGGTATCGATCCCACTGGTACCTATCATGGTGACTCC
GATTTGCAATTGGAAAGAATCAACGTTTATTACAATGAAGCTACTGGTGGTAGATACGTC
CCCAGAGCTATCTTGATGGACTTAGAACCTGGTACCATGGACTCCGTCAGAGCTGGTCCT
TTCGGTCAACTCTTCAGACCTGATAACTTCGTTTTCGGTCAAACTGGTGCTGGTAACAAC
TGGGCTAAGGGTCACTACACCGAAGGTGCTGAATTAATTGACTCCGTTTTGGATGTTGTC
AGAAAGGAAGCTGAAGGTTGCGATTGCCTCTAAGGTTTCTAAATCACCCACTCCCTCGGT
GGTGGTACTGGTTCTGGTATGGGTACCCTCCTTATTTCCAAGGTCAGAGAAGAATATCCT
GATAGAATCATGGAAACCTTCTCCGTCGTCCCCTCTCCCAAGGTCTCTGATACCGTCGTT
GAACCCTACAATGCCACCCTTTCCGTCCATCAATTGGTCGAAAATGCTGATGAATGTATG
GTCATCGATAACGAAGCTCTTTACGATATCTGCTTCAGAACCCTCAAGCTCACCACCCCC
ACTTATGGTGATCTTAACCACTTGGTCTCTGCTGCCATGTCTGGTGTTACTTGCTGTCTC
AGATTCCCTGGTCAATTGAACTCCGATCTTAGAAAGCTCGCTGTCAACTTGATTCCCTTC
CCTCGTCTCCACTTCTTCATGATTGGTTTCGCTCCCCTTACCTCCAGAGGTTCTCAATAA
TACAGAGCCCTCACTGTTCCTGAATTGACCTAATAAATGTTCGATGCCAAGAATATGATG
TGCGCTGCTGATCCCAGACACGGTAGATATTTGACTGCCTCCGCTCTCTTCAGAGGTAGA
ATGTCCACCAAGGAAGTCGACGAATAAATGCTCAACGTCTAAAACAAGAACTCTTCTTAC
TTCGTTGAATGGATTCCCAACAACATCAAGTCTTCCATTTGTGATATTCCTCCTAAGGGT
CTTAAGATGGCTGTCACCTTCGTTGGTAACTCCACTGCTATCCAAGAAATGTTCAAGAGA
GTCGCTGAATAATTCACTGCTATGTTCAGAAGAAAGGCTTTCTTACATTGGTACACTGGT
GAAGGTATGGACGAAATGGAATTCACTGAAGCTGAATCCAACATGAACGATCTCGTCTCC
GAATATCAACAATATCAAGATGCCACCGCTGAAGAAGAAGGTGAATTCGAAGAAGAAGAA
GGTGAAAACTGA


>TTHERM_00348510(protein)
MREIVHIQGGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGRYV
PRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVV
RKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVVPSPKVSDTVV
EPYNATLSVHQLVENADECMVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCL
RFPGQLNSDLRKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
CAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSICDIPPKG
LKMAVTFVGNSTAIQEMFKRVAEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEFEEEEGEN