ID   TBA1D_BOVIN             Reviewed;         452 AA.
AC   Q2HJ86;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Tubulin alpha-1D chain;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P68363};
DE   Contains:
DE     RecName: Full=Detyrosinated tubulin alpha-1D chain;
GN   Name=TUBA1D;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=6504138; DOI=10.1038/312237a0;
RA   Mitchison T., Kirschner M.;
RT   "Dynamic instability of microtubule growth.";
RL   Nature 312:237-242(1984).
RN   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=2207090; DOI=10.1021/bi00479a022;
RA   Stewart R.J., Farrell K.W., Wilson L.;
RT   "Role of GTP hydrolysis in microtubule polymerization: evidence for a
RT   coupled hydrolysis mechanism.";
RL   Biochemistry 29:6489-6498(1990).
RN   [4]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=7704569; DOI=10.1016/s0960-9822(00)00243-8;
RA   Drechsel D.N., Kirschner M.W.;
RT   "The minimum GTP cap required to stabilize microtubules.";
RL   Curr. Biol. 4:1053-1061(1994).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder
CC       consisting of laterally associated linear protofilaments composed of
CC       alpha- and beta-tubulin heterodimers (PubMed:6504138, PubMed:2207090,
CC       PubMed:7704569). Microtubules grow by the addition of GTP-tubulin
CC       dimers to the microtubule end, where a stabilizing cap forms. Below the
CC       cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of
CC       alpha-tubulin (PubMed:6504138, PubMed:2207090, PubMed:7704569).
CC       {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138,
CC       ECO:0000269|PubMed:7704569}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P68363};
CC   -!- SUBUNIT: Dimer of alpha and beta chains (PubMed:6504138,
CC       PubMed:2207090, PubMed:7704569). A typical microtubule is a hollow
CC       water-filled tube with an outer diameter of 25 nm and an inner diameter
CC       of 15 nM. Alpha-beta heterodimers associate head-to-tail to form
CC       protofilaments running lengthwise along the microtubule wall with the
CC       beta-tubulin subunit facing the microtubule plus end conferring a
CC       structural polarity. Microtubules usually have 13 protofilaments but
CC       different protofilament numbers can be found in some organisms and
CC       specialized cells. {ECO:0000269|PubMed:2207090,
CC       ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138,
CC       ECO:0000269|PubMed:7704569}.
CC   -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation.
CC       {ECO:0000250|UniProtKB:P68363}.
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC       resulting in polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into axonemes
CC       (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC       cells, centrioles, axonemes, and the mitotic spindle. Both
CC       modifications can coexist on the same protein on adjacent residues, and
CC       lowering polyglycylation levels increases polyglutamylation, and
CC       reciprocally. Cilia and flagella glycylation is required for their
CC       stability and maintenance. Flagella glycylation controls sperm
CC       motility. {ECO:0000250|UniProtKB:P68369}.
CC   -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC       resulting in polyglutamate chains on the gamma-carboxyl group (By
CC       similarity). Polyglutamylation plays a key role in microtubule severing
CC       by spastin (SPAST). SPAST preferentially recognizes and acts on
CC       microtubules decorated with short polyglutamate tails: severing
CC       activity by SPAST increases as the number of glutamates per tubulin
CC       rises from one to eight, but decreases beyond this glutamylation
CC       threshold (By similarity). Glutamylation is also involved in cilia
CC       motility (By similarity). {ECO:0000250|UniProtKB:P68369,
CC       ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC       microtubule lumen. This modification has been correlated with increased
CC       microtubule stability, intracellular transport and ciliary assembly.
CC       {ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC       microtubules and is required for normal mitosis and cytokinesis
CC       contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
CC   -!- PTM: Nitration of Tyr-452 is irreversible and interferes with normal
CC       dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC       and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC       tyrosine carboxypeptidase (MATCAP, VASH1 or VASH2) and tubulin tyrosine
CC       ligase (TTL), respectively. {ECO:0000250|UniProtKB:P68369,
CC       ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: [Tubulin alpha-1D chain]: Tyrosination promotes microtubule
CC       interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC       CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation
CC       of dynein-dynactin motility via interaction with DCTN1, which brings
CC       the dynein-dynactin complex into contact with microtubules. In neurons,
CC       tyrosinated tubulins mediate the initiation of retrograde vesicle
CC       transport (By similarity). {ECO:0000250|UniProtKB:P68369,
CC       ECO:0000250|UniProtKB:Q71U36}.
CC   -!- PTM: [Detyrosinated tubulin alpha-1D chain]: Detyrosination is involved
CC       in metaphase plate congression by guiding chromosomes during mitosis:
CC       detyrosination promotes interaction with CENPE, promoting pole-proximal
CC       transport of chromosomes toward the equator (By similarity).
CC       Detyrosination increases microtubules-dependent mechanotransduction in
CC       dystrophic cardiac and skeletal muscle. In cardiomyocytes,
CC       detyrosinated microtubules are required to resist to contractile
CC       compression during contraction: detyrosination promotes association
CC       with desmin (DES) at force-generating sarcomeres, leading to buckled
CC       microtubules and mechanical resistance to contraction (By similarity).
CC       {ECO:0000250|UniProtKB:P68373, ECO:0000250|UniProtKB:Q9BQE3}.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR   EMBL; BC113253; AAI13254.1; -; mRNA.
DR   RefSeq; NP_001039875.1; NM_001046410.1.
DR   PDB; 1JFF; EM; 3.50 A; A=1-452.
DR   PDB; 1SA0; X-ray; 3.58 A; A/C=1-452.
DR   PDB; 1SA1; X-ray; 4.20 A; A/C=1-452.
DR   PDB; 1TVK; EM; 2.89 A; A=1-440.
DR   PDB; 1Z2B; X-ray; 4.10 A; A/C=1-451.
DR   PDB; 2WBE; EM; 9.40 A; A=1-452.
DR   PDB; 2XRP; EM; 8.20 A; B/D/F/H=1-449.
DR   PDB; 3EDL; EM; 28.00 A; F=1-452.
DR   PDB; 3IZ0; EM; 8.60 A; A=1-452.
DR   PDB; 4AQV; EM; 9.70 A; A=1-452.
DR   PDB; 4AQW; EM; 9.50 A; A=1-452.
DR   PDB; 4ATU; EM; 8.30 A; B/D/F/H=1-452.
DR   PDB; 4ATX; EM; 8.20 A; B=1-452.
DR   PDB; 4CK5; EM; 10.00 A; A=1-452.
DR   PDB; 4CK6; EM; 9.20 A; A=1-452.
DR   PDB; 4CK7; EM; 9.20 A; A=1-452.
DR   PDB; 5M5I; EM; 9.30 A; A=1-447.
DR   PDB; 5M5L; EM; 9.30 A; A=1-452.
DR   PDB; 5M5M; EM; 9.30 A; A=1-452.
DR   PDB; 5M5N; EM; 9.30 A; A=1-452.
DR   PDB; 5M5O; EM; 9.30 A; A=1-452.
DR   PDB; 7RRO; EM; 3.40 A; AA/AC/AE/AG/AI/AK/AM/BA/BC/BE/BG/BI/BK/BM/CA/CC/CE/CG/CI/CK/CM/DA/DC/DE/DG/DI/DK/DM/EC/EE=1-452.
DR   PDBsum; 1JFF; -.
DR   PDBsum; 1SA0; -.
DR   PDBsum; 1SA1; -.
DR   PDBsum; 1TVK; -.
DR   PDBsum; 1Z2B; -.
DR   PDBsum; 2WBE; -.
DR   PDBsum; 2XRP; -.
DR   PDBsum; 3EDL; -.
DR   PDBsum; 3IZ0; -.
DR   PDBsum; 4AQV; -.
DR   PDBsum; 4AQW; -.
DR   PDBsum; 4ATU; -.
DR   PDBsum; 4ATX; -.
DR   PDBsum; 4CK5; -.
DR   PDBsum; 4CK6; -.
DR   PDBsum; 4CK7; -.
DR   PDBsum; 5M5I; -.
DR   PDBsum; 5M5L; -.
DR   PDBsum; 5M5M; -.
DR   PDBsum; 5M5N; -.
DR   PDBsum; 5M5O; -.
DR   PDBsum; 7RRO; -.
DR   AlphaFoldDB; Q2HJ86; -.
DR   EMDB; EMD-16435; -.
DR   EMDB; EMD-16436; -.
DR   EMDB; EMD-1788; -.
DR   EMDB; EMD-2078; -.
DR   EMDB; EMD-2095; -.
DR   EMDB; EMD-2098; -.
DR   EMDB; EMD-21919; -.
DR   EMDB; EMD-24664; -.
DR   EMDB; EMD-2533; -.
DR   EMDB; EMD-2534; -.
DR   EMDB; EMD-2535; -.
DR   EMDB; EMD-2536; -.
DR   EMDB; EMD-2537; -.
DR   EMDB; EMD-2538; -.
DR   EMDB; EMD-2539; -.
DR   EMDB; EMD-2540; -.
DR   EMDB; EMD-2541; -.
DR   EMDB; EMD-2542; -.
DR   EMDB; EMD-25649; -.
DR   EMDB; EMD-25658; -.
DR   EMDB; EMD-25664; -.
DR   EMDB; EMD-25674; -.
DR   EMDB; EMD-25897; -.
DR   EMDB; EMD-25908; -.
DR   EMDB; EMD-3445; -.
DR   EMDB; EMD-8546; -.
DR   EMDB; EMD-8547; -.
DR   SMR; Q2HJ86; -.
DR   STRING; 9913.ENSBTAP00000057311; -.
DR   PaxDb; 9913-ENSBTAP00000038183; -.
DR   PeptideAtlas; Q2HJ86; -.
DR   Ensembl; ENSBTAT00000076713.1; ENSBTAP00000057311.1; ENSBTAG00000030973.2.
DR   GeneID; 535605; -.
DR   KEGG; bta:535605; -.
DR   CTD; 535605; -.
DR   VEuPathDB; HostDB:ENSBTAG00000030973; -.
DR   eggNOG; KOG1376; Eukaryota.
DR   GeneTree; ENSGT00950000182825; -.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; Q2HJ86; -.
DR   OMA; MAISREC; -.
DR   OrthoDB; 899149at2759; -.
DR   TreeFam; TF300314; -.
DR   EvolutionaryTrace; Q2HJ86; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000030973; Expressed in oviduct epithelium and 89 other cell types or tissues.
DR   ExpressionAtlas; Q2HJ86; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd02186; alpha_tubulin; 1.
DR   Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR   Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR   Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   PANTHER; PTHR11588; TUBULIN; 1.
DR   PANTHER; PTHR11588:SF292; TUBULIN ALPHA-1D CHAIN; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR   SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase;
KW   Isopeptide bond; Magnesium; Metal-binding; Methylation; Microtubule;
KW   Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..452
FT                   /note="Tubulin alpha-1D chain"
FT                   /id="PRO_0000288849"
FT   CHAIN           1..448
FT                   /note="Detyrosinated tubulin alpha-1D chain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQE3"
FT                   /id="PRO_0000437391"
FT   REGION          432..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..4
FT                   /note="MREC motif"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   COMPBIAS        438..452
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         11
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         144
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         179
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         206
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   BINDING         228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P68363"
FT   SITE            452
FT                   /note="Involved in polymerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT   MOD_RES         282
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P68373"
FT   MOD_RES         446
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P68369"
FT   MOD_RES         452
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q71U36"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           10..26
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            77..80
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           103..106
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            107..111
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           112..127
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          128..138
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          164..168
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           184..195
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            211..215
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            228..231
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           232..238
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            239..243
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           252..259
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           288..295
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            298..300
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          312..315
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          318..322
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           328..335
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          354..357
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            382..384
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           385..399
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            403..405
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           406..409
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            410..412
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   HELIX           415..432
FT                   /evidence="ECO:0007829|PDB:1TVK"
FT   TURN            433..437
FT                   /evidence="ECO:0007829|PDB:1TVK"
SQ   SEQUENCE   452 AA;  50283 MW;  BF41F4296CAC7A56 CRC64;
     MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKELIDLVLD
     RIRKLADQCT GLQGFLIFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGMDSV EGEGEEEEGD EY
//