ACTNA_DICDI
ID ACTNA_DICDI Reviewed; 861 AA.
AC P05095; Q55EP1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alpha-actinin A;
DE AltName: Full=Actin-binding protein A;
DE AltName: Full=F-actin cross-linking protein;
GN Name=abpA; Synonyms=actnA; ORFNames=DDB_G0268632;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX2;
RX PubMed=3622778; DOI=10.1016/0014-5793(87)80962-6;
RA Noegel A., Witke W., Schleicher M.;
RT "Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and
RT highly conserved regions.";
RL FEBS Lett. 221:391-396(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-504, PROTEIN SEQUENCE OF 126-139;
RP 275-285; 293-309; 313-328; 397-405 AND 481-487, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=3745276; DOI=10.1083/jcb.103.3.969;
RA Witke W., Schleicher M., Lottspeich F., Noegel A.;
RT "Studies on the transcription, translation, and structure of alpha-actinin
RT in Dictyostelium discoideum.";
RL J. Cell Biol. 103:969-975(1986).
RN [4]
RP FUNCTION.
RX PubMed=6746725; DOI=10.1083/jcb.99.1.119s;
RA Condeelis J., Vahey M., Carboni J.M., DeMey J., Ogihara S.;
RT "Properties of the 120,000- and 95,000-dalton actin-binding proteins from
RT Dictyostelium discoideum and their possible functions in assembling the
RT cytoplasmic matrix.";
RL J. Cell Biol. 99:119-126(1984).
RN [5]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=3956480; DOI=10.1002/j.1460-2075.1986.tb04178.x;
RA Wallraff E., Schleicher M., Modersitzki M., Rieger D., Isenberg G.,
RA Gerisch G.;
RT "Selection of Dictyostelium mutants defective in cytoskeletal proteins: use
RT of an antibody that binds to the ends of alpha-actinin rods.";
RL EMBO J. 5:61-67(1986).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1732064; DOI=10.1016/0092-8674(92)90205-q;
RA Witke W., Schleicher M., Noegel A.A.;
RT "Redundancy in the microfilament system: abnormal development of
RT Dictyostelium cells lacking two F-actin cross-linking proteins.";
RL Cell 68:53-62(1992).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-742; ASP-744; ASP-746; GLU-753; ASP-778;
RP ASP-780; SER-786 AND GLU-789.
RX PubMed=8486739; DOI=10.1083/jcb.121.3.599;
RA Witke W., Hofmann A., Koeppel B., Schleicher M., Noegel A.A.;
RT "The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical
RT and genetic analysis.";
RL J. Cell Biol. 121:599-606(1993).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=7820857; DOI=10.1002/cm.970290105;
RA Furukawa R., Fechheimer M.;
RT "Differential localization of alpha-actinin and the 30 kD actin-bundling
RT protein in the cleavage furrow, phagocytic cup, and contractile vacuole of
RT Dictyostelium discoideum.";
RL Cell Motil. Cytoskeleton 29:46-56(1994).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8937986; DOI=10.1242/jcs.109.11.2679;
RA Rivero F., Koeppel B., Peracino B., Bozzaro S., Siegert F., Weijer C.J.,
RA Schleicher M., Albrecht R., Noegel A.A.;
RT "The role of the cortical cytoskeleton: F-actin crosslinking proteins
RT protect against osmotic stress, ensure cell size, cell shape and motility,
RT and contribute to phagocytosis and development.";
RL J. Cell Sci. 109:2679-2691(1996).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10411959;
RA Weber I.;
RT "Computer-assisted morphometry of cell-substratum contacts.";
RL Croat. Med. J. 40:334-339(1999).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10413681; DOI=10.1242/jcs.112.16.2737;
RA Rivero F., Furukawa R., Fechheimer M., Noegel A.A.;
RT "Three actin cross-linking proteins, the 34 kDa actin-bundling protein,
RT alpha-actinin and gelation factor (ABP-120), have both unique and redundant
RT roles in the growth and development of Dictyostelium.";
RL J. Cell Sci. 112:2737-2751(1999).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10704840; DOI=10.1016/s0925-4773(99)00292-0;
RA Ponte E., Rivero F., Fechheimer M., Noegel A., Bozzaro S.;
RT "Severe developmental defects in Dictyostelium null mutants for actin-
RT binding proteins.";
RL Mech. Dev. 91:153-161(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 265-502.
RX PubMed=11226153; DOI=10.1093/emboj/20.1.40;
RA Kliche W., Fujita-Becker S., Kollmar M., Manstein D.J., Kull F.J.;
RT "Structure of a genetically engineered molecular motor.";
RL EMBO J. 20:40-46(2001).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein. Increases the actin-stimulated ATPase activity of myosin.
CC Involved in vegetative cell growth, phagocytosis, motility and
CC development, probably through stabilization of the actin network in the
CC cortical cytoskeleton. {ECO:0000269|PubMed:10411959,
CC ECO:0000269|PubMed:10413681, ECO:0000269|PubMed:10704840,
CC ECO:0000269|PubMed:1732064, ECO:0000269|PubMed:3956480,
CC ECO:0000269|PubMed:6746725, ECO:0000269|PubMed:8486739,
CC ECO:0000269|PubMed:8937986}.
CC -!- SUBUNIT: Homodimer; antiparallel. {ECO:0000269|PubMed:3956480}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7820857}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:7820857}. Contractile
CC vacuole {ECO:0000269|PubMed:7820857}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:7820857}. Note=Expressed diffusely throughout the
CC cytoplasm. Accumulates in the cell cortex, contractile vesicle and
CC phagosome.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Levels increase
CC during aggregation (1-6 hours) and are then maintained until late
CC culmination when they start to decrease. {ECO:0000269|PubMed:3745276}.
CC -!- DISRUPTION PHENOTYPE: Cells show a minor impairment of growth under
CC conditions of reduced temperature and hyperosmotic stress. Fruiting
CC body development and spore production on soil plates is strongly
CC impaired in mutants lacking abpA, but is only mildly affected in
CC mutants on agar plates. Double mutants lacking both abpA and abpC show
CC a marked reduction in growth, cell size and resistance to osmotic
CC shock, and decreased motility and phagocytosis rates. Development is
CC blocked at the tip stage of aggregation, although expression of
CC developmentally regulated genes does not appear to be affected. Double
CC mutants lacking abpA and abpB show a significant reduction in growth
CC and a slight reduction in motility. Development appears to proceed
CC normally until culmination when aberrant fruiting bodies are formed.
CC The phenotypes of the double mutants suggests a partial redundancy in
CC the microfilament system. {ECO:0000269|PubMed:10411959,
CC ECO:0000269|PubMed:10413681, ECO:0000269|PubMed:10704840,
CC ECO:0000269|PubMed:1732064, ECO:0000269|PubMed:3956480,
CC ECO:0000269|PubMed:8937986}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; Y00689; CAA68685.1; -; mRNA.
DR EMBL; AAFI02000004; EAL72905.1; -; Genomic_DNA.
DR EMBL; X04324; CAA27855.1; -; Genomic_DNA.
DR PIR; S00103; FADOAA.
DR RefSeq; XP_646979.1; XM_641887.1.
DR PDB; 1G8X; X-ray; 2.80 A; A/B=265-502.
DR PDB; 4PD3; X-ray; 2.84 A; A/B=265-502.
DR PDB; 5I4E; X-ray; 2.25 A; A=265-489.
DR PDB; 5JLH; EM; 3.90 A; F/G=265-502.
DR PDBsum; 1G8X; -.
DR PDBsum; 4PD3; -.
DR PDBsum; 5I4E; -.
DR PDBsum; 5JLH; -.
DR AlphaFoldDB; P05095; -.
DR SMR; P05095; -.
DR STRING; 44689.DDB0191133; -.
DR PaxDb; P05095; -.
DR PRIDE; P05095; -.
DR EnsemblProtists; EAL72905; EAL72905; DDB_G0268632.
DR GeneID; 8616670; -.
DR KEGG; ddi:DDB_G0268632; -.
DR dictyBase; DDB_G0268632; abpA.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_005217_0_2_1; -.
DR InParanoid; P05095; -.
DR OMA; IMILVDP; -.
DR PhylomeDB; P05095; -.
DR Reactome; R-DDI-114608; Platelet degranulation.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013420; RHOU GTPase cycle.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR EvolutionaryTrace; P05095; -.
DR PRO; PR:P05095; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005884; C:actin filament; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0000331; C:contractile vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:dictyBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:dictyBase.
DR GO; GO:0051764; P:actin crosslink formation; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0009267; P:cellular response to starvation; IEP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IGI:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 3.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Calcium; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Direct protein sequencing; Metal-binding;
KW Reference proteome; Repeat; Vacuole.
FT CHAIN 1..861
FT /note="Alpha-actinin A"
FT /id="PRO_0000073445"
FT DOMAIN 22..127
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 136..242
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 240..365
FT /note="Spectrin 1"
FT REPEAT 366..480
FT /note="Spectrin 2"
FT REPEAT 481..601
FT /note="Spectrin 3"
FT REPEAT 602..714
FT /note="Spectrin 4"
FT DOMAIN 729..764
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 765..800
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..239
FT /note="Actin-binding"
FT BINDING 742
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 744
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 748
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 753
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 778
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 780
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 782
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MUTAGEN 742
FT /note="D->A: Abolishes cross-linking activity and reduces
FT calcium binding by 55%; when associated with A-744; A-746
FT and A-753."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 744
FT /note="D->A: Abolishes cross-linking activity and reduces
FT calcium binding by 55%; when associated with A-742; A-746
FT and A-753."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 746
FT /note="D->A: Abolishes cross-linking activity and reduces
FT calcium binding by 55%; when associated with A-742; A-744
FT and A-753."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 753
FT /note="E->A: Abolishes cross-linking activity and reduces
FT calcium binding by 55%; when associated with A-742; A-744
FT and A-746."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 778
FT /note="D->A: Decreases sensitivity to inhibition by
FT calcium; when associated with A-780; A-786 and A-789."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 780
FT /note="D->A: Decreases sensitivity to inhibition by
FT calcium; when associated with A-778; A-786 and A-789."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 786
FT /note="S->A: Decreases sensitivity to inhibition by
FT calcium; when associated with A-778; A-780 and A-789."
FT /evidence="ECO:0000269|PubMed:8486739"
FT MUTAGEN 789
FT /note="E->A: Decreases sensitivity to inhibition by
FT calcium; when associated with A-778; A-780 and A-786."
FT /evidence="ECO:0000269|PubMed:8486739"
FT CONFLICT 78
FT /note="R -> RR (in Ref. 1; CAA68685)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="T -> P (in Ref. 3; CAA27855)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="I -> T (in Ref. 3; CAA27855)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="A -> R (in Ref. 1; CAA68685)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="I -> L (in Ref. 1; CAA68685)"
FT /evidence="ECO:0000305"
FT HELIX 265..289
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 298..314
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 316..336
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:1G8X"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4PD3"
FT HELIX 353..404
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 432..450
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 460..483
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:1G8X"
FT TURN 489..494
FT /evidence="ECO:0007829|PDB:1G8X"
FT TURN 496..501
FT /evidence="ECO:0007829|PDB:1G8X"
SQ SEQUENCE 861 AA; 97358 MW; 17F4364B8059EAFA CRC64;
MSEEPTPVSG NDKQLLNKAW EITQKKTFTA WCNSHLRKLG SSIEQIDTDF TDGIKLAQLL
EVISNDPVFK VNKTPKLRIH NIQNVGLCLK HIESHGVKLV GIGAEELVDK NLKMTLGMIW
TIILRFAIQD ISIEELSAKE ALLLWCQRKT EGYDRVKVGN FHTSFQDGLA FCALIHKHRP
DLINFDSLNK DDKAGNLQLA FDIAEKELDI PKMLDVSDML DVVRPDERSV MTYVAQYYHH
FSASRKAETA GKQVGKVLDT FMLLEQTKSD YLKRANELVQ WINDKQASLE SRDFGDSIES
VQSFMNAHKE YKKTEKPPKG QEVSELEAIY NSLQTKLRLI KREPFVAPAG LTPNEIDSTW
SALEKAEQEH AEALRIELKR QKKIAVLLQK YNRILKKLEN WATTKSVYLG SNETGDSITA
VQAKLKNLEA FDGECQSLEG QSNSDLLSIL AQLTELNYNG VPELTERKDT FFAQQWTGVK
SSAETYKNTL LAELERLQKI EDSLVEFAKR AAQLNVWIEA ADDHVFDPIN VDSVQGVQEI
QEKFDAFLHD QSQQFAELEA LAALTQQLRE LGRSENDYSV ISYDELSAKW NNLLAGIEER
KVQLANELTT QTNNDVLCQS FSVKANEISD YVRVTLDAIS QNTSSDPQEQ LNNIRAIITA
HAEKKPELDE LYTIASQLEE AQVVDNKHTQ HSLESIKLKW DKLNTLAKKN EQVVEGEILA
KQLTGVTAEE LSEFKACFSH FDKDNDNKLN RLEFSSCLKS IGDELTEEQL NQVISKIDTD
GNGTISFEEF IDYMVSSRKG TDSVESTKAA FKVMAEDKDF ITEAQIRAAI SDSKQIDYLL
ASMPAVEGGF DYNSFAEKLY Q
