SPTN1_CHICK
ID SPTN1_CHICK Reviewed; 2477 AA.
AC P07751;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Spectrin alpha chain, non-erythrocytic 1;
DE AltName: Full=Alpha-II spectrin;
DE AltName: Full=Fodrin alpha chain;
GN Name=SPTAN1; Synonyms=SPTA2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2910879; DOI=10.1083/jcb.108.1.79;
RA Wasenius V.-M., Saraste M., Salven P., Eraemaa M., Holm L., Lehto V.-P.;
RT "Primary structure of the brain alpha-spectrin.";
RL J. Cell Biol. 108:79-93(1989).
RN [2]
RP ERRATUM OF PUBMED:2910879, AND SEQUENCE REVISION.
RA Wasenius V.-M., Saraste M., Salven P., Eraemaa M., Holm L., Lehto V.-P.;
RL J. Cell Biol. 108:1177-1178(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1695-2153.
RX PubMed=4029118; DOI=10.1002/j.1460-2075.1985.tb03797.x;
RA Wasenius V.-M., Saraste M., Knowles J., Virtanen I., Lehto V.-P.;
RT "Sequencing of the chicken non-erythroid spectrin cDNA reveals an internal
RT repetitive structure homologous to the human erythrocyte spectrin.";
RL EMBO J. 4:1425-1430(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 965-1025.
RX PubMed=1279434; DOI=10.1038/359851a0;
RA Musacchio A., Noble M., Pauptit R., Wierenga R.K., Saraste M.;
RT "Crystal structure of a Src-homology 3 (SH3) domain.";
RL Nature 359:851-855(1992).
RN [5]
RP STRUCTURE BY NMR OF 2320-2403.
RX PubMed=7588621; DOI=10.1002/j.1460-2075.1995.tb00175.x;
RA Trave G., Lacombe J.-P., Pfuhl M., Saraste M., Pastore A.;
RT "Molecular mechanism of the calcium-induced conformational change in the
RT spectrin EF-hands.";
RL EMBO J. 14:4922-4931(1995).
RN [6]
RP STRUCTURE BY NMR OF 1763-1872.
RX PubMed=9356261; DOI=10.1006/jmbi.1997.1344;
RA Pascual J., Pfuhl M., Walther D., Saraste M., Nilges M.;
RT "Solution structure of the spectrin repeat: a left-handed antiparallel
RT triple-helical coiled-coil.";
RL J. Mol. Biol. 273:740-751(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 969-1025.
RX PubMed=9699637; DOI=10.1038/1418;
RA Martinez J.C., Pisabarro M.T., Serrano L.;
RT "Obligatory steps in protein folding and the conformational diversity of
RT the transition state.";
RL Nat. Struct. Biol. 5:721-729(1998).
RN [8] {ECO:0007744|PDB:1U4Q, ECO:0007744|PDB:1U5P}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1662-1876.
RX PubMed=15522301; DOI=10.1016/j.jmb.2004.09.019;
RA Kusunoki H., Minasov G., Macdonald R.I., Mondragon A.;
RT "Independent movement, dimerization and stability of tandem repeats of
RT chicken brain alpha-spectrin.";
RL J. Mol. Biol. 344:495-511(2004).
RN [9] {ECO:0007744|PDB:3M0P, ECO:0007744|PDB:3M0Q, ECO:0007744|PDB:3M0R, ECO:0007744|PDB:3M0S, ECO:0007744|PDB:3M0T, ECO:0007744|PDB:3M0U}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 965-1025.
RX PubMed=21358049; DOI=10.1107/s0907444911001715;
RA Camara-Artigas A., Gavira J.A., Casares S., Garcia-Ruiz J.M.,
RA Conejero-Lara F., Allen J.P., Martinez J.C.;
RT "Understanding the polymorphic behaviour of a mutant of the alpha-spectrin
RT SH3 domain by means of two 1.1 Aa resolution structures.";
RL Acta Crystallogr. D 67:189-196(2011).
RN [10] {ECO:0007744|PDB:5M6S}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF 1763-1872.
RX PubMed=28112730; DOI=10.1038/nsmb.3355;
RA Nilsson O.B., Nickson A.A., Hollins J.J., Wickles S., Steward A.,
RA Beckmann R., von Heijne G., Clarke J.;
RT "Cotranslational folding of spectrin domains via partially structured
RT states.";
RL Nat. Struct. Mol. Biol. 24:221-225(2017).
CC -!- FUNCTION: Morphologically, spectrin-like proteins appear to be related
CC to spectrin, showing a flexible rod-like structure. They can bind actin
CC but seem to differ in their calmodulin-binding activity. In
CC nonerythroid tissues, spectrins, in association with some other
CC proteins, may play an important role in membrane organization.
CC -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC capable of forming dimers which can further associate to tetramers.
CC Interacts with ACP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by
CC calpain in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X14518; CAA32662.1; -; Genomic_DNA.
DR EMBL; X14519; CAA32663.1; ALT_SEQ; mRNA.
DR EMBL; X02593; CAB51571.1; ALT_SEQ; mRNA.
DR PIR; A30122; SJCHA.
DR RefSeq; NP_001036003.1; NM_001042538.1.
DR PDB; 1AEY; NMR; -; A=965-1025.
DR PDB; 1AJ3; NMR; -; A=1763-1872.
DR PDB; 1BK2; X-ray; 2.01 A; A=969-1025.
DR PDB; 1CUN; X-ray; 2.00 A; A/B/C=1770-1982.
DR PDB; 1E6G; X-ray; 2.30 A; A=965-1025.
DR PDB; 1E6H; X-ray; 2.01 A; A=965-1025.
DR PDB; 1E7O; X-ray; 3.20 A; A=965-1025.
DR PDB; 1G2B; X-ray; 1.12 A; A=967-1025.
DR PDB; 1H8K; X-ray; 2.70 A; A=965-1025.
DR PDB; 1HD3; X-ray; 1.98 A; A=965-1025.
DR PDB; 1M8M; NMR; -; A=965-1025.
DR PDB; 1NEG; X-ray; 2.30 A; A=965-1024.
DR PDB; 1PWT; X-ray; 1.77 A; A=967-1025.
DR PDB; 1QKW; X-ray; 2.00 A; A=964-1025.
DR PDB; 1QKX; X-ray; 1.80 A; A=964-1025.
DR PDB; 1SHG; X-ray; 1.80 A; A=965-1025.
DR PDB; 1TUC; X-ray; 2.02 A; A=983-1026, A=1030-1090.
DR PDB; 1TUD; X-ray; 1.77 A; A=964-1010.
DR PDB; 1U06; X-ray; 1.49 A; A=965-1025.
DR PDB; 1U4Q; X-ray; 2.50 A; A/B=1662-1982.
DR PDB; 1U5P; X-ray; 2.00 A; A=1662-1876.
DR PDB; 1UUE; X-ray; 2.60 A; A=965-1025.
DR PDB; 2CDT; X-ray; 2.54 A; A=965-1025.
DR PDB; 2F2V; X-ray; 1.85 A; A=965-1025.
DR PDB; 2F2W; X-ray; 1.70 A; A=965-1025.
DR PDB; 2F2X; X-ray; 1.60 A; A=965-1025.
DR PDB; 2JM8; NMR; -; A=965-1025.
DR PDB; 2JM9; NMR; -; A=965-1025.
DR PDB; 2JMA; NMR; -; A=965-1025.
DR PDB; 2JMC; NMR; -; A=983-1025.
DR PDB; 2KR3; NMR; -; A=965-1025.
DR PDB; 2KXD; NMR; -; A=967-1025.
DR PDB; 2LJ3; NMR; -; A=965-1025.
DR PDB; 2NUZ; X-ray; 1.85 A; A=965-1025.
DR PDB; 2OAW; X-ray; 1.90 A; A/B/C/D=969-1025.
DR PDB; 2RMO; NMR; -; A=965-1025.
DR PDB; 2ROT; NMR; -; A=965-1025.
DR PDB; 3I9Q; X-ray; 1.45 A; A=969-1025.
DR PDB; 3M0P; X-ray; 2.60 A; A=965-1025.
DR PDB; 3M0Q; X-ray; 1.75 A; A=965-1025.
DR PDB; 3M0R; X-ray; 1.10 A; A=965-1025.
DR PDB; 3M0S; X-ray; 1.60 A; A=969-1025.
DR PDB; 3M0T; X-ray; 1.70 A; A=965-1025.
DR PDB; 3M0U; X-ray; 1.10 A; A=965-1025.
DR PDB; 3NGP; X-ray; 1.08 A; A=965-1025.
DR PDB; 4F16; X-ray; 1.93 A; A=965-1025.
DR PDB; 4F17; X-ray; 1.55 A; A=965-1025.
DR PDB; 5IHI; X-ray; 1.45 A; A=965-1025.
DR PDB; 5IHK; X-ray; 1.35 A; A=965-1025.
DR PDB; 5IHN; X-ray; 1.50 A; A=965-1025.
DR PDB; 5M6S; EM; 4.80 A; A=1764-1872.
DR PDB; 7S4R; X-ray; 2.10 A; A=970-1025.
DR PDBsum; 1AEY; -.
DR PDBsum; 1AJ3; -.
DR PDBsum; 1BK2; -.
DR PDBsum; 1CUN; -.
DR PDBsum; 1E6G; -.
DR PDBsum; 1E6H; -.
DR PDBsum; 1E7O; -.
DR PDBsum; 1G2B; -.
DR PDBsum; 1H8K; -.
DR PDBsum; 1HD3; -.
DR PDBsum; 1M8M; -.
DR PDBsum; 1NEG; -.
DR PDBsum; 1PWT; -.
DR PDBsum; 1QKW; -.
DR PDBsum; 1QKX; -.
DR PDBsum; 1SHG; -.
DR PDBsum; 1TUC; -.
DR PDBsum; 1TUD; -.
DR PDBsum; 1U06; -.
DR PDBsum; 1U4Q; -.
DR PDBsum; 1U5P; -.
DR PDBsum; 1UUE; -.
DR PDBsum; 2CDT; -.
DR PDBsum; 2F2V; -.
DR PDBsum; 2F2W; -.
DR PDBsum; 2F2X; -.
DR PDBsum; 2JM8; -.
DR PDBsum; 2JM9; -.
DR PDBsum; 2JMA; -.
DR PDBsum; 2JMC; -.
DR PDBsum; 2KR3; -.
DR PDBsum; 2KXD; -.
DR PDBsum; 2LJ3; -.
DR PDBsum; 2NUZ; -.
DR PDBsum; 2OAW; -.
DR PDBsum; 2RMO; -.
DR PDBsum; 2ROT; -.
DR PDBsum; 3I9Q; -.
DR PDBsum; 3M0P; -.
DR PDBsum; 3M0Q; -.
DR PDBsum; 3M0R; -.
DR PDBsum; 3M0S; -.
DR PDBsum; 3M0T; -.
DR PDBsum; 3M0U; -.
DR PDBsum; 3NGP; -.
DR PDBsum; 4F16; -.
DR PDBsum; 4F17; -.
DR PDBsum; 5IHI; -.
DR PDBsum; 5IHK; -.
DR PDBsum; 5IHN; -.
DR PDBsum; 5M6S; -.
DR PDBsum; 7S4R; -.
DR AlphaFoldDB; P07751; -.
DR BMRB; P07751; -.
DR SASBDB; P07751; -.
DR SMR; P07751; -.
DR MINT; P07751; -.
DR STRING; 9031.ENSGALP00000038979; -.
DR PaxDb; P07751; -.
DR PRIDE; P07751; -.
DR GeneID; 374234; -.
DR KEGG; gga:374234; -.
DR CTD; 6709; -.
DR VEuPathDB; HostDB:geneid_374234; -.
DR eggNOG; KOG0040; Eukaryota.
DR InParanoid; P07751; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; P07751; -.
DR EvolutionaryTrace; P07751; -.
DR PRO; PR:P07751; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 13.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Calcium; Calmodulin-binding;
KW Cytoplasm; Cytoskeleton; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..2477
FT /note="Spectrin alpha chain, non-erythrocytic 1"
FT /id="PRO_0000073454"
FT REPEAT 45..146
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 150..251
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..358
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 361..465
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 468..570
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 574..676
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 679..781
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 785..888
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 891..969
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 967..1026
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1096..1162
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1234..1336
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1339..1442
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1446..1549
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1552..1661
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1664..1767
FT /note="Spectrin 15"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15522301"
FT REPEAT 1769..1873
FT /note="Spectrin 16"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15522301,
FT ECO:0000305|PubMed:28112730, ECO:0000305|PubMed:9356261"
FT REPEAT 1876..1979
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1983..2086
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2097..2199
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2211..2315
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2328..2363
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2371..2406
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2409..2444
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..14
FT /note="N-terminal domain"
FT REGION 2257..2477
FT /note="C-terminal domain"
FT BINDING 2341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 1176..1177
FT /note="Cleavage; by mu-calpain"
FT /evidence="ECO:0000250"
FT MOD_RES 1176
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT STRAND 952..956
FT /evidence="ECO:0007829|PDB:1TUD"
FT HELIX 957..959
FT /evidence="ECO:0007829|PDB:1TUD"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:1G2B"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:1G2B"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:3NGP"
FT STRAND 981..984
FT /evidence="ECO:0007829|PDB:1H8K"
FT STRAND 993..998
FT /evidence="ECO:0007829|PDB:3NGP"
FT STRAND 1001..1009
FT /evidence="ECO:0007829|PDB:3NGP"
FT STRAND 1012..1017
FT /evidence="ECO:0007829|PDB:3NGP"
FT HELIX 1018..1020
FT /evidence="ECO:0007829|PDB:3NGP"
FT STRAND 1021..1023
FT /evidence="ECO:0007829|PDB:3NGP"
FT STRAND 1034..1036
FT /evidence="ECO:0007829|PDB:1TUC"
FT HELIX 1664..1686
FT /evidence="ECO:0007829|PDB:1U5P"
FT HELIX 1695..1730
FT /evidence="ECO:0007829|PDB:1U5P"
FT STRAND 1733..1735
FT /evidence="ECO:0007829|PDB:1U5P"
FT HELIX 1771..1791
FT /evidence="ECO:0007829|PDB:1CUN"
FT HELIX 1801..1837
FT /evidence="ECO:0007829|PDB:1CUN"
FT HELIX 1843..1898
FT /evidence="ECO:0007829|PDB:1CUN"
FT HELIX 1907..1944
FT /evidence="ECO:0007829|PDB:1CUN"
FT HELIX 1949..1981
FT /evidence="ECO:0007829|PDB:1CUN"
SQ SEQUENCE 2477 AA; 285363 MW; AD4C876994E6AB39 CRC64;
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ RDADELGKWI
QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV KLDETGNQMI NEGHFASETI
RTRLQELHRL WELLLEKMRE KGVKLLQAQK LVQFLRECED VMDWINDKEA IVTSEELGQD
LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNASWQRL
KGLAQQRQGK LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL
ERDLAAFHHK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA AERHARLNDS
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFRSA
DESGQALLAA GHYASDEVKE KLTILSDERS ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
MDDVATRRDA LLSRRNALHE RAMKRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA ARMNEVISLW
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TSVQNLQKKH
ALLEADVAAH QDPIDGITIQ ARQFQDAGHF DADNIKKKQE ALVARYEALK DPMVARKQKL
ADSLRLQQLF RDIEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
KAVTQKGNAM VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN
EAQSWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTLITKEVG SVSLRMKQVE ELYHSLLELG
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL
KANESRLKDI NKVANDLESE GLMAEEVQAV EHQEVYGMMP RDETDSKTVS PWKSARMMVH
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SADEVQRFHR DADETKEWIE EKNQALNTDN
YGHDLASVQA LQRNDEGFER DLAALGDKVN SLGETAQRLI QSHPELAEDL QEKCTELNQA
WSSLGKRADQ RKEKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
HQEHRTEIDA RAGTFQAFEQ FGQQLLARGH YASPEIKEKL DILDQERTDL EKAWVQRRMM
LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV
DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIEMGNP
LIERGACAGS EDAVKARLAA LADQWEFLVQ KSSEKSQKLK EANKQQNFNT GIKDFDFWLS
EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV
KDKRETINGR FQRIKSMAAA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD
LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL AQFVDHWKEL
KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF
ETDFTVHKDR VNDVCANGED LIKKNNHHVE NITAKMKGLK GKVSDLEKAA AQRKAKLDEN
SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN
ITALKDQLLA AKHIQSKAIE VRHASLMKRW NQLLANSAAR KKKLLEAQEH FRKVEDLFLT
FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR
QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN
AFHQWIQETR TYLLDGSCMV EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA
LILDNKYTEH STVGLAQQWD QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF
DKDKSGRLNH QEFKSCLRSL GYDLPMVEEG EPDPEFESIL DTVDPNRDGH VSLQEYMAFM
ISRETENVKS SEEIESAFRA LSSERKPYVT KEELYQNLTR EQADYCISHM KPYMDGKGRE
LPSAYDYIEF TRSLFVN
