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   27-MAR-2024, entry version 182.
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}.
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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   PDB; 8CF4; NMR; -; A=965-1025.
DR   PDB; 8CHG; NMR; -; A=965-1025.
DR   PDB; 8CHH; NMR; -; A=965-1025.
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   PDBsum; 8CF4; -.
DR   PDBsum; 8CHG; -.
DR   PDBsum; 8CHH; -.
DR   AlphaFoldDB; P07751; -.
DR   BMRB; P07751; -.
DR   SASBDB; P07751; -.
DR   SMR; P07751; -.
DR   MINT; P07751; -.
DR   STRING; 9031.ENSGALP00000066200; -.
DR   PaxDb; 9031-ENSGALP00000038979; -.
DR   GeneID; 374234; -.
DR   KEGG; gga:374234; -.
DR   CTD; 6709; -.
DR   VEuPathDB; HostDB:geneid_374234; -.
DR   eggNOG; KOG0040; Eukaryota.
DR   InParanoid; P07751; -.
DR   PhylomeDB; P07751; -.
DR   EvolutionaryTrace; P07751; -.
DR   PRO; PR:P07751; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.58.60; -; 20.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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   PANTHER; PTHR11915:SF422; PH_9 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
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   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 16.
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
//