AT1A1_PIG
ID AT1A1_PIG Reviewed; 1021 AA.
AC P05024; P18874;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE EC=7.2.2.13 {ECO:0000269|PubMed:18075585};
DE AltName: Full=Sodium pump subunit alpha-1;
DE Flags: Precursor;
GN Name=ATP1A1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2423371; DOI=10.1016/0014-5793(86)80616-0;
RA Ovchinnikov Y.A., Modyanov N.N., Broude N.E., Petrukhin K.E., Grishin A.V.,
RA Arzamazova N.M., Aldanova N.A., Monastyrskaya G.S., Sverdlov E.D.;
RT "Pig kidney Na+,K+-ATPase. Primary structure and spatial organization.";
RL FEBS Lett. 201:237-245(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ovchinnikov Y.A., Arsenyan S.G., Broude N.E., Petrukhin K.E., Grishin A.V.,
RA Aldanova N.A., Arzamazova N.M., Aristarkhova E.A., Melkov A.M.,
RA Smirnov Y.V., Gur'Ev S.O., Monastyrskaya G.S., Modyanov N.N.;
RT "Nucleotide sequence of cDNA and primary structure of the alpha-subunit of
RT porcine kidney Na(+)-K(+)-ATPase.";
RL Dokl. Biochem. 285:403-407(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3032208;
RA Monastyrskaya G.S., Broude N.E., Melkov A.M., Smirnov Y.V., Malyshev I.V.,
RA Arsenyan S.G., Salomatina I.S., Sverdlov V.E., Grishin A.V.,
RA Petrukhin K.E., Modyanov N.N.;
RT "Primary structure of the alpha-subunit of Na+,K+-ATPase from the swine
RT kidney. III. Complete nucleotide sequence corresponding to the structural
RT region of the gene.";
RL Bioorg. Khim. 13:20-26(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2844194;
RA Kostetsky P.V., Dobrova I.E.;
RT "Reconstruction of long polynucleotide sequences from fragments using the
RT Iskra-226 personal computer.";
RL Bioorg. Khim. 14:515-521(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 469-617.
RA Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E.,
RA Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V.,
RA Modyanov N.N.;
RT "Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic
RT region of the alpha-subunit of Na+,K+ -ATPase.";
RL Dokl. Biochem. 283:270-272(1985).
RN [6]
RP INTERACTION WITH FXYD1.
RX PubMed=15563542; DOI=10.1152/ajpheart.00142.2004;
RA Jia L.G., Donnet C., Bogaev R.C., Blatt R.J., McKinney C.E., Day K.H.,
RA Berr S.S., Jones L.R., Moorman J.R., Sweadner K.J., Tucker A.L.;
RT "Hypertrophy, increased ejection fraction, and reduced Na-K-ATPase activity
RT in phospholemman-deficient mice.";
RL Am. J. Physiol. 288:H1982-H1988(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 24-1021, AND CATALYTIC ACTIVITY.
RX PubMed=18075585; DOI=10.1038/nature06419;
RA Morth J.P., Pedersen B.P., Toustrup-Jensen M.S., Sorensen T.L.,
RA Petersen J., Andersen J.P., Vilsen B., Nissen P.;
RT "Crystal structure of the sodium-potassium pump.";
RL Nature 450:1043-1049(2007).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000250|UniProtKB:P05023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13; Evidence={ECO:0000269|PubMed:18075585};
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. Interacts with regulatory subunit FXYD1
CC (PubMed:15563542). Interacts with regulatory subunit FXYD3 (By
CC similarity). Interacts with SIK1 (By similarity). Interacts with
CC SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this
CC interaction regulates the sodium/potassium-transporting ATPase complex
CC localization at the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P05023, ECO:0000250|UniProtKB:P06685,
CC ECO:0000269|PubMed:15563542}.
CC -!- INTERACTION:
CC P05024; P05027: ATP1B1; NbExp=3; IntAct=EBI-9014019, EBI-9014008;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P06685}.
CC Melanosome {ECO:0000250|UniProtKB:P05023}.
CC -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
CC Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to
CC PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following
CC increases in intracellular sodium, leading to increase catalytic
CC activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; X03938; CAA27576.1; -; mRNA.
DR EMBL; M38445; AAA31002.1; -; mRNA.
DR EMBL; M32512; AAA31004.1; -; mRNA.
DR PIR; B24862; B24862.
DR RefSeq; NP_999414.1; NM_214249.1.
DR PDB; 3B8E; X-ray; 3.50 A; A/C=24-1021.
DR PDB; 3KDP; X-ray; 3.50 A; A/C=24-1021.
DR PDB; 3N23; X-ray; 4.60 A; A/C=30-1021.
DR PDB; 3WGU; X-ray; 2.80 A; A/C=6-1021.
DR PDB; 3WGV; X-ray; 2.80 A; A/C=6-1021.
DR PDB; 4HQJ; X-ray; 4.30 A; A/C=1-1021.
DR PDB; 4HYT; X-ray; 3.40 A; A/C=1-1021.
DR PDB; 4RES; X-ray; 3.41 A; A/C=1-1021.
DR PDB; 4RET; X-ray; 4.00 A; A/C=1-1021.
DR PDB; 7D91; X-ray; 3.35 A; A=6-1021.
DR PDB; 7D92; X-ray; 3.90 A; A=6-1021.
DR PDB; 7D93; X-ray; 3.65 A; A/C=6-1021.
DR PDB; 7D94; X-ray; 3.50 A; A/C=6-1021.
DR PDB; 7DDF; X-ray; 4.62 A; A/C=6-1021.
DR PDB; 7DDH; X-ray; 3.46 A; A/C=6-1021.
DR PDB; 7DDI; X-ray; 3.72 A; A/C=6-1021.
DR PDB; 7DDK; X-ray; 3.50 A; A/C=6-1021.
DR PDB; 7DDL; X-ray; 3.20 A; A/C=6-1021.
DR PDB; 7WYS; X-ray; 3.71 A; A/C=6-1021.
DR PDB; 7WYT; X-ray; 2.90 A; A/C=6-1021.
DR PDBsum; 3B8E; -.
DR PDBsum; 3KDP; -.
DR PDBsum; 3N23; -.
DR PDBsum; 3WGU; -.
DR PDBsum; 3WGV; -.
DR PDBsum; 4HQJ; -.
DR PDBsum; 4HYT; -.
DR PDBsum; 4RES; -.
DR PDBsum; 4RET; -.
DR PDBsum; 7D91; -.
DR PDBsum; 7D92; -.
DR PDBsum; 7D93; -.
DR PDBsum; 7D94; -.
DR PDBsum; 7DDF; -.
DR PDBsum; 7DDH; -.
DR PDBsum; 7DDI; -.
DR PDBsum; 7DDK; -.
DR PDBsum; 7DDL; -.
DR PDBsum; 7WYS; -.
DR PDBsum; 7WYT; -.
DR AlphaFoldDB; P05024; -.
DR BMRB; P05024; -.
DR SMR; P05024; -.
DR ComplexPortal; CPX-57; Sodium:potassium-exchanging ATPase complex.
DR CORUM; P05024; -.
DR DIP; DIP-60365N; -.
DR IntAct; P05024; 2.
DR STRING; 9823.ENSSSCP00000007190; -.
DR BindingDB; P05024; -.
DR ChEMBL; CHEMBL4131; -.
DR CarbonylDB; P05024; -.
DR PaxDb; P05024; -.
DR PeptideAtlas; P05024; -.
DR PRIDE; P05024; -.
DR GeneID; 397481; -.
DR KEGG; ssc:397481; -.
DR CTD; 476; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P05024; -.
DR OrthoDB; 100699at2759; -.
DR BRENDA; 7.2.2.13; 6170.
DR EvolutionaryTrace; P05024; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IMP:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:BHF-UCL.
DR GO; GO:0030955; F:potassium ion binding; IDA:BHF-UCL.
DR GO; GO:0031402; F:sodium ion binding; IMP:AgBase.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IC:BHF-UCL.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0055085; P:transmembrane transport; IDA:BHF-UCL.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Cell projection;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome; Sodium;
KW Sodium transport; Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..5
FT /id="PRO_0000002487"
FT CHAIN 6..1021
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002488"
FT TOPO_DOM 6..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..800
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..916
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 937..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..983
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1005..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..82
FT /note="Phosphoinositide-3 kinase binding"
FT /evidence="ECO:0000250"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 258
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 540
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05023"
FT MOD_RES 659
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 941
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT CONFLICT 7
FT /note="R -> P (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="S -> F (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="S -> T (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="S -> L (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="R -> Q (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="P -> A (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="T -> S (in Ref. 3; no nucleotide entry and 4; no
FT nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3B8E"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4RES"
FT HELIX 98..119
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 126..155
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3KDP"
FT STRAND 199..212
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 281..310
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:7D91"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:7D94"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:4HYT"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:7WYT"
FT HELIX 449..461
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 530..545
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 548..558
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7D91"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 578..590
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 619..628
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:7WYT"
FT HELIX 639..646
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 673..681
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 684..689
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 693..705
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 710..714
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:7WYT"
FT HELIX 720..725
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 726..732
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 738..743
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 755..779
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 781..793
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 802..812
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 815..819
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 820..822
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:3B8E"
FT HELIX 845..851
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 852..854
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 855..873
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 878..881
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 882..884
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 885..888
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 895..897
FT /evidence="ECO:0007829|PDB:3B8E"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:7WYT"
FT HELIX 906..934
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 942..945
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 950..968
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 972..975
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 983..988
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 990..1009
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 1010..1012
FT /evidence="ECO:0007829|PDB:3B8E"
FT HELIX 1016..1019
FT /evidence="ECO:0007829|PDB:3WGU"
SQ SEQUENCE 1021 AA; 112681 MW; F369C6273CEB561D CRC64;
MGKGVGRDKY EPAAVSEHGD KKKAKKERDM DELKKEVSMD DHKLSLDELH RKYGTDLSRG
LTPARAAEIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSM LLWIGAILCF LAYGIQAATE
EEPQNDNLYL GVVLSAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVI RNGEKMSINA
EEVVVGDLVE VKGGDRIPAD LRIISANGCK VDNSSLTGES EPQTRSPDFT NENPLETRNI
AFFSTNCVEG TARGIVVYTG DRTVMGRIAT LASGLEGGQT PIAAEIEHFI HIITGVAVFL
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVETLGSTST ICSDKTGTLT QNRMTVAHMW SDNQIHEADT TENQSGVSFD KTSATWLALS
RIAGLCNRAV FQANQENLPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRE RYTKIVEIPF
NSTNKYQLSI HKNPNTAEPR HLLVMKGAPE RILDRCSSIL IHGKEQPLDE ELKDAFQNAY
LELGGLGERV LGFCHLFLPD EQFPEGFQFD TDDVNFPLDN LCFVGLISMI DPPRAAVPDA
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISEGNETVE DIAARLNIPV SQVNPRDAKA
CVVHGSDLKD MTSEQLDDIL KYHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
PASKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
NIPEITPFLI FIIANIPLPL GTVTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD
KLVNEQLISM AYGQIGMIQA LGGFFTYFVI LAENGFLPIH LLGLRVNWDD RWINDVEDSY
GQQWTYEQRK IVEFTCHTPF FVTIVVVQWA DLVICKTRRN SVFQQGMKNK ILIFGLFEET
ALAAFLSYCP GMGVALRMYP LKPTWWFCAF PYSLLIFVYD EVRKLIIRRR PGGWVEKETY
Y
