ID   AT12A_RAT               Reviewed;        1036 AA.
AC   P54708;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 184.
DE   RecName: Full=Potassium-transporting ATPase alpha chain 2;
DE   AltName: Full=HK alpha 2 {ECO:0000250|UniProtKB:Q9TV52};
DE   AltName: Full=Non-gastric H(+)/K(+) ATPase subunit alpha;
DE            EC=7.2.2.19 {ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
DE   AltName: Full=Non-gastric Na(+)/K(+) ATPase subunit alpha;
DE            EC=7.2.2.13 {ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
DE   AltName: Full=Proton pump;
DE   AltName: Full=Sodium pump {ECO:0000250|UniProtKB:P54707};
GN   Name=Atp12a; Synonyms=Atp1al1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RC   STRAIN=Sprague-Dawley; TISSUE=Colon;
RX   PubMed=1320029; DOI=10.1016/s0021-9258(18)42276-4;
RA   Crowson M.S., Shull G.E.;
RT   "Isolation and characterization of a cDNA encoding the putative distal
RT   colon H+,K(+)-ATPase. Similarity of deduced amino acid sequence to gastric
RT   H+,K(+)-ATPase and Na+,K(+)-ATPase and mRNA expression in distal colon,
RT   kidney, and uterus.";
RL   J. Biol. Chem. 267:13740-13748(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=9446555; DOI=10.1074/jbc.273.5.2543;
RA   Kone B.C., Higham S.C.;
RT   "A novel N-terminal splice variant of the rat H+-K+-ATPase alpha2 subunit.
RT   Cloning, functional expression, and renal adaptive response to chronic
RT   hypokalemia.";
RL   J. Biol. Chem. 273:2543-2552(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 779-785, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=7560093; DOI=10.1172/jci118247;
RA   Lee J., Rajendran V.M., Mann A.S., Kashgarian M., Binder H.J.;
RT   "Functional expression and segmental localization of rat colonic K-
RT   adenosine triphosphatase.";
RL   J. Clin. Invest. 96:2002-2008(1995).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9872395; DOI=10.1016/s0014-5793(98)01483-5;
RA   Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B.,
RA   Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N.;
RT   "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian
RT   genes encoding the catalytic alpha subunit.";
RL   FEBS Lett. 440:320-324(1998).
RN   [6]
RP   INTERACTION WITH ATP1B3, AND SUBCELLULAR LOCATION.
RX   PubMed=9950762; DOI=10.1152/ajpcell.1999.276.2.c350;
RA   Sangan P., Kolla S.S., Rajendran V.M., Kashgarian M., Binder H.J.;
RT   "Colonic H-K-ATPase beta-subunit: identification in apical membranes and
RT   regulation by dietary K depletion.";
RL   Am. J. Physiol. 276:C350-C360(1999).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=10644526; DOI=10.1152/ajpcell.2000.278.1.c182;
RA   Sangan P., Thevananther S., Sangan S., Rajendran V.M., Binder H.J.;
RT   "Colonic H-K-ATPase alpha- and beta-subunits express ouabain-insensitive H-
RT   K-ATPase.";
RL   Am. J. Physiol. 278:C182-C189(2000).
RN   [8]
RP   INTERACTION WITH ATP1B1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14749213; DOI=10.1152/ajpcell.00393.2003;
RA   Pestov N.B., Korneenko T.V., Radkov R., Zhao H., Shakhparonov M.I.,
RA   Modyanov N.N.;
RT   "Identification of the beta-subunit for nongastric H-K-ATPase in rat
RT   anterior prostate.";
RL   Am. J. Physiol. 286:C1229-C1237(2004).
CC   -!- FUNCTION: The catalytic subunit of a H(+)/K(+) ATPase and/or Na(+)/K(+)
CC       ATPase pump which transports K(+) ions in exchange for Na(+) and/or
CC       H(+) ions across the apical membrane of epithelial cells. Uses ATP as
CC       an energy source to pump K(+) ions into the cell while transporting
CC       Na(+) and/or H(+) ions to the extracellular compartment
CC       (PubMed:10644526, PubMed:7560093). Involved in the maintenance of
CC       electrolyte homeostasis through K(+) ion absorption in kidney and colon
CC       (By similarity). In the airway epithelium, may play a primary role in
CC       mucus acidification regulating its viscosity and clearance (By
CC       similarity). {ECO:0000250|UniProtKB:P54707,
CC       ECO:0000250|UniProtKB:Q9Z1W8, ECO:0000269|PubMed:10644526,
CC       ECO:0000269|PubMed:7560093}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=K(+)(out) + ATP + H2O + H(+)(in) = K(+)(in) + ADP + phosphate
CC         + 2 H(+)(out); Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
CC         Evidence={ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
CC         Evidence={ECO:0000305|PubMed:10644526, ECO:0000305|PubMed:7560093};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 K(+)(out) + 3 Na(+)(in) + ATP + H2O = 2 K(+)(in) + 3
CC         Na(+)(out) + ADP + phosphate + H(+); Xref=Rhea:RHEA:18353,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.13;
CC         Evidence={ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354;
CC         Evidence={ECO:0000305|PubMed:10644526, ECO:0000305|PubMed:7560093};
CC   -!- ACTIVITY REGULATION: Up-regulated by K(+) ions in a dose-dependent way.
CC       {ECO:0000269|PubMed:10644526, ECO:0000269|PubMed:7560093}.
CC   -!- SUBUNIT: The ATPase pump is composed of a catalytic alpha subunit and
CC       an auxiliary non-catalytic beta subunit. The alpha subunit pairs with
CC       the beta subunit of gastric H(+)/K(+) ATPase ATP4B or the beta subunit
CC       of Na(+)/K(+) ATPases ATP1B1 and ATP1B3; this interaction is required
CC       for the formation of a functionally active pump and its targeting at
CC       the plasma membrane. {ECO:0000250|UniProtKB:P54707,
CC       ECO:0000269|PubMed:14749213, ECO:0000269|PubMed:9950762}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:14749213, ECO:0000269|PubMed:7560093,
CC       ECO:0000269|PubMed:9950762}; Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long; Synonyms=2a;
CC         IsoId=P54708-1; Sequence=Displayed;
CC       Name=Short; Synonyms=2b;
CC         IsoId=P54708-2; Sequence=VSP_000414;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in distal colon,
CC       coagulating and preputial glands; at much lower levels in proximal
CC       colon, kidney, uterus, brain, placenta and lung; and at trace levels in
CC       heart and forestomach (PubMed:9872395). Expressed in distal colon
CC       epithelium (at protein level) (PubMed:7560093). Expressed in anterior
CC       prostate (at protein level) (PubMed:14749213).
CC       {ECO:0000269|PubMed:14749213, ECO:0000269|PubMed:7560093,
CC       ECO:0000269|PubMed:9872395}.
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; M90398; AAA40779.1; -; mRNA.
DR   EMBL; U94911; AAB93900.1; -; Genomic_DNA.
DR   EMBL; U94912; AAB93901.1; -; mRNA.
DR   EMBL; U94913; AAB93902.1; -; mRNA.
DR   PIR; A42895; A42895.
DR   PDB; 7X20; X-ray; 3.30 A; A=53-1036.
DR   PDB; 7X21; EM; 2.80 A; A=53-1036.
DR   PDB; 7X22; EM; 3.00 A; A=53-1036.
DR   PDB; 7X23; EM; 3.20 A; A=53-1036.
DR   PDB; 7X24; EM; 3.40 A; A=53-1036.
DR   PDB; 8IJL; EM; 2.62 A; A=53-1036.
DR   PDB; 8IJM; EM; 3.13 A; A=53-1036.
DR   AlphaFoldDB; P54708; -.
DR   EMDB; EMD-32954; -.
DR   EMDB; EMD-32955; -.
DR   EMDB; EMD-32956; -.
DR   EMDB; EMD-32957; -.
DR   SMR; P54708; -.
DR   FunCoup; P54708; 66.
DR   STRING; 10116.ENSRNOP00000028093; -.
DR   TCDB; 3.A.3.1.4; the p-type atpase (p-atpase) superfamily.
DR   GlyGen; P54708; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P54708; -.
DR   PhosphoSitePlus; P54708; -.
DR   jPOST; P54708; -.
DR   PaxDb; 10116-ENSRNOP00000028093; -.
DR   UCSC; RGD:620569; rat. [P54708-1]
DR   AGR; RGD:620569; -.
DR   RGD; 620569; Atp12a.
DR   eggNOG; KOG0203; Eukaryota.
DR   InParanoid; P54708; -.
DR   PhylomeDB; P54708; -.
DR   Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR   PRO; PR:P54708; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008900; F:P-type potassium:proton transporter activity; EXP:UniProtKB.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; EXP:UniProtKB.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0055075; P:potassium ion homeostasis; ISO:RGD.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006885; P:regulation of pH; ISO:RGD.
DR   GO; GO:0010038; P:response to metal ion; IDA:RGD.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR   CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR   FunFam; 1.20.1110.10:FF:000079; Sodium/potassium-transporting ATPase subunit alpha; 1.
DR   FunFam; 2.70.150.10:FF:000003; Sodium/potassium-transporting ATPase subunit alpha; 1.
DR   FunFam; 3.40.1110.10:FF:000001; Sodium/potassium-transporting ATPase subunit alpha; 1.
DR   FunFam; 3.40.50.1000:FF:000004; Sodium/potassium-transporting ATPase subunit alpha; 1.
DR   FunFam; 1.20.1110.10:FF:000095; Sodium/potassium-transporting ATPase subunit alpha-1; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR059000; ATPase_P-type_domA.
DR   InterPro; IPR050510; Cation_transp_ATPase_P-type.
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   NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294:SF1; POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 2; 1.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PDBsum; 7X20; -.
DR   PDBsum; 7X21; -.
DR   PDBsum; 7X22; -.
DR   PDBsum; 7X23; -.
DR   PDBsum; 7X24; -.
DR   PDBsum; 8IJL; -.
DR   PDBsum; 8IJM; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Potassium; Potassium transport; Reference proteome; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1036
FT                   /note="Potassium-transporting ATPase alpha chain 2"
FT                   /id="PRO_0000046263"
FT   TOPO_DOM        1..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..143
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        321..332
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..784
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        785..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        805..814
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        815..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        836..855
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        856..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        879..930
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        931..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        951..964
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        965..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        984..998
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        999..1019
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1020..1036
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        388
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         729
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         733
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         955
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..108
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:9446555"
FT                   /id="VSP_000414"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           61..67
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           78..88
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           101..106
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:7X24"
FT   HELIX           114..133
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           141..162
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          173..177
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          213..226
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:7X21"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          260..272
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           278..288
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           292..294
FT                   /evidence="ECO:0007829|PDB:8IJM"
FT   HELIX           295..323
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           329..343
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           348..364
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          367..372
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           375..378
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            379..381
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          384..387
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           389..393
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          399..405
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          408..411
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          427..429
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           430..439
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           454..456
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          459..461
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           463..476
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           480..485
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          488..492
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            496..498
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          500..506
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            510..512
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          515..521
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           523..528
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          530..535
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          538..541
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           544..558
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            559..561
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          563..572
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            574..576
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            585..588
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          593..604
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           611..620
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          624..628
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           633..643
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           653..660
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            664..666
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            669..671
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          674..678
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           679..683
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           687..696
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          698..704
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           707..718
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            719..721
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          724..728
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           731..733
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           734..739
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          740..749
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           752..756
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          759..762
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           768..808
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           816..821
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           822..826
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           828..833
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           834..836
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           837..839
FT                   /evidence="ECO:0007829|PDB:7X21"
FT   HELIX           843..845
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           848..850
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            851..853
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           859..863
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           864..870
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           871..886
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            887..889
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           892..895
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           899..902
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           920..948
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          952..954
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           956..959
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   STRAND          961..963
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           965..983
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            984..989
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           995..997
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           998..1001
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   TURN            1002..1004
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           1005..1024
FT                   /evidence="ECO:0007829|PDB:8IJL"
FT   HELIX           1029..1034
FT                   /evidence="ECO:0007829|PDB:8IJL"
SQ   SEQUENCE   1036 AA;  114975 MW;  453918E65CD4813B CRC64;
     MRRKTEIYSV ELNGTKDVKP ADQRDDKKFK GAKNKDLEPN KSHEKEELKK ELDLDDHRLS
     NTELEQKYGT NIIQGLSSVR ATELLARDGP NTLTPPKQTP EIIKFLKQMV GGFSILLWIG
     AALCWIAFVI QYVNNSASLD NVYLGAILVL VVILTGIFAY YQEAKSTNIM ASFSKMIPQQ
     ALVIRDAEKK VISAEQLVVG DVVEIKGGDQ IPADIRLVFS QGCKVDNSSL TGESEPQARS
     TEFTHENPLE TKNIGFYSTT CLEGTATGIV INTGDRTIIG RIASLASGVG SEKTPIAIEI
     EHFVHIVAGV AVSIDIIFFI TAVCMKYYVL DAIIFLISII VANVPEGLLA TVTVTLSLTA
     KRMAKKNCLV KNLEAVETLG STSIICSDKT GTLTQNRMTV AHLWFDNQIF VADTSENQTK
     QAFDQSSGTW ASLSKIITLC NRAEFRPGQE SVPIMKRTVV GDASETALLK FSEVILGDVM
     GIRKRNHKVA EIPFNSTNKF QLSIHETEDP NNKRFLVVMK GAPERILEKC STIMINGQEQ
     PLDKSSADSF HTAYMELGGL GERVLGFCHL YLPAEQFPQS YIFDVDSVNF PTSNFCFVGL
     LSMIDPPRST VPDAVSKCRS AGIKVIMVTG DHPITAKAIA KSVGIISANN ETVEDIAKRR
     NIAVEQVNKR EAKAAVVTGM ELKDMTPEQL DELLTNYQEI VFARTSPQQK LIIVEGCQRQ
     DAIVAVTGDG VNDSPALKKA DIGIAMGIAG SDAAKNAADM VLLDDNFASI VTGVEEGRLI
     FDNLKKTIAY TLTKNIAELC PFLIYIVAGL PLPIGTITIL FIDLGTDIIP SIALAYEKAE
     SDIMNRKPRH KKKDRLVNTQ LAIYSYLHIG LMQALGGFLV YFTVYAQQGF WPTSLINLRV
     AWETDDINDL EDSYGQEWTR YQRKYLEWTG STAFFVAIMI QQIADLIIRK TRRNSIFQQG
     LFRNKVIWVG IASQVIVALI LSYGLGSVPA LSFTMLRVQY WFVAVPHAIL IWVYDEMRKL
     FIRLYPGSWW DKNMYY
//