AT2A1_BOVIN
ID AT2A1_BOVIN Reviewed; 993 AA.
AC Q0VCY0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1;
DE Short=SERCA1;
DE Short=SR Ca(2+)-ATPase 1;
DE EC=7.2.2.10 {ECO:0000269|PubMed:22387132};
DE AltName: Full=Calcium pump 1;
DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform;
DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
GN Name=ATP2A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:3TLM}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 1-992 IN COMPLEX WITH ATP ANALOG;
RP MAGNESIUM AND CALCIUM, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=22387132; DOI=10.1016/j.jsb.2012.02.008;
RA Sacchetto R., Bertipaglia I., Giannetti S., Cendron L., Mascarello F.,
RA Damiani E., Carafoli E., Zanotti G.;
RT "Crystal structure of sarcoplasmic reticulum Ca2+-ATPase (SERCA) from
RT bovine muscle.";
RL J. Struct. Biol. 178:38-44(2012).
CC -!- FUNCTION: Key regulator of striated muscle performance by acting as the
CC major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+)
CC into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP
CC coupled with the translocation of calcium from the cytosol to the
CC sarcoplasmic reticulum lumen (PubMed:22387132). Contributes to calcium
CC sequestration involved in muscular excitation/contraction.
CC {ECO:0000250|UniProtKB:Q8R429, ECO:0000269|PubMed:22387132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000269|PubMed:22387132};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:22387132};
CC -!- ACTIVITY REGULATION: Inhibited by sarcolipin (SLN), phospholamban (PLN)
CC and myoregulin (MRLN) (By similarity). Reversibly inhibited by
CC phospholamban (PLN) at low calcium concentrations (By similarity).
CC Dephosphorylated PLN decreases the apparent affinity of the ATPase for
CC calcium. This inhibition is regulated by the phosphorylation of PLN (By
CC similarity). Enhanced by DWORF; DWORF increases activity by displacing
CC sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By
CC similarity). {ECO:0000250|UniProtKB:P04191,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity). Interacts
CC with phospholamban (PLN) (By similarity). Interacts with myoregulin
CC (MRLN). Interacts with DWORF (By similarity). Interacts VMP1 (By
CC similarity). {ECO:0000250|UniProtKB:O14983,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22387132}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22387132}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22387132}.
CC -!- TISSUE SPECIFICITY: Detected in fast-twitch skeletal muscle (at protein
CC level). {ECO:0000269|PubMed:22387132}.
CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the
CC cytoplasmic and transmembrane domains. According to the E1-E2 model,
CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity
CC E1 conformation is followed by the ATP-dependent phosphorylation of the
CC active site Asp, giving rise to E1P. A conformational change of the
CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the
CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release.
CC Dephosphorylation of the active site Asp mediates the subsequent return
CC to the E1 conformation. {ECO:0000250|UniProtKB:P04191}.
CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy
CC a similar binding site on ATP2A1 that is situated between the ATP2A1
CC transmembrane helices. {ECO:0000250|UniProtKB:P04191}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; BC119938; AAI19939.1; -; mRNA.
DR RefSeq; NP_001069235.1; NM_001075767.1.
DR PDB; 3TLM; X-ray; 2.95 A; A=1-992.
DR PDBsum; 3TLM; -.
DR AlphaFoldDB; Q0VCY0; -.
DR SMR; Q0VCY0; -.
DR STRING; 9913.ENSBTAP00000008593; -.
DR PaxDb; Q0VCY0; -.
DR PeptideAtlas; Q0VCY0; -.
DR PRIDE; Q0VCY0; -.
DR Ensembl; ENSBTAT00000008593; ENSBTAP00000008593; ENSBTAG00000006541.
DR GeneID; 518117; -.
DR KEGG; bta:518117; -.
DR CTD; 487; -.
DR VEuPathDB; HostDB:ENSBTAG00000006541; -.
DR VGNC; VGNC:26290; ATP2A1.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000159895; -.
DR InParanoid; Q0VCY0; -.
DR OMA; GRVEVIC; -.
DR OrthoDB; 100699at2759; -.
DR BRENDA; 7.2.2.10; 908.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000006541; Expressed in biceps femoris and 100 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISS:UniProtKB.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051659; P:maintenance of mitochondrion location; IEA:Ensembl.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:1902082; P:positive regulation of calcium ion import into sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0106134; P:positive regulation of cardiac muscle cell contraction; ISS:UniProtKB.
DR GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
DR GO; GO:0090076; P:relaxation of skeletal muscle; IEA:Ensembl.
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; IPR005782; P-type_ATPase_IIA.
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 PRINTS; PR00120; HATPASE.
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; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Calcium transport; Disulfide bond;
KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..993
FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 1"
FT /id="PRO_0000266030"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 314..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 757..776
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 777..786
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 787..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 808..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 828..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 851..896
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 897..916
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 917..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 930..948
FT /note="Helical; Name=9"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 949..963
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TRANSMEM 964..984
FT /note="Helical; Name=10"
FT /evidence="ECO:0000269|PubMed:22387132"
FT TOPO_DOM 985..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22387132"
FT REGION 787..807
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT REGION 931..942
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 624..626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 624..625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 767
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT BINDING 907
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22387132,
FT ECO:0007744|PDB:3TLM"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT DISULFID 875..887
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 60..78
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 89..120
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 248..273
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 288..306
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 470..476
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 493..500
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 517..522
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 559..568
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 589..599
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 628..638
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 654..659
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 673..677
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 682..691
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 692..694
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 697..703
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 724..729
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 740..774
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 775..779
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 788..798
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 801..804
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 805..808
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 830..844
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 849..855
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 858..861
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 865..869
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 889..891
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 894..911
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 912..914
FT /evidence="ECO:0007829|PDB:3TLM"
FT STRAND 915..918
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 921..923
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 926..928
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 930..948
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 950..952
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 953..955
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 962..964
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 965..973
FT /evidence="ECO:0007829|PDB:3TLM"
FT HELIX 975..987
FT /evidence="ECO:0007829|PDB:3TLM"
FT TURN 988..991
FT /evidence="ECO:0007829|PDB:3TLM"
SQ SEQUENCE 993 AA; 109290 MW; E6E3F70C527683C1 CRC64;
MEAAHSKTTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVLEQFEDL
LVRILLLAAC ISFVLAWFEE GEETVTAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILTIKS TTLRVDQSIL
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAI GIVATTGVGT EIGKIRDQMA
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCKMFIID RIDGDLCLLN EFSVTGSTYA PEGEVLKNDK PVRSGQYDGL VELATICALC
NDSSLDFNET KGIYEKVGEA TETALTTLVE KMNVFNTEVR NLSKVERANA CNSVIRQLMK
KEFTLEFSRD RKSMSVYCSP AKSRAAVGNK MFVKGAPEGV IDRCNYVRVG TTRVPMTGPV
KEKILSVIKE WGTGRDTLRC LALATRDTPP KREEMVLDDS TKFMEYETDL TFVGVVGMLD
PPRKEVMGSI QLCRDAGIRV IMITGDNKGT AIAICRRIGI FGENEDVADR AYTGREFDDL
PLAEQREACR RACCFARVEP THKSKIVEYL QSFDEITAMT GDGVNDAPAL KKAEIGIAMG
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GLPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMDRPP RTPKEPLISG WLFFRYMAIG
GYVGAATVGA AAWWFLYAED GPHVTYSQLT HFMKCSEHSP DFEGVDCEVF EAPQPMTMAL
SVLVTIEMCN ALNSLSENQS LVRMPPWVNI WLVGSIGLSM SLHFLILYVD PLPMIFKLQA
LDLYHWLMVL KISLPVIGLD EILKFVARNY LEG
