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Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)

 HSP7C_BOVIN             Reviewed;         650 AA.
P19120; A5D968; Q3MHM4;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
27-SEP-2017, entry version 166.
RecName: Full=Heat shock cognate 71 kDa protein;
AltName: Full=Heat shock 70 kDa protein 8;
Name=HSPA8; Synonyms=HSC70;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain cortex;
PubMed=2216746; DOI=10.1093/nar/18.18.5569;
Deluca-Flaherty C., McKay D.B.;
"Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock
cognate protein.";
Nucleic Acids Res. 18:5569-5569(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
PubMed=2143562; DOI=10.1038/346623a0;
Flaherty K.M., de Luca-Flaherty C., McKay D.B.;
"Three-dimensional structure of the ATPase fragment of a 70K heat-
shock cognate protein.";
Nature 346:623-628(1990).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385 IN COMPLEXES WITH ADP
AND ATP.
PubMed=8175707;
Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B.;
"Structural basis of the 70-kilodalton heat shock cognate protein ATP
hydrolytic activity. II. Structure of the active site with ADP or ATP
bound to wild type and mutant ATPase fragment.";
J. Biol. Chem. 269:12899-12907(1994).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
PubMed=9585559; DOI=10.1021/bi973046m;
Wilbanks S.M., McKay D.B.;
"Structural replacement of active site monovalent cations by the
epsilon-amino group of lysine in the ATPase fragment of bovine
Hsc70.";
Biochemistry 37:7456-7462(1998).
[7]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381 IN COMPLEX WITH ADP.
PubMed=9799500; DOI=10.1021/bi981510x;
Sousa M.C., McKay D.B.;
"The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate
protein is essential for transducing the ATP-induced conformational
change.";
Biochemistry 37:15392-15399(1998).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
PubMed=10451379; DOI=10.1021/bi990816g;
Johnson E.R., McKay D.B.;
"Mapping the role of active site residues for transducing an ATP-
induced conformational change in the bovine 70-kDa heat shock cognate
protein.";
Biochemistry 38:10823-10830(1999).
[9]
X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 2-554 IN COMPLEX WITH ADP.
PubMed=18550409; DOI=10.1016/j.molcel.2008.05.006;
Schuermann J.P., Jiang J., Cuellar J., Llorca O., Wang L.,
Gimenez L.E., Jin S., Taylor A.B., Demeler B., Morano K.A., Hart P.J.,
Valpuesta J.M., Lafer E.M., Sousa R.;
"Structure of the Hsp110:Hsc70 nucleotide exchange machine.";
Mol. Cell 31:232-243(2008).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation. This is achieved
through cycles of ATP binding, ATP hydrolysis and ADP release,
mediated by co-chaperones. The co-chaperones have been shown to
not only regulate different steps of the ATPase cycle of HSP70,
but they also have an individual specificity such that one co-
chaperone may promote folding of a substrate while another may
promote degradation. The affinity of HSP70 for polypeptides is
regulated by its nucleotide bound state. In the ATP-bound form, it
has a low affinity for substrate proteins. However, upon
hydrolysis of the ATP to ADP, it undergoes a conformational change
that increases its affinity for substrate proteins. HSP70 goes
through repeated cycles of ATP hydrolysis and nucleotide exchange,
which permits cycles of substrate binding and release. The HSP70-
associated co-chaperones are of three types: J-domain co-
chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the
nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate
conversion of HSP70 from the ADP-bound to the ATP-bound state
thereby promoting substrate release), and the TPR domain
chaperones such as HOPX and STUB1. Acts as a repressor of
transcriptional activation. Inhibits the transcriptional
coactivator activity of CITED1 on Smad-mediated transcription.
Component of the PRP19-CDC5L complex that forms an integral part
of the spliceosome and is required for activating pre-mRNA
splicing. May have a scaffolding role in the spliceosome assembly
as it contacts all other components of the core complex. Binds
bacterial lipopolysaccharide (LPS) and mediates LPS-induced
inflammatory response, including TNF secretion. Participates in
the ER-associated degradation (ERAD) quality control pathway in
conjunction with J domain-containing co-chaperones and the E3
ligase STUB1. {ECO:0000250|UniProtKB:P11142}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs. Interacts with PACRG. Interacts
with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts
with DNAJC7. Interacts with DNAJB12 (via J domain). Interacts with
DNAJB14 (via J domain). Interacts (via C-terminus) with the E3
ligase STUB1 forming a 210 kDa complex of one STUB1 and two HSPA8
molecules. Interacts with CITED1 (via N-terminus); the interaction
suppresses the association of CITED1 to p300/CBP and Smad-mediated
transcription transactivation. Component of the PRP19-CDC5L
splicing complex composed of a core complex comprising a
homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three
less stably associated proteins CTNNBL1, CWC15 and HSPA8.
Interacts with TRIM5. Part of a complex composed at least of
ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A,
WDR5 and ZNF335; this complex may have a histone H3-specific
methyltransferase activity. Interacts with METTL21A. Following LPS
binding, may form a complex with CXCR4, GDF5 and HSP90AA1.
Interacts with PRKN. Interacts with FOXP3. Interacts with DNAJC9
(via J domain). Interacts with MLLT11. Interacts with RNF207.
Interacts with DNAJC21. Interacts with DNAJB2. Interacts with TTC1
(via TPR repeats). Interacts with SGTA (via TPR repeats).
Interacts with HSF1 (via transactivation domain). Interacts with
HOPX, STUB1, HSP40, HSP90, BAG2 and BAG3. Interacts with DNAJC12.
{ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P63018}.
-!- INTERACTION:
P13569:CFTR (xeno); NbExp=2; IntAct=EBI-907802, EBI-349854;
P26361:Cftr (xeno); NbExp=5; IntAct=EBI-907802, EBI-6115317;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
{ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Localized in cytoplasmic mRNP granules
containing untranslated mRNAs. Translocates rapidly from the
cytoplasm to the nuclei, and especially to the nucleoli, upon heat
shock (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: Constitutively synthesized.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000250|UniProtKB:P11142}.
-!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.
-!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
{ECO:0000250|UniProtKB:P11142}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; X53827; CAA37823.1; -; mRNA.
EMBL; X53335; CAA37422.1; -; mRNA.
EMBL; BT030487; ABQ12927.1; -; mRNA.
EMBL; BC105182; AAI05183.1; -; mRNA.
PIR; S11456; S11456.
RefSeq; NP_776770.2; NM_174345.4.
UniGene; Bt.12309; -.
PDB; 1ATR; X-ray; 2.34 A; A=1-386.
PDB; 1ATS; X-ray; 2.43 A; A=1-386.
PDB; 1BA0; X-ray; 1.90 A; A=1-386.
PDB; 1BA1; X-ray; 1.70 A; A=1-386.
PDB; 1BUP; X-ray; 1.70 A; A=1-386.
PDB; 1HPM; X-ray; 1.70 A; A=1-386.
PDB; 1HX1; X-ray; 1.90 A; A=4-381.
PDB; 1KAX; X-ray; 1.70 A; A=1-381.
PDB; 1KAY; X-ray; 1.70 A; A=1-381.
PDB; 1KAZ; X-ray; 1.70 A; A=1-381.
PDB; 1NGA; X-ray; 2.18 A; A=1-386.
PDB; 1NGB; X-ray; 2.18 A; A=1-386.
PDB; 1NGC; X-ray; 2.20 A; A=1-386.
PDB; 1NGD; X-ray; 2.18 A; A=1-386.
PDB; 1NGE; X-ray; 2.05 A; A=1-386.
PDB; 1NGF; X-ray; 2.17 A; A=1-386.
PDB; 1NGG; X-ray; 2.19 A; A=1-386.
PDB; 1NGH; X-ray; 2.23 A; A=1-386.
PDB; 1NGI; X-ray; 2.15 A; A=1-386.
PDB; 1NGJ; X-ray; 2.10 A; A=1-386.
PDB; 1Q2G; Model; -; B=4-381.
PDB; 1QQM; X-ray; 1.90 A; A=4-381.
PDB; 1QQN; X-ray; 1.90 A; A=4-381.
PDB; 1QQO; X-ray; 1.90 A; A=4-381.
PDB; 1YUW; X-ray; 2.60 A; A=1-554.
PDB; 2BUP; X-ray; 1.70 A; A=1-381.
PDB; 2QW9; X-ray; 1.85 A; A/B=1-394.
PDB; 2QWL; X-ray; 1.75 A; A/B=1-394.
PDB; 2QWM; X-ray; 1.86 A; A/B=1-394.
PDB; 2QWN; X-ray; 2.40 A; A=1-394.
PDB; 2QWO; X-ray; 1.70 A; A=1-394.
PDB; 2QWP; X-ray; 1.75 A; A=1-394.
PDB; 2QWQ; X-ray; 2.21 A; A=1-394.
PDB; 2QWR; X-ray; 2.21 A; A=1-394.
PDB; 3C7N; X-ray; 3.12 A; B=1-554.
PDB; 3HSC; X-ray; 1.93 A; A=1-386.
PDB; 4FL9; X-ray; 1.90 A; A=1-554.
PDBsum; 1ATR; -.
PDBsum; 1ATS; -.
PDBsum; 1BA0; -.
PDBsum; 1BA1; -.
PDBsum; 1BUP; -.
PDBsum; 1HPM; -.
PDBsum; 1HX1; -.
PDBsum; 1KAX; -.
PDBsum; 1KAY; -.
PDBsum; 1KAZ; -.
PDBsum; 1NGA; -.
PDBsum; 1NGB; -.
PDBsum; 1NGC; -.
PDBsum; 1NGD; -.
PDBsum; 1NGE; -.
PDBsum; 1NGF; -.
PDBsum; 1NGG; -.
PDBsum; 1NGH; -.
PDBsum; 1NGI; -.
PDBsum; 1NGJ; -.
PDBsum; 1Q2G; -.
PDBsum; 1QQM; -.
PDBsum; 1QQN; -.
PDBsum; 1QQO; -.
PDBsum; 1YUW; -.
PDBsum; 2BUP; -.
PDBsum; 2QW9; -.
PDBsum; 2QWL; -.
PDBsum; 2QWM; -.
PDBsum; 2QWN; -.
PDBsum; 2QWO; -.
PDBsum; 2QWP; -.
PDBsum; 2QWQ; -.
PDBsum; 2QWR; -.
PDBsum; 3C7N; -.
PDBsum; 3HSC; -.
PDBsum; 4FL9; -.
ProteinModelPortal; P19120; -.
SMR; P19120; -.
BioGrid; 159144; 2.
DIP; DIP-35481N; -.
IntAct; P19120; 7.
MINT; MINT-157582; -.
STRING; 9913.ENSBTAP00000017497; -.
BindingDB; P19120; -.
ChEMBL; CHEMBL1275213; -.
PaxDb; P19120; -.
PeptideAtlas; P19120; -.
PRIDE; P19120; -.
Ensembl; ENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
GeneID; 281831; -.
KEGG; bta:281831; -.
CTD; 3312; -.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00890000139357; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; P19120; -.
KO; K03283; -.
OMA; IANPIMT; -.
OrthoDB; EOG091G03SF; -.
TreeFam; TF105042; -.
Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-BTA-3371568; Attenuation phase.
Reactome; R-BTA-3371571; HSF1-dependent transactivation.
Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-72163; mRNA Splicing - Major Pathway.
Reactome; R-BTA-8856828; Clathrin-mediated endocytosis.
Reactome; R-BTA-8876725; Protein methylation.
EvolutionaryTrace; P19120; -.
PRO; PR:P19120; -.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000013162; -.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C.
InterPro; IPR029047; HSP70_peptide-bd.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Isopeptide bond; Membrane; Methylation;
mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Spliceosome;
Stress response; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11142}.
CHAIN 2 650 Heat shock cognate 71 kDa protein.
/FTId=PRO_0000078268.
NP_BIND 12 15 ATP.
NP_BIND 202 204 ATP.
NP_BIND 268 275 ATP.
NP_BIND 339 342 ATP.
REGION 2 386 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 186 377 Interaction with BAG1. {ECO:0000250}.
REGION 394 509 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 71 71 ATP.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 246 246 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 319 319 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 319 319 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 328 328 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 512 512 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 512 512 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 524 524 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63017}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 589 589 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 597 597 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
MOD_RES 601 601 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11142}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P11142}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P11142}.
CONFLICT 180 180 A -> T (in Ref. 3; AAI05183).
{ECO:0000305}.
CONFLICT 543 543 E -> K (in Ref. 1; CAA37422/CAA37823).
{ECO:0000305}.
STRAND 7 10 {ECO:0000244|PDB:1BA1}.
STRAND 13 22 {ECO:0000244|PDB:1BA1}.
STRAND 25 28 {ECO:0000244|PDB:1BA1}.
STRAND 36 39 {ECO:0000244|PDB:1BA1}.
STRAND 42 44 {ECO:0000244|PDB:1BA1}.
STRAND 49 51 {ECO:0000244|PDB:1BA1}.
HELIX 53 56 {ECO:0000244|PDB:1BA1}.
TURN 57 61 {ECO:0000244|PDB:1BA1}.
HELIX 63 65 {ECO:0000244|PDB:1BA1}.
STRAND 66 68 {ECO:0000244|PDB:4FL9}.
HELIX 70 72 {ECO:0000244|PDB:1BA1}.
TURN 73 75 {ECO:0000244|PDB:1BA1}.
HELIX 81 87 {ECO:0000244|PDB:1BA1}.
STRAND 91 97 {ECO:0000244|PDB:1BA1}.
STRAND 100 107 {ECO:0000244|PDB:1BA1}.
STRAND 110 114 {ECO:0000244|PDB:1BA1}.
HELIX 116 135 {ECO:0000244|PDB:1BA1}.
STRAND 141 146 {ECO:0000244|PDB:1BA1}.
HELIX 152 164 {ECO:0000244|PDB:1BA1}.
STRAND 168 174 {ECO:0000244|PDB:1BA1}.
HELIX 175 182 {ECO:0000244|PDB:1BA1}.
TURN 183 186 {ECO:0000244|PDB:1BA1}.
STRAND 187 191 {ECO:0000244|PDB:2QWL}.
STRAND 193 200 {ECO:0000244|PDB:1BA1}.
STRAND 205 213 {ECO:0000244|PDB:1BA1}.
STRAND 216 225 {ECO:0000244|PDB:1BA1}.
HELIX 230 249 {ECO:0000244|PDB:1BA1}.
HELIX 253 255 {ECO:0000244|PDB:4FL9}.
HELIX 257 273 {ECO:0000244|PDB:1BA1}.
TURN 274 276 {ECO:0000244|PDB:1BA1}.
STRAND 277 288 {ECO:0000244|PDB:1BA1}.
STRAND 291 298 {ECO:0000244|PDB:1BA1}.
HELIX 299 312 {ECO:0000244|PDB:1BA1}.
HELIX 314 323 {ECO:0000244|PDB:1BA1}.
HELIX 328 330 {ECO:0000244|PDB:1BA1}.
STRAND 333 338 {ECO:0000244|PDB:1BA1}.
HELIX 339 342 {ECO:0000244|PDB:1BA1}.
HELIX 344 353 {ECO:0000244|PDB:1BA1}.
TURN 354 356 {ECO:0000244|PDB:1BA1}.
HELIX 365 367 {ECO:0000244|PDB:1BA1}.
HELIX 368 380 {ECO:0000244|PDB:1BA1}.
STRAND 386 388 {ECO:0000244|PDB:2QWO}.
STRAND 392 396 {ECO:0000244|PDB:3C7N}.
STRAND 401 405 {ECO:0000244|PDB:4FL9}.
TURN 406 408 {ECO:0000244|PDB:4FL9}.
STRAND 409 414 {ECO:0000244|PDB:4FL9}.
STRAND 419 432 {ECO:0000244|PDB:4FL9}.
STRAND 438 446 {ECO:0000244|PDB:4FL9}.
HELIX 450 452 {ECO:0000244|PDB:4FL9}.
STRAND 453 461 {ECO:0000244|PDB:4FL9}.
STRAND 474 480 {ECO:0000244|PDB:4FL9}.
STRAND 486 492 {ECO:0000244|PDB:4FL9}.
TURN 493 495 {ECO:0000244|PDB:4FL9}.
STRAND 498 503 {ECO:0000244|PDB:4FL9}.
HELIX 512 524 {ECO:0000244|PDB:4FL9}.
HELIX 526 534 {ECO:0000244|PDB:4FL9}.
STRAND 539 542 {ECO:0000244|PDB:4FL9}.
HELIX 547 549 {ECO:0000244|PDB:4FL9}.
SEQUENCE 650 AA; 71241 MW; FBE109C14A28B925 CRC64;
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD


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