HSP76_HUMAN
ID HSP76_HUMAN Reviewed; 643 AA.
AC P17066; Q1HBA8; Q8IYK7; Q9BT95;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Heat shock 70 kDa protein 6;
DE AltName: Full=Heat shock 70 kDa protein B';
GN Name=HSPA6; Synonyms=HSP70B';
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Lung;
RX PubMed=2327978; DOI=10.1042/bj2670125;
RA Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.;
RT "The human heat-shock protein family. Expression of a novel heat-inducible
RT HSP70 (HSP70B') and isolation of its cDNA and genomic DNA.";
RL Biochem. J. 267:125-132(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-65; GLN-95; THR-150;
RP SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178; LYS-194; PHE-198;
RP LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577 AND ALA-626.
RG NIEHS SNPs program;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
RX PubMed=1346391; DOI=10.1016/0888-7543(92)90409-l;
RA Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.;
RT "The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize
RT to chromosome 1.";
RL Genomics 12:74-79(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=3184191; DOI=10.1016/0022-2836(88)90094-0;
RA Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.;
RT "Cis-acting elements involved in the regulated expression of a human HSP70
RT gene.";
RL J. Mol. Biol. 203:97-105(1988).
RN [7]
RP METHYLATION AT LYS-563, AND MUTAGENESIS OF LYS-563.
RX PubMed=23921388; DOI=10.1074/jbc.m113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human methyltransferase
RT modulating Hsp70 function through lysine methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [8]
RP REVIEW.
RX PubMed=26865365; DOI=10.1007/s12192-016-0676-6;
RA Radons J.;
RT "The human HSP70 family of chaperones: where do we stand?";
RL Cell Stress Chaperones 21:379-404(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-385 IN COMPLEX WITH ADP AND
RP PHOSPHATE.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70 isoforms:
RT HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
CC -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC processes, including protection of the proteome from stress, folding
CC and transport of newly synthesized polypeptides, activation of
CC proteolysis of misfolded proteins and the formation and dissociation of
CC protein complexes. Plays a pivotal role in the protein quality control
CC system, ensuring the correct folding of proteins, the re-folding of
CC misfolded proteins and controlling the targeting of proteins for
CC subsequent degradation. This is achieved through cycles of ATP binding,
CC ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity
CC for polypeptides is regulated by its nucleotide bound state. In the
CC ATP-bound form, it has a low affinity for substrate proteins. However,
CC upon hydrolysis of the ATP to ADP, it undergoes a conformational change
CC that increases its affinity for substrate proteins. It goes through
CC repeated cycles of ATP hydrolysis and nucleotide exchange, which
CC permits cycles of substrate binding and release (PubMed:26865365).
CC {ECO:0000303|PubMed:26865365}.
CC -!- INTERACTION:
CC P17066; O43865: AHCYL1; NbExp=3; IntAct=EBI-355106, EBI-2371423;
CC P17066; O95429: BAG4; NbExp=3; IntAct=EBI-355106, EBI-2949658;
CC P17066; Q8WYQ4-2: C22orf15; NbExp=3; IntAct=EBI-355106, EBI-12030460;
CC P17066; Q7Z4G1: COMMD6; NbExp=3; IntAct=EBI-355106, EBI-1550081;
CC P17066; P21333-2: FLNA; NbExp=3; IntAct=EBI-355106, EBI-9641086;
CC P17066; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-355106, EBI-8473062;
CC P17066; P47929: LGALS7B; NbExp=3; IntAct=EBI-355106, EBI-357504;
CC P17066; P23284: PPIB; NbExp=3; IntAct=EBI-355106, EBI-359252;
CC P17066; Q96NZ9: PRAP1; NbExp=3; IntAct=EBI-355106, EBI-2116102;
CC P17066; P27694: RPA1; NbExp=3; IntAct=EBI-355106, EBI-621389;
CC P17066; P54274: TERF1; NbExp=2; IntAct=EBI-355106, EBI-710997;
CC -!- INDUCTION: Only at higher temperatures, and no basal expression.
CC -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC C-terminal substrate-binding domain (SBD) (also known as peptide-
CC binding domain) binds to the client/substrate proteins. The two domains
CC are allosterically coupled so that, when ATP is bound to the NBD, the
CC SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC conformational change enhances the affinity of the SBD for client
CC proteins. {ECO:0000305|PubMed:26865365}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa6/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51757; CAA36061.1; -; Genomic_DNA.
DR EMBL; X51758; CAA36062.1; -; mRNA.
DR EMBL; DQ521571; ABF47108.1; -; Genomic_DNA.
DR EMBL; AL590385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004279; AAH04279.1; -; mRNA.
DR EMBL; BC035665; AAH35665.1; -; mRNA.
DR EMBL; S78631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1231.1; -.
DR PIR; S09036; S09036.
DR RefSeq; NP_002146.2; NM_002155.4.
DR PDB; 3FE1; X-ray; 2.20 A; A/B/C=6-385.
DR PDBsum; 3FE1; -.
DR AlphaFoldDB; P17066; -.
DR SMR; P17066; -.
DR BioGRID; 109542; 290.
DR IntAct; P17066; 108.
DR MINT; P17066; -.
DR STRING; 9606.ENSP00000310219; -.
DR ChEMBL; CHEMBL3232688; -.
DR GlyConnect; 1298; 1 N-Linked glycan (1 site).
DR GlyGen; P17066; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P17066; -.
DR PhosphoSitePlus; P17066; -.
DR SwissPalm; P17066; -.
DR BioMuta; HSPA6; -.
DR DMDM; 34978357; -.
DR UCD-2DPAGE; P17066; -.
DR EPD; P17066; -.
DR jPOST; P17066; -.
DR MassIVE; P17066; -.
DR MaxQB; P17066; -.
DR PaxDb; P17066; -.
DR PeptideAtlas; P17066; -.
DR PRIDE; P17066; -.
DR ProteomicsDB; 53451; -.
DR Antibodypedia; 34311; 331 antibodies from 31 providers.
DR DNASU; 3310; -.
DR Ensembl; ENST00000309758.6; ENSP00000310219.4; ENSG00000173110.8.
DR GeneID; 3310; -.
DR KEGG; hsa:3310; -.
DR MANE-Select; ENST00000309758.6; ENSP00000310219.4; NM_002155.5; NP_002146.2.
DR UCSC; uc001gaq.4; human.
DR CTD; 3310; -.
DR DisGeNET; 3310; -.
DR GeneCards; HSPA6; -.
DR HGNC; HGNC:5239; HSPA6.
DR HPA; ENSG00000173110; Tissue enriched (brain).
DR MIM; 140555; gene.
DR neXtProt; NX_P17066; -.
DR OpenTargets; ENSG00000173110; -.
DR PharmGKB; PA29505; -.
DR VEuPathDB; HostDB:ENSG00000173110; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000163722; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P17066; -.
DR OMA; CFELSGI; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P17066; -.
DR TreeFam; TF105042; -.
DR PathwayCommons; P17066; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P17066; -.
DR SIGNOR; P17066; -.
DR BioGRID-ORCS; 3310; 17 hits in 1044 CRISPR screens.
DR EvolutionaryTrace; P17066; -.
DR GeneWiki; HSPA6; -.
DR GenomeRNAi; 3310; -.
DR Pharos; P17066; Tbio.
DR PRO; PR:P17066; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P17066; protein.
DR Bgee; ENSG00000173110; Expressed in blood and 95 other tissues.
DR ExpressionAtlas; P17066; baseline and differential.
DR Genevisible; P17066; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Methylation; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..643
FT /note="Heat shock 70 kDa protein 6"
FT /id="PRO_0000078264"
FT REGION 3..388
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 396..511
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 616..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 204..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 341..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 563
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000269|PubMed:23921388"
FT VARIANT 65
FT /note="P -> T (in dbSNP:rs41297698)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060718"
FT VARIANT 95
FT /note="R -> Q (in dbSNP:rs400835)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060719"
FT VARIANT 150
FT /note="A -> T (in dbSNP:rs10919224)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049605"
FT VARIANT 153
FT /note="N -> S (in dbSNP:rs10919225)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049606"
FT VARIANT 154
FT /note="D -> N (in dbSNP:rs10919226)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049607"
FT VARIANT 159
FT /note="A -> V (in dbSNP:rs41297702)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060720"
FT VARIANT 170
FT /note="N -> K (in dbSNP:rs41297704)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049608"
FT VARIANT 173
FT /note="R -> P (in dbSNP:rs41297708)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049609"
FT VARIANT 178
FT /note="P -> A (in dbSNP:rs41297710)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049610"
FT VARIANT 194
FT /note="E -> K (in dbSNP:rs41297714)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049611"
FT VARIANT 198
FT /note="L -> F (in dbSNP:rs1079109)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_024182"
FT VARIANT 260
FT /note="R -> H (in dbSNP:rs41299256)"
FT /id="VAR_049612"
FT VARIANT 297
FT /note="T -> K (in dbSNP:rs41297718)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_060721"
FT VARIANT 336
FT /note="V -> F (in dbSNP:rs417707)"
FT /id="VAR_059360"
FT VARIANT 464
FT /note="S -> I (in dbSNP:rs388218)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049613"
FT VARIANT 471
FT /note="R -> H (in dbSNP:rs41299256)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049614"
FT VARIANT 528
FT /note="K -> E (in dbSNP:rs570189)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049615"
FT VARIANT 528
FT /note="K -> R (in dbSNP:rs570167)"
FT /id="VAR_059361"
FT VARIANT 562
FT /note="D -> E (in dbSNP:rs753856)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_024183"
FT VARIANT 572
FT /note="M -> V (in dbSNP:rs452004)"
FT /id="VAR_049616"
FT VARIANT 577
FT /note="R -> Q (in dbSNP:rs368844)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049617"
FT VARIANT 626
FT /note="T -> A (in dbSNP:rs41299260)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_049618"
FT MUTAGEN 563
FT /note="K->R: Complete loss of in vitro methylation by
FT METTL21A."
FT /evidence="ECO:0000269|PubMed:23921388"
FT CONFLICT 106..108
FT /note="RVC -> PVS (in Ref. 1; CAA36061)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> G (in Ref. 1; CAA36061)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 232..251
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3FE1"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:3FE1"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3FE1"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:3FE1"
SQ SEQUENCE 643 AA; 71028 MW; BCE348F0226DB70B CRC64;
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ
AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE
ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV
NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA
TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF
DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA
KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
