HS71L_HUMAN
ID HS71L_HUMAN Reviewed; 641 AA.
AC P34931; A6NNB0; B0UXW8; O75634; Q2HXR3; Q8NE72; Q96QC9; Q9UQM1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Heat shock 70 kDa protein 1-like;
DE Short=Heat shock 70 kDa protein 1L;
DE AltName: Full=Heat shock 70 kDa protein 1-Hom;
DE Short=HSP70-Hom;
GN Name=HSPA1L;
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], AND INDUCTION.
RX PubMed=1700760; DOI=10.1007/bf00187095;
RA Milner C.M., Campbell R.D.;
RT "Structure and expression of the three MHC-linked HSP70 genes.";
RL Immunogenetics 32:242-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9685725; DOI=10.1093/oxfordjournals.jbchem.a022118;
RA Ito Y., Ando A., Ando H., Ando J., Saijoh Y., Inoko H., Fujimoto H.;
RT "Genomic structure of the spermatid-specific HSP70 homolog gene located in
RT the class III region of the major histocompatibility complex of mouse and
RT man.";
RL J. Biochem. 124:347-353(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-8; THR-268; GLY-294;
RP MET-479; MET-493; ALA-558 AND LYS-602.
RG NIEHS SNPs program;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-493.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-493.
RC TISSUE=Testis;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION IN PRKN TRANSLOCATION, INTERACTION WITH PRKN, AND MUTAGENESIS OF
RP LYS-73; LEU-396 AND 638-GLU--ASP-641.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E.,
RA Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.;
RT "High-content genome-wide RNAi screens identify regulators of parkin
RT upstream of mitophagy.";
RL Nature 504:291-295(2013).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-386 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).
RN [12]
RP VARIANT MET-493.
RX PubMed=1356099; DOI=10.1007/bf00218042;
RA Milner C.M., Campbell R.D.;
RT "Polymorphic analysis of the three MHC-linked HSP70 genes.";
RL Immunogenetics 36:357-362(1992).
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 Positive regulator of PRKN translocation to damaged mitochondria
CC (PubMed:24270810). {ECO:0000269|PubMed:24270810,
CC ECO:0000303|PubMed:26865365}.
CC -!- SUBUNIT: Interacts with PRKN. {ECO:0000269|PubMed:20072699,
CC ECO:0000269|PubMed:24270810}.
CC -!- INTERACTION:
CC P34931; O95429: BAG4; NbExp=4; IntAct=EBI-354912, EBI-2949658;
CC P34931; O00635: TRIM38; NbExp=3; IntAct=EBI-354912, EBI-2130415;
CC -!- TISSUE SPECIFICITY: Expressed in spermatids.
CC {ECO:0000269|PubMed:9685725}.
CC -!- INDUCTION: Not induced by heat shock. {ECO:0000269|PubMed:1700760}.
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/hspa1l/";
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; M59829; AAA63228.1; -; Genomic_DNA.
DR EMBL; D85730; BAA32521.1; -; mRNA.
DR EMBL; AF134726; AAD21817.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63301.1; -; Genomic_DNA.
DR EMBL; DQ383515; ABC88476.1; -; Genomic_DNA.
DR EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034483; AAH34483.1; -; mRNA.
DR CCDS; CCDS34413.1; -.
DR PIR; B45871; B45871.
DR RefSeq; NP_005518.3; NM_005527.3.
DR PDB; 3GDQ; X-ray; 1.80 A; A=1-386.
DR PDBsum; 3GDQ; -.
DR AlphaFoldDB; P34931; -.
DR SMR; P34931; -.
DR BioGRID; 109537; 270.
DR ELM; P34931; -.
DR IntAct; P34931; 81.
DR MINT; P34931; -.
DR STRING; 9606.ENSP00000364805; -.
DR GlyConnect; 1297; 2 N-Linked glycans (2 sites).
DR GlyGen; P34931; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P34931; -.
DR PhosphoSitePlus; P34931; -.
DR SwissPalm; P34931; -.
DR BioMuta; HSPA1L; -.
DR DMDM; 23831140; -.
DR UCD-2DPAGE; P34931; -.
DR EPD; P34931; -.
DR jPOST; P34931; -.
DR MassIVE; P34931; -.
DR MaxQB; P34931; -.
DR PaxDb; P34931; -.
DR PeptideAtlas; P34931; -.
DR PRIDE; P34931; -.
DR ProteomicsDB; 54956; -.
DR TopDownProteomics; P34931; -.
DR Antibodypedia; 13096; 428 antibodies from 35 providers.
DR DNASU; 3305; -.
DR Ensembl; ENST00000375654.5; ENSP00000364805.4; ENSG00000204390.10.
DR Ensembl; ENST00000383390.4; ENSP00000372881.4; ENSG00000206383.8.
DR Ensembl; ENST00000417601.2; ENSP00000396486.2; ENSG00000234258.6.
DR Ensembl; ENST00000456772.2; ENSP00000408347.2; ENSG00000236251.6.
DR GeneID; 3305; -.
DR KEGG; hsa:3305; -.
DR MANE-Select; ENST00000375654.5; ENSP00000364805.4; NM_005527.4; NP_005518.3.
DR UCSC; uc003nxh.4; human.
DR CTD; 3305; -.
DR DisGeNET; 3305; -.
DR GeneCards; HSPA1L; -.
DR HGNC; HGNC:5234; HSPA1L.
DR HPA; ENSG00000204390; Tissue enriched (testis).
DR MIM; 140559; gene.
DR neXtProt; NX_P34931; -.
DR OpenTargets; ENSG00000204390; -.
DR PharmGKB; PA29500; -.
DR VEuPathDB; HostDB:ENSG00000204390; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000162096; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P34931; -.
DR OMA; ESYAYHM; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P34931; -.
DR TreeFam; TF105042; -.
DR PathwayCommons; P34931; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
DR SignaLink; P34931; -.
DR BioGRID-ORCS; 3305; 11 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; P34931; -.
DR GeneWiki; HSPA1L; -.
DR GenomeRNAi; 3305; -.
DR Pharos; P34931; Tbio.
DR PRO; PR:P34931; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P34931; protein.
DR Bgee; ENSG00000204390; Expressed in left testis and 100 other tissues.
DR ExpressionAtlas; P34931; baseline and differential.
DR Genevisible; P34931; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
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:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
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; Nucleotide-binding; Reference proteome.
FT CHAIN 1..641
FT /note="Heat shock 70 kDa protein 1-like"
FT /id="PRO_0000078255"
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 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 VARIANT 8
FT /note="A -> P (in dbSNP:rs9469057)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025841"
FT VARIANT 268
FT /note="A -> T (in dbSNP:rs34620296)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025842"
FT VARIANT 294
FT /note="D -> G (in dbSNP:rs34360259)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025843"
FT VARIANT 479
FT /note="T -> M (in dbSNP:rs482145)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025844"
FT VARIANT 493
FT /note="T -> M (in dbSNP:rs2227956)"
FT /evidence="ECO:0000269|PubMed:1356099,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_003820"
FT VARIANT 558
FT /note="E -> A (in dbSNP:rs2227955)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025845"
FT VARIANT 602
FT /note="E -> K (in dbSNP:rs2075800)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_025846"
FT MUTAGEN 73
FT /note="K->E: No rescue of PRKN translocation deficit in
FT knockout cells."
FT /evidence="ECO:0000269|PubMed:24270810"
FT MUTAGEN 396
FT /note="L->D: No rescue of PRKN translocation deficit in
FT knockout cells."
FT /evidence="ECO:0000269|PubMed:24270810"
FT MUTAGEN 638..641
FT /note="Missing: No rescue of PRKN translocation deficit in
FT knockout cells."
FT /evidence="ECO:0000269|PubMed:24270810"
FT CONFLICT 408
FT /note="A -> V (in Ref. 1; AAA63228)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="I -> M (in Ref. 7; AAH34483)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="T -> P (in Ref. 1; AAA63228)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="T -> A (in Ref. 7; AAH34483)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="V -> M (in Ref. 2; BAA32521)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:3GDQ"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 232..251
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:3GDQ"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3GDQ"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:3GDQ"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:3GDQ"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3GDQ"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:3GDQ"
SQ SEQUENCE 641 AA; 70375 MW; A9339D7657166FF7 CRC64;
MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE
ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF
DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA
KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE
LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV D
