ID   DNJC3_HUMAN             Reviewed;         504 AA.
AC   Q13217; Q86WT9; Q8N4N2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   28-JAN-2026, entry version 210.
DE   RecName: Full=DnaJ homolog subfamily C member 3;
DE   AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 6;
DE            Short=ER-resident protein ERdj6;
DE            Short=ERdj6;
DE   AltName: Full=Interferon-induced, double-stranded RNA-activated protein kinase inhibitor;
DE   AltName: Full=Protein kinase inhibitor of 58 kDa;
DE            Short=Protein kinase inhibitor p58;
DE   Flags: Precursor;
GN   Name=DNAJC3; Synonyms=P58IPK, PRKRI;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=8666242; DOI=10.1016/0378-1119(95)00883-7;
RA   Korth M.J., Lyons C.N., Wambach M., Katze M.G.;
RT   "Cloning, expression, and cellular localization of the oncogenic 58-kDa
RT   inhibitor of the RNA-activated human and mouse protein kinase.";
RL   Gene 170:181-188(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Leukocyte;
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   FUNCTION, AND INTERACTION WITH EIF2AK2.
RX   PubMed=8576172; DOI=10.1074/jbc.271.3.1702;
RA   Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.;
RT   "The P58 cellular inhibitor complexes with the interferon-induced, double-
RT   stranded RNA-dependent protein kinase, PKR, to regulate its
RT   autophosphorylation and activity.";
RL   J. Biol. Chem. 271:1702-1707(1996).
RN   [6]
RP   FUNCTION, INTERACTION WITH THAP12, AND INDUCTION.
RX   PubMed=9447982; DOI=10.1128/mcb.18.2.859;
RA   Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M.,
RA   Romano P.R., Katze M.G.;
RT   "Regulation of interferon-induced protein kinase PKR: modulation of P58IPK
RT   inhibitory function by a novel protein, P52rIPK.";
RL   Mol. Cell. Biol. 18:859-871(1998).
RN   [7]
RP   FUNCTION, INTERACTION WITH DNAJB1 AND HSPA8, AND INDUCTION.
RX   PubMed=9920933; DOI=10.1074/jbc.274.6.3797;
RA   Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.;
RT   "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an
RT   influenza virus-activated co-chaperone that modulates heat shock protein 70
RT   activity.";
RL   J. Biol. Chem. 274:3797-3803(1999).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12601012; DOI=10.1074/jbc.m212074200;
RA   van Huizen R., Martindale J.L., Gorospe M., Holbrook N.J.;
RT   "P58IPK, a novel endoplasmic reticulum stress-inducible protein and
RT   potential negative regulator of eIF2alpha signaling.";
RL   J. Biol. Chem. 278:15558-15564(2003).
RN   [9]
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   [10]
RP   INVOLVEMENT IN ACPHD.
RX   PubMed=25466870; DOI=10.1016/j.ajhg.2014.10.013;
RA   Synofzik M., Haack T.B., Kopajtich R., Gorza M., Rapaport D., Greiner M.,
RA   Schoenfeld C., Freiberg C., Schorr S., Holl R.W., Gonzalez M.A.,
RA   Fritsche A., Fallier-Becker P., Zimmermann R., Strom T.M., Meitinger T.,
RA   Zuechner S., Schuele R., Schoels L., Prokisch H.;
RT   "Absence of BiP co-chaperone DNAJC3 causes diabetes mellitus and
RT   multisystemic neurodegeneration.";
RL   Am. J. Hum. Genet. 95:689-697(2014).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   PHOSPHORYLATION AT SER-274.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-461, AND DISULFIDE BONDS.
RX   PubMed=21799829; DOI=10.1371/journal.pone.0022337;
RA   Svard M., Biterova E.I., Bourhis J.M., Guy J.E.;
RT   "The crystal structure of the human co-chaperone P58(IPK).";
RL   PLoS ONE 6:E22337-E22337(2011).
CC   -!- FUNCTION: Involved in the unfolded protein response (UPR) during
CC       endoplasmic reticulum (ER) stress. Acts as a negative regulator of the
CC       EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-
CC       2-alpha at 'Ser-52' and hence attenuating general protein synthesis
CC       under ER stress, hypothermic and amino acid starving stress conditions
CC       (By similarity). Co-chaperone of HSPA8/HSC70, it stimulates its ATPase
CC       activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and
CC       the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May
CC       inhibit EIF2AK3/PERK activity. {ECO:0000250|UniProtKB:Q27968,
CC       ECO:0000250|UniProtKB:Q91YW3, ECO:0000269|PubMed:12601012,
CC       ECO:0000269|PubMed:8576172, ECO:0000269|PubMed:9447982,
CC       ECO:0000269|PubMed:9920933}.
CC   -!- SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction occurs under
CC       endoplasmic reticulum (ER) stress, hypothermic and amino acid starving
CC       stress conditions and inhibits EIF2AK4/GCN2 kinase activity. Interacts
CC       with EIF2AK3 (By similarity). Interacts with EIF2AK2 (PubMed:8576172).
CC       Forms a trimeric complex with DNAJB1 and HSPA8 (PubMed:9920933).
CC       Interacts with THAP12 (PubMed:9447982). {ECO:0000250|UniProtKB:Q91YW3,
CC       ECO:0000269|PubMed:8576172, ECO:0000269|PubMed:9447982,
CC       ECO:0000269|PubMed:9920933}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with high level in the pancreas
CC       and testis. Also expressed in cell lines with different levels.
CC       {ECO:0000269|PubMed:8666242}.
CC   -!- INDUCTION: Up-regulated during an endoplasmic reticulum stress via
CC       ATF6. Activated in response to infection by influenza virus through the
CC       dissociation of DNAJB1. Down-regulated by DNAJB1 and THAP12.
CC       {ECO:0000269|PubMed:12601012, ECO:0000269|PubMed:9447982,
CC       ECO:0000269|PubMed:9920933}.
CC   -!- DOMAIN: The J domain mediates interaction with HSPA8.
CC   -!- DOMAIN: Binding to misfolded proteins is mediated by a hydrophobic
CC       patch forming a large groove within the first two TPR repeats.
CC       {ECO:0000250}.
CC   -!- DISEASE: Ataxia, combined cerebellar and peripheral, with hearing loss
CC       and diabetes mellitus (ACPHD) [MIM:616192]: A disease characterized by
CC       juvenile-onset diabetes and neurodegeneration, resulting in ataxia,
CC       upper-motor-neuron damage, peripheral neuropathy, hearing loss, and
CC       cerebral atrophy. {ECO:0000269|PubMed:25466870}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
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DR   EMBL; U28424; AAC50502.1; -; mRNA.
DR   EMBL; AY795482; AAV40838.1; -; Genomic_DNA.
DR   EMBL; AL138955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047936; AAH47936.2; -; mRNA.
DR   CCDS; CCDS9479.1; -.
DR   PIR; JC4775; JC4775.
DR   RefSeq; NP_006251.1; NM_006260.5.
DR   PDB; 2Y4T; X-ray; 3.00 A; A/B/C=35-461.
DR   PDB; 2Y4U; X-ray; 3.20 A; A=35-461.
DR   PDBsum; 2Y4T; -.
DR   PDBsum; 2Y4U; -.
DR   AlphaFoldDB; Q13217; -.
DR   SMR; Q13217; -.
DR   BioGRID; 111597; 258.
DR   CORUM; Q13217; -.
DR   FunCoup; Q13217; 2297.
DR   IntAct; Q13217; 108.
DR   MINT; Q13217; -.
DR   STRING; 9606.ENSP00000473631; -.
DR   GlyGen; Q13217; 2 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; Q13217; -.
DR   MetOSite; Q13217; -.
DR   PhosphoSitePlus; Q13217; -.
DR   SwissPalm; Q13217; -.
DR   BioMuta; DNAJC3; -.
DR   DMDM; 73620807; -.
DR   jPOST; Q13217; -.
DR   MassIVE; Q13217; -.
DR   PaxDb; 9606-ENSP00000473631; -.
DR   PeptideAtlas; Q13217; -.
DR   ProteomicsDB; 59230; -.
DR   Pumba; Q13217; -.
DR   Antibodypedia; 24863; 164 antibodies from 29 providers.
DR   DNASU; 5611; -.
DR   Ensembl; ENST00000602402.6; ENSP00000473631.1; ENSG00000102580.16.
DR   GeneID; 5611; -.
DR   KEGG; hsa:5611; -.
DR   MANE-Select; ENST00000602402.6; ENSP00000473631.1; NM_006260.5; NP_006251.1.
DR   UCSC; uc001vmq.3; human.
DR   AGR; HGNC:9439; -.
DR   ClinPGx; PA27420; -.
DR   CTD; 5611; -.
DR   DisGeNET; 5611; -.
DR   GeneCards; DNAJC3; -.
DR   HGNC; HGNC:9439; DNAJC3.
DR   HPA; ENSG00000102580; Low tissue specificity.
DR   MalaCards; DNAJC3; -.
DR   MIM; 601184; gene.
DR   MIM; 616192; phenotype.
DR   OpenTargets; ENSG00000102580; -.
DR   Orphanet; 445062; Juvenile-onset diabetes mellitus-central and peripheral neurodegeneration syndrome.
DR   VEuPathDB; HostDB:ENSG00000102580; -.
DR   eggNOG; KOG0624; Eukaryota.
DR   GeneTree; ENSGT00940000159806; -.
DR   InParanoid; Q13217; -.
DR   OMA; PFAHFQH; -.
DR   OrthoDB; 1726119at2759; -.
DR   PAN-GO; Q13217; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q13217; -.
DR   PathwayCommons; Q13217; -.
DR   Reactome; R-HSA-192823; Viral mRNA Translation.
DR   Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-HSA-9833482; PKR-mediated signaling.
DR   SignaLink; Q13217; -.
DR   SIGNOR; Q13217; -.
DR   Agora; ENSG00000102580; -.
DR   BioGRID-ORCS; 5611; 17 hits in 1163 CRISPR screens.
DR   ChiTaRS; DNAJC3; human.
DR   EvolutionaryTrace; Q13217; -.
DR   GeneWiki; DNAJC3; -.
DR   GenomeRNAi; 5611; -.
DR   Pharos; Q13217; Tbio.
DR   PRO; PR:Q13217; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q13217; protein.
DR   Bgee; ENSG00000102580; Expressed in corpus epididymis and 192 other cell types or tissues.
DR   ExpressionAtlas; Q13217; baseline and differential.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; ISS:UniProtKB.
DR   GO; GO:1902010; P:negative regulation of translation in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0036494; P:positive regulation of translation initiation in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   FunFam; 1.25.40.10:FF:000122; DnaJ (Hsp40) homolog, subfamily C, member 3; 1.
DR   FunFam; 1.10.287.110:FF:000015; dnaJ homolog subfamily C member 3; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR051727; DnaJ_C3_Co-chaperones.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR44140:SF3; DNAJ HOMOLOG SUBFAMILY C MEMBER 3; 1.
DR   PANTHER; PTHR44140; LD25575P; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50005; TPR; 8.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Chaperone; Deafness; Diabetes mellitus;
KW   Disulfide bond; Endoplasmic reticulum; Neurodegeneration; Neuropathy;
KW   Phosphoprotein; Proteomics identification; Reference proteome; Repeat;
KW   Repressor; Signal; Stress response; TPR repeat; Translation regulation;
KW   Unfolded protein response.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..504
FT                   /note="DnaJ homolog subfamily C member 3"
FT                   /id="PRO_0000071045"
FT   REPEAT          37..70
FT                   /note="TPR 1"
FT   REPEAT          72..104
FT                   /note="TPR 2"
FT   REPEAT          105..138
FT                   /note="TPR 3"
FT   REPEAT          154..187
FT                   /note="TPR 4"
FT   REPEAT          189..221
FT                   /note="TPR 5"
FT   REPEAT          222..255
FT                   /note="TPR 6"
FT   REPEAT          268..301
FT                   /note="TPR 7"
FT   REPEAT          306..339
FT                   /note="TPR 8"
FT   REPEAT          340..373
FT                   /note="TPR 9"
FT   DOMAIN          394..462
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          375..393
FT                   /note="Flexible linker"
FT   REGION          451..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         274
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   DISULFID        248..258
FT                   /evidence="ECO:0000269|PubMed:21799829"
FT   DISULFID        313..329
FT                   /evidence="ECO:0000269|PubMed:21799829"
FT   HELIX           35..49
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           53..66
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           71..83
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           87..100
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:2Y4U"
FT   HELIX           105..117
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           138..167
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           170..183
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           188..200
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           208..218
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           222..234
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           238..251
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           256..281
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           284..297
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           302..317
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   TURN            318..320
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           322..335
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           340..352
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           356..367
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           374..391
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           396..398
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           409..420
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           423..425
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           429..448
FT                   /evidence="ECO:0007829|PDB:2Y4T"
FT   HELIX           451..454
FT                   /evidence="ECO:0007829|PDB:2Y4T"
SQ   SEQUENCE   504 AA;  57580 MW;  E720A1E7F618B912 CRC64;
     MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF
     HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL KMDFTAARLQ RGHLLLKQGK
     LDEAEDDFKK VLKSNPSENE EKEAQSQLIK SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI
     LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL
     SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS
     IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY LIEEMYDEAI
     QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ
     WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR
     SWNSWQGFNP FSSGGPFRFK FHFN
//