DNJC3_HUMAN
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 03-AUG-2022, entry version 193.
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.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/dnajc3/";
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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_006260.4.
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; 187.
DR CORUM; Q13217; -.
DR IntAct; Q13217; 14.
DR STRING; 9606.ENSP00000473631; -.
DR iPTMnet; Q13217; -.
DR MetOSite; Q13217; -.
DR PhosphoSitePlus; Q13217; -.
DR BioMuta; DNAJC3; -.
DR DMDM; 73620807; -.
DR EPD; Q13217; -.
DR jPOST; Q13217; -.
DR MassIVE; Q13217; -.
DR MaxQB; Q13217; -.
DR PaxDb; Q13217; -.
DR PeptideAtlas; Q13217; -.
DR PRIDE; Q13217; -.
DR ProteomicsDB; 59230; -.
DR Antibodypedia; 24863; 170 antibodies from 29 providers.
DR DNASU; 5611; -.
DR Ensembl; ENST00000602402.6; ENSP00000473631.1; ENSG00000102580.15.
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 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 neXtProt; NX_Q13217; -.
DR OpenTargets; ENSG00000102580; -.
DR Orphanet; 445062; Juvenile-onset diabetes mellitus-central and peripheral neurodegeneration syndrome.
DR PharmGKB; PA27420; -.
DR VEuPathDB; HostDB:ENSG00000102580; -.
DR eggNOG; KOG0624; Eukaryota.
DR GeneTree; ENSGT00940000159806; -.
DR InParanoid; Q13217; -.
DR OMA; PFAHFQH; -.
DR OrthoDB; 1106865at2759; -.
DR PhylomeDB; Q13217; -.
DR TreeFam; TF105162; -.
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 SignaLink; Q13217; -.
DR SIGNOR; Q13217; -.
DR BioGRID-ORCS; 5611; 17 hits in 1083 CRISPR screens.
DR ChiTaRS; DNAJC3; human.
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 190 other tissues.
DR ExpressionAtlas; Q13217; baseline and differential.
DR Genevisible; Q13217; HS.
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:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
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: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; 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 Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR018704; TPR_21.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09976; TPR_21; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48452; SSF48452; 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; Reference proteome; Repeat; Repressor; Signal;
KW 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
