DJC10_MOUSE
ID DJC10_MOUSE Reviewed; 793 AA.
AC Q9DC23; A2ASA2; Q71S84; Q8CH78; Q8CIB0; Q99LV4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DnaJ homolog subfamily C member 10;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 5;
DE Short=ER-resident protein ERdj5;
DE Short=ERdj5;
DE AltName: Full=Endoplasmic reticulum DnaJ-PDI fusion protein 1;
DE AltName: Full=J domain-containing protein disulfide isomerase-like protein;
DE Short=J domain-containing PDI-like protein;
DE Short=JPDI;
DE Flags: Precursor;
GN Name=Dnajc10; Synonyms=Erdj5, Jpdi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12411443; DOI=10.1074/jbc.m206995200;
RA Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E.,
RA Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R.,
RA Spyrou G.;
RT "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and
RT thioredoxin domains, is expressed in secretory cells or following ER
RT stress.";
RL J. Biol. Chem. 278:1059-1066(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Simmen T., Mezghrani A., Bertoli G., Sitia R.;
RT "ERDJPs, a novel family of ER chaperones.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N x C57BL/6J; TISSUE=Mammary tumor;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
RP INTERACTION WITH HSPA5.
RX PubMed=12446677; DOI=10.1074/jbc.m208346200;
RA Hosoda A., Kimata Y., Tsuru A., Kohno K.;
RT "JPDI, a novel endoplasmic reticulum-resident protein containing both a
RT BiP-interacting J-domain and thioredoxin-like motifs.";
RL J. Biol. Chem. 278:2669-2676(2003).
RN [7]
RP FUNCTION, INTERACTION WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161;
RP CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
RX PubMed=18653895; DOI=10.1126/science.1159293;
RA Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.;
RT "ERdj5 is required as a disulfide reductase for degradation of misfolded
RT proteins in the ER.";
RL Science 321:569-572(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=19788412; DOI=10.1042/bj20091269;
RA Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T.;
RT "Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein
RT quality control in the salivary gland.";
RL Biochem. J. 425:117-125(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-793, FUNCTION, INTERACTION
RP WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161; CYS-480; CYS-483; CYS-588;
RP CYS-591; CYS-700 AND CYS-703.
RX PubMed=21329881; DOI=10.1016/j.molcel.2011.01.021;
RA Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K., Matsumoto Y.,
RA Hoseki J., Nagata K., Inaba K.;
RT "Structural basis of an ERAD pathway mediated by the ER-resident protein
RT disulfide reductase ERdj5.";
RL Mol. Cell 41:432-444(2011).
CC -!- FUNCTION: Endoplasmic reticulum disulfide reductase involved both in
CC the correct folding of proteins and degradation of misfolded proteins.
CC Required for efficient folding of proteins in the endoplasmic reticulum
CC by catalyzing the removal of non-native disulfide bonds formed during
CC the folding of proteins, such as LDLR. Also involved in endoplasmic
CC reticulum-associated degradation (ERAD) by reducing incorrect disulfide
CC bonds in misfolded glycoproteins recognized by EDEM1. Interaction with
CC HSPA5 is required its activity, not for the disulfide reductase
CC activity, but to facilitate the release of DNAJC10 from its substrate.
CC Promotes apoptotic signaling pathway in response to endoplasmic
CC reticulum stress. {ECO:0000269|PubMed:12411443,
CC ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895,
CC ECO:0000269|PubMed:21329881}.
CC -!- SUBUNIT: Interacts with HSPA5 (via its J domain). Interacts with EDEM1.
CC {ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895,
CC ECO:0000269|PubMed:21329881}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12446677}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in secretory
CC tissues. Ubiquitous in fetal tissues and tumor tissues. Higher
CC expression in fetal tissues than in adult tissues. Expressed in testis,
CC pancreas, fetal thymus and fetal kidney. High expression in heart,
CC liver, kidney, and testis. Low expression in spleen and skeletal
CC muscle. {ECO:0000269|PubMed:12411443, ECO:0000269|PubMed:12446677}.
CC -!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase domains.
CC {ECO:0000269|PubMed:21329881}.
CC -!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-active
CC CXXC motif. {ECO:0000269|PubMed:21329881}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and healthy but show enhanced
CC endoplasmic reticulum stress response in the salivary gland.
CC {ECO:0000269|PubMed:19788412}.
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DR EMBL; AF255459; AAN73273.1; -; mRNA.
DR EMBL; AF314002; AAQ14555.1; -; mRNA.
DR EMBL; AK004617; BAB23413.1; -; mRNA.
DR EMBL; AL928587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002207; AAH02207.1; -; mRNA.
DR EMBL; BC033461; AAH33461.1; -; mRNA.
DR CCDS; CCDS38159.1; -.
DR RefSeq; NP_077143.2; NM_024181.2.
DR PDB; 3APO; X-ray; 2.40 A; A=33-793.
DR PDB; 3APQ; X-ray; 1.84 A; A/B=34-242.
DR PDB; 3APS; X-ray; 1.90 A; A/B=668-789.
DR PDB; 5AYK; X-ray; 2.25 A; A=32-793.
DR PDB; 5AYL; X-ray; 2.40 A; A=32-793.
DR PDBsum; 3APO; -.
DR PDBsum; 3APQ; -.
DR PDBsum; 3APS; -.
DR PDBsum; 5AYK; -.
DR PDBsum; 5AYL; -.
DR AlphaFoldDB; Q9DC23; -.
DR SMR; Q9DC23; -.
DR BioGRID; 211769; 18.
DR IntAct; Q9DC23; 2.
DR MINT; Q9DC23; -.
DR STRING; 10090.ENSMUSP00000028392; -.
DR GlyGen; Q9DC23; 1 site.
DR iPTMnet; Q9DC23; -.
DR PhosphoSitePlus; Q9DC23; -.
DR EPD; Q9DC23; -.
DR MaxQB; Q9DC23; -.
DR PaxDb; Q9DC23; -.
DR PeptideAtlas; Q9DC23; -.
DR PRIDE; Q9DC23; -.
DR ProteomicsDB; 279417; -.
DR Antibodypedia; 33990; 232 antibodies from 29 providers.
DR DNASU; 66861; -.
DR Ensembl; ENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006.
DR GeneID; 66861; -.
DR KEGG; mmu:66861; -.
DR UCSC; uc008khj.1; mouse.
DR CTD; 54431; -.
DR MGI; MGI:1914111; Dnajc10.
DR VEuPathDB; HostDB:ENSMUSG00000027006; -.
DR eggNOG; KOG0191; Eukaryota.
DR eggNOG; KOG0713; Eukaryota.
DR GeneTree; ENSGT00940000155558; -.
DR HOGENOM; CLU_023279_0_0_1; -.
DR InParanoid; Q9DC23; -.
DR OMA; APTWRKF; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q9DC23; -.
DR TreeFam; TF105169; -.
DR BRENDA; 1.8.1.8; 3474.
DR BioGRID-ORCS; 66861; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Dnajc10; mouse.
DR EvolutionaryTrace; Q9DC23; -.
DR PRO; PR:Q9DC23; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DC23; protein.
DR Bgee; ENSMUSG00000027006; Expressed in prostate gland ventral lobe and 252 other tissues.
DR Genevisible; Q9DC23; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IMP:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IMP:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd03004; PDI_a_ERdj5_C; 3.
DR CDD; cd03003; PDI_a_ERdj5_N; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR021170; ERdj5.
DR InterPro; IPR035674; ERdj5_TRX_C.
DR InterPro; IPR035673; ERdj5_TRX_N.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00085; Thioredoxin; 4.
DR PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52833; SSF52833; 6.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Oxidoreductase; Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..793
FT /note="DnaJ homolog subfamily C member 10"
FT /id="PRO_0000281484"
FT DOMAIN 35..100
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 130..232
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 454..553
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 557..665
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 671..776
FT /note="Thioredoxin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 235..350
FT /note="Trxb 1"
FT REGION 348..463
FT /note="Trxb 2"
FT MOTIF 790..793
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..161
FT /note="Redox-active"
FT DISULFID 480..483
FT /note="Redox-active"
FT DISULFID 588..591
FT /note="Redox-active"
FT DISULFID 700..703
FT /note="Redox-active"
FT MUTAGEN 158
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-161; A-480; A-483; A-588; A-591; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 161
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-480; A-483; A-588; A-591; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 480
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-483; A-588; A-591; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 483
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-480; A-588; A-591; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 588
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-480; A-483; A-591; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 591
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-480; A-483; A-588; A-700
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 700
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-480; A-483; A-588; A-591
FT and A-703."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT MUTAGEN 703
FT /note="C->A: Abolishes disulfide reductase activity; when
FT associated with A-158; A-161; A-480; A-483; A-588; A-591
FT and A-700."
FT /evidence="ECO:0000269|PubMed:18653895,
FT ECO:0000269|PubMed:21329881"
FT CONFLICT 91
FT /note="D -> H (in Ref. 3; BAB23413)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="T -> A (in Ref. 2; AAQ14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> G (in Ref. 4; AAH33461)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="I -> T (in Ref. 4; AAH33461)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="E -> G (in Ref. 2; AAQ14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 651..652
FT /note="NG -> RP (in Ref. 2; AAQ14555)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="N -> NS (in Ref. 1; AAN73273)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="F -> FR (in Ref. 1; AAN73273)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="D -> M (in Ref. 2; AAQ14555)"
FT /evidence="ECO:0000305"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:3APQ"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3APQ"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:3APQ"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3APQ"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3APQ"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:3APQ"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:3APO"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:5AYL"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:5AYL"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 481..496
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 512..517
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 563..569
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 589..604
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 605..608
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:5AYK"
FT TURN 616..619
FT /evidence="ECO:0007829|PDB:5AYK"
FT HELIX 620..625
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 630..637
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:3APO"
FT HELIX 657..665
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:3APS"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:3APS"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:3APS"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:5AYK"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:3APS"
FT HELIX 701..717
FT /evidence="ECO:0007829|PDB:3APS"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:3APS"
FT STRAND 722..727
FT /evidence="ECO:0007829|PDB:3APS"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:3APS"
FT HELIX 732..737
FT /evidence="ECO:0007829|PDB:3APS"
FT STRAND 742..752
FT /evidence="ECO:0007829|PDB:3APS"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:3APS"
FT STRAND 757..763
FT /evidence="ECO:0007829|PDB:3APS"
FT HELIX 768..780
FT /evidence="ECO:0007829|PDB:3APS"
SQ SEQUENCE 793 AA; 90583 MW; 00C88EF3F5497BE1 CRC64;
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL
STGNFVNAIE TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANQLED
RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQPCL
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC
PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH
HSAEQILEFI EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY NGWNRDAYSL
RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC GPCQNFAPEF ELLARMIKGK
VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ YERAKKSIWE EQINSRDAKT IAALIYGKLE
TLQSQVKRNK DEL
