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DnaJ homolog subfamily C member 10 (EC 1.8.4.-) (Endoplasmic reticulum DNA J domain-containing protein 5) (ER-resident protein ERdj5) (ERdj5) (Endoplasmic reticulum DnaJ-PDI fusion protein 1) (J domain-containing protein disulfide isomerase-like protein) (J domain-containing PDI-like protein) (JPDI)

 DJC10_MOUSE             Reviewed;         793 AA.
Q9DC23; A2ASA2; Q71S84; Q8CH78; Q8CIB0; Q99LV4;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-FEB-2018, entry version 132.
RecName: Full=DnaJ homolog subfamily C member 10;
EC=1.8.4.-;
AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 5;
Short=ER-resident protein ERdj5;
Short=ERdj5;
AltName: Full=Endoplasmic reticulum DnaJ-PDI fusion protein 1;
AltName: Full=J domain-containing protein disulfide isomerase-like protein;
Short=J domain-containing PDI-like protein;
Short=JPDI;
Flags: Precursor;
Name=Dnajc10; Synonyms=Erdj5, Jpdi;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12411443; DOI=10.1074/jbc.M206995200;
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T.,
Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P.,
Gustafsson J.-A., Sitia R., Spyrou G.;
"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ
and thioredoxin domains, is expressed in secretory cells or following
ER stress.";
J. Biol. Chem. 278:1059-1066(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Simmen T., Mezghrani A., Bertoli G., Sitia R.;
"ERDJPs, a novel family of ER chaperones.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N x C57BL/6J; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND
INTERACTION WITH HSPA5.
PubMed=12446677; DOI=10.1074/jbc.M208346200;
Hosoda A., Kimata Y., Tsuru A., Kohno K.;
"JPDI, a novel endoplasmic reticulum-resident protein containing both
a BiP-interacting J-domain and thioredoxin-like motifs.";
J. Biol. Chem. 278:2669-2676(2003).
[7]
FUNCTION, INTERACTION WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161;
CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
PubMed=18653895; DOI=10.1126/science.1159293;
Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.;
"ERdj5 is required as a disulfide reductase for degradation of
misfolded proteins in the ER.";
Science 321:569-572(2008).
[8]
DISRUPTION PHENOTYPE.
PubMed=19788412; DOI=10.1042/BJ20091269;
Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T.;
"Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein
quality control in the salivary gland.";
Biochem. J. 425:117-125(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-793, FUNCTION,
INTERACTION WITH EDEM1, AND MUTAGENESIS OF CYS-158; CYS-161; CYS-480;
CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
PubMed=21329881; DOI=10.1016/j.molcel.2011.01.021;
Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K.,
Matsumoto Y., Hoseki J., Nagata K., Inaba K.;
"Structural basis of an ERAD pathway mediated by the ER-resident
protein disulfide reductase ERdj5.";
Mol. Cell 41:432-444(2011).
-!- FUNCTION: Endoplasmic reticulum disulfide reductase involved both
in the correct folding of proteins and degradation of misfolded
proteins. Required for efficient folding of proteins in the
endoplasmic reticulum by catalyzing the removal of non-native
disulfide bonds formed during the folding of proteins, such as
LDLR. Also involved in endoplasmic reticulum-associated
degradation (ERAD) by reducing incorrect disulfide bonds in
misfolded glycoproteins recognized by EDEM1. Interaction with
HSPA5 is required its activity, not for the disulfide reductase
activity, but to facilitate the release of DNAJC10 from its
substrate. Promotes apoptotic signaling pathway in response to
endoplasmic reticulum stress. {ECO:0000269|PubMed:12411443,
ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
-!- SUBUNIT: Interacts with HSPA5 (via its J domain). Interacts with
EDEM1. {ECO:0000269|PubMed:12446677, ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138,
ECO:0000269|PubMed:12446677}.
-!- TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in secretory
tissues. Ubiquitous in fetal tissues and tumor tissues. Higher
expression in fetal tissues than in adult tissues. Expressed in
testis, pancreas, fetal thymus and fetal kidney. High expression
in heart, liver, kidney, and testis. Low expression in spleen and
skeletal muscle. {ECO:0000269|PubMed:12411443,
ECO:0000269|PubMed:12446677}.
-!- DOMAIN: Thioredoxin domains 3 and 4 are the primary reductase
domains. {ECO:0000269|PubMed:21329881}.
-!- DOMAIN: The thioredoxin-like regions Trxb 1 and 2 lack a redox-
active CXXC motif. {ECO:0000269|PubMed:21329881}.
-!- DISRUPTION PHENOTYPE: Mice are viable and healthy but show
enhanced endoplasmic reticulum stress response in the salivary
gland. {ECO:0000269|PubMed:19788412}.
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EMBL; AF255459; AAN73273.1; -; mRNA.
EMBL; AF314002; AAQ14555.1; -; mRNA.
EMBL; AK004617; BAB23413.1; -; mRNA.
EMBL; AL928587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002207; AAH02207.1; -; mRNA.
EMBL; BC033461; AAH33461.1; -; mRNA.
CCDS; CCDS38159.1; -.
RefSeq; NP_077143.2; NM_024181.2.
UniGene; Mm.21762; -.
PDB; 3APO; X-ray; 2.40 A; A=33-793.
PDB; 3APQ; X-ray; 1.84 A; A/B=34-242.
PDB; 3APS; X-ray; 1.90 A; A/B=668-789.
PDB; 5AYK; X-ray; 2.25 A; A=32-793.
PDB; 5AYL; X-ray; 2.40 A; A=32-793.
PDBsum; 3APO; -.
PDBsum; 3APQ; -.
PDBsum; 3APS; -.
PDBsum; 5AYK; -.
PDBsum; 5AYL; -.
ProteinModelPortal; Q9DC23; -.
SMR; Q9DC23; -.
BioGrid; 211769; 2.
IntAct; Q9DC23; 1.
STRING; 10090.ENSMUSP00000028392; -.
iPTMnet; Q9DC23; -.
PhosphoSitePlus; Q9DC23; -.
EPD; Q9DC23; -.
MaxQB; Q9DC23; -.
PaxDb; Q9DC23; -.
PeptideAtlas; Q9DC23; -.
PRIDE; Q9DC23; -.
Ensembl; ENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006.
GeneID; 66861; -.
KEGG; mmu:66861; -.
UCSC; uc008khj.1; mouse.
CTD; 54431; -.
MGI; MGI:1914111; Dnajc10.
eggNOG; ENOG410IMZF; Eukaryota.
eggNOG; KOG0191; Eukaryota.
eggNOG; COG0526; LUCA.
eggNOG; COG2214; LUCA.
GeneTree; ENSGT00860000133723; -.
HOGENOM; HOG000231882; -.
HOVERGEN; HBG057048; -.
InParanoid; Q9DC23; -.
KO; K09530; -.
OMA; RAYPTVK; -.
OrthoDB; EOG091G0BFU; -.
TreeFam; TF105169; -.
BRENDA; 1.8.1.8; 3474.
EvolutionaryTrace; Q9DC23; -.
PRO; PR:Q9DC23; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027006; -.
CleanEx; MM_DNAJC10; -.
Genevisible; Q9DC23; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IMP:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0032781; P:positive regulation of ATPase activity; IMP:UniProtKB.
GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
CDD; cd06257; DnaJ; 1.
CDD; cd03004; PDI_a_ERdj5_C; 3.
CDD; cd03003; PDI_a_ERdj5_N; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR021170; ERdj5.
InterPro; IPR035674; ERdj5_TRX_C.
InterPro; IPR035673; ERdj5_TRX_N.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00226; DnaJ; 1.
Pfam; PF00085; Thioredoxin; 4.
PIRSF; PIRSF037293; DnaJ_homolog_subfam-C; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF52833; SSF52833; 6.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Oxidoreductase;
Redox-active center; Reference proteome; Repeat; Signal.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 793 DnaJ homolog subfamily C member 10.
/FTId=PRO_0000281484.
DOMAIN 35 100 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
DOMAIN 130 232 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 454 553 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 557 665 Thioredoxin 3. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 671 776 Thioredoxin 4. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 235 350 Trxb 1.
REGION 348 463 Trxb 2.
MOTIF 790 793 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 158 161 Redox-active.
DISULFID 480 483 Redox-active.
DISULFID 588 591 Redox-active.
DISULFID 700 703 Redox-active.
MUTAGEN 158 158 C->A: Abolishes disulfide reductase
activity; when associated with A-161; A-
480; A-483; A-588; A-591; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 161 161 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
480; A-483; A-588; A-591; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 480 480 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-483; A-588; A-591; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 483 483 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-480; A-588; A-591; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 588 588 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-480; A-483; A-591; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 591 591 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-480; A-483; A-588; A-700 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 700 700 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-480; A-483; A-588; A-591 and A-
703. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
MUTAGEN 703 703 C->A: Abolishes disulfide reductase
activity; when associated with A-158; A-
161; A-480; A-483; A-588; A-591 and A-
700. {ECO:0000269|PubMed:18653895,
ECO:0000269|PubMed:21329881}.
CONFLICT 91 91 D -> H (in Ref. 3; BAB23413).
{ECO:0000305}.
CONFLICT 310 310 T -> A (in Ref. 2; AAQ14555).
{ECO:0000305}.
CONFLICT 324 324 E -> G (in Ref. 4; AAH33461).
{ECO:0000305}.
CONFLICT 433 433 I -> T (in Ref. 4; AAH33461).
{ECO:0000305}.
CONFLICT 538 538 E -> G (in Ref. 2; AAQ14555).
{ECO:0000305}.
CONFLICT 651 652 NG -> RP (in Ref. 2; AAQ14555).
{ECO:0000305}.
CONFLICT 654 654 N -> NS (in Ref. 1; AAN73273).
{ECO:0000305}.
CONFLICT 680 680 F -> FR (in Ref. 1; AAN73273).
{ECO:0000305}.
CONFLICT 767 767 D -> M (in Ref. 2; AAQ14555).
{ECO:0000305}.
HELIX 36 40 {ECO:0000244|PDB:3APQ}.
HELIX 48 62 {ECO:0000244|PDB:3APQ}.
HELIX 64 66 {ECO:0000244|PDB:3APQ}.
HELIX 73 87 {ECO:0000244|PDB:3APQ}.
HELIX 90 99 {ECO:0000244|PDB:3APQ}.
TURN 100 103 {ECO:0000244|PDB:3APQ}.
HELIX 115 120 {ECO:0000244|PDB:3APQ}.
STRAND 121 123 {ECO:0000244|PDB:3APQ}.
TURN 124 127 {ECO:0000244|PDB:3APQ}.
STRAND 131 133 {ECO:0000244|PDB:3APQ}.
HELIX 136 145 {ECO:0000244|PDB:3APQ}.
STRAND 149 154 {ECO:0000244|PDB:3APQ}.
HELIX 159 174 {ECO:0000244|PDB:3APQ}.
TURN 175 178 {ECO:0000244|PDB:5AYK}.
STRAND 179 185 {ECO:0000244|PDB:3APQ}.
TURN 186 188 {ECO:0000244|PDB:3APQ}.
HELIX 190 195 {ECO:0000244|PDB:3APQ}.
STRAND 200 207 {ECO:0000244|PDB:3APQ}.
STRAND 214 216 {ECO:0000244|PDB:5AYK}.
HELIX 222 234 {ECO:0000244|PDB:3APQ}.
STRAND 237 239 {ECO:0000244|PDB:5AYK}.
HELIX 242 255 {ECO:0000244|PDB:5AYK}.
STRAND 258 264 {ECO:0000244|PDB:5AYK}.
HELIX 273 282 {ECO:0000244|PDB:5AYK}.
TURN 283 286 {ECO:0000244|PDB:5AYK}.
STRAND 287 293 {ECO:0000244|PDB:5AYK}.
TURN 294 296 {ECO:0000244|PDB:5AYK}.
HELIX 298 301 {ECO:0000244|PDB:5AYK}.
TURN 302 304 {ECO:0000244|PDB:5AYK}.
STRAND 310 314 {ECO:0000244|PDB:5AYK}.
TURN 322 324 {ECO:0000244|PDB:3APO}.
TURN 325 327 {ECO:0000244|PDB:5AYK}.
STRAND 328 331 {ECO:0000244|PDB:5AYK}.
HELIX 336 346 {ECO:0000244|PDB:5AYK}.
STRAND 351 353 {ECO:0000244|PDB:5AYK}.
HELIX 355 361 {ECO:0000244|PDB:5AYK}.
TURN 362 364 {ECO:0000244|PDB:5AYK}.
STRAND 365 372 {ECO:0000244|PDB:5AYK}.
TURN 377 380 {ECO:0000244|PDB:5AYL}.
HELIX 382 386 {ECO:0000244|PDB:5AYK}.
HELIX 387 390 {ECO:0000244|PDB:5AYK}.
HELIX 392 394 {ECO:0000244|PDB:5AYK}.
STRAND 396 402 {ECO:0000244|PDB:5AYK}.
HELIX 403 405 {ECO:0000244|PDB:5AYK}.
HELIX 407 412 {ECO:0000244|PDB:5AYK}.
STRAND 417 423 {ECO:0000244|PDB:5AYK}.
STRAND 426 428 {ECO:0000244|PDB:5AYL}.
STRAND 431 433 {ECO:0000244|PDB:5AYK}.
HELIX 440 451 {ECO:0000244|PDB:5AYK}.
STRAND 455 457 {ECO:0000244|PDB:5AYK}.
HELIX 460 462 {ECO:0000244|PDB:5AYK}.
STRAND 471 476 {ECO:0000244|PDB:5AYK}.
HELIX 481 496 {ECO:0000244|PDB:5AYK}.
TURN 497 500 {ECO:0000244|PDB:5AYK}.
STRAND 502 507 {ECO:0000244|PDB:5AYK}.
TURN 508 510 {ECO:0000244|PDB:5AYK}.
HELIX 512 517 {ECO:0000244|PDB:5AYK}.
STRAND 525 530 {ECO:0000244|PDB:5AYK}.
STRAND 533 536 {ECO:0000244|PDB:5AYK}.
HELIX 543 554 {ECO:0000244|PDB:5AYK}.
STRAND 557 561 {ECO:0000244|PDB:5AYK}.
HELIX 563 569 {ECO:0000244|PDB:5AYK}.
TURN 570 572 {ECO:0000244|PDB:5AYK}.
STRAND 579 584 {ECO:0000244|PDB:5AYK}.
HELIX 589 604 {ECO:0000244|PDB:5AYK}.
TURN 605 608 {ECO:0000244|PDB:5AYK}.
STRAND 609 615 {ECO:0000244|PDB:5AYK}.
TURN 616 619 {ECO:0000244|PDB:5AYK}.
HELIX 620 625 {ECO:0000244|PDB:5AYK}.
STRAND 630 637 {ECO:0000244|PDB:5AYK}.
STRAND 641 643 {ECO:0000244|PDB:3APO}.
HELIX 657 665 {ECO:0000244|PDB:5AYK}.
STRAND 672 674 {ECO:0000244|PDB:3APS}.
HELIX 677 683 {ECO:0000244|PDB:3APS}.
TURN 684 686 {ECO:0000244|PDB:3APS}.
STRAND 687 689 {ECO:0000244|PDB:5AYK}.
STRAND 691 696 {ECO:0000244|PDB:3APS}.
HELIX 701 717 {ECO:0000244|PDB:3APS}.
TURN 718 720 {ECO:0000244|PDB:3APS}.
STRAND 722 727 {ECO:0000244|PDB:3APS}.
TURN 728 730 {ECO:0000244|PDB:3APS}.
HELIX 732 737 {ECO:0000244|PDB:3APS}.
STRAND 742 752 {ECO:0000244|PDB:3APS}.
HELIX 753 755 {ECO:0000244|PDB:3APS}.
STRAND 757 763 {ECO:0000244|PDB:3APS}.
HELIX 768 780 {ECO:0000244|PDB:3APS}.
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


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