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Protein disulfide-isomerase A4 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72)

 PDIA4_HUMAN             Reviewed;         645 AA.
P13667; A8K4K6; Q549T6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
25-APR-2018, entry version 200.
RecName: Full=Protein disulfide-isomerase A4;
EC=5.3.4.1;
AltName: Full=Endoplasmic reticulum resident protein 70;
Short=ER protein 70;
Short=ERp70;
AltName: Full=Endoplasmic reticulum resident protein 72;
Short=ER protein 72;
Short=ERp-72;
Short=ERp72;
Flags: Precursor;
Name=PDIA4; Synonyms=ERP70, ERP72;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2549034;
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
"Human deoxycytidine kinase. Sequence of cDNA clones and analysis of
expression in cell lines with and without enzyme activity.";
J. Biol. Chem. 264:14762-14768(1989).
[2]
ERRATUM, AND SEQUENCE REVISION.
PubMed=2002068;
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
J. Biol. Chem. 266:5353-5353(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Muscle;
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).
[7]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 53-284.
PubMed=20600112; DOI=10.1016/j.jmb.2010.06.045;
Kozlov G., Azeroual S., Rosenauer A., Maeaettaenen P., Denisov A.Y.,
Thomas D.Y., Gehring K.;
"Structure of the catalytic a(0)a fragment of the protein disulfide
isomerase ERp72.";
J. Mol. Biol. 401:618-625(2010).
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX.
-!- INTERACTION:
Q76353:- (xeno); NbExp=3; IntAct=EBI-1054653, EBI-6248077;
P23284:PPIB; NbExp=3; IntAct=EBI-1054653, EBI-8771982;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:12643545}. Melanosome
{ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV
(PubMed:17081065). {ECO:0000269|PubMed:17081065}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a deoxycytidine kinase.
{ECO:0000305|PubMed:2549034}.
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EMBL; J05016; AAA58460.1; -; mRNA.
EMBL; AK290971; BAF83660.1; -; mRNA.
EMBL; AC093743; AAQ96863.1; -; Genomic_DNA.
EMBL; CH471146; EAW80065.1; -; Genomic_DNA.
EMBL; CH471146; EAW80066.1; -; Genomic_DNA.
EMBL; BC000425; AAH00425.1; -; mRNA.
EMBL; BC001928; AAH01928.1; -; mRNA.
EMBL; BC006344; AAH06344.1; -; mRNA.
EMBL; BC011754; AAH11754.1; -; mRNA.
CCDS; CCDS5893.1; -.
PIR; A23723; A23723.
RefSeq; NP_004902.1; NM_004911.4.
UniGene; Hs.93659; -.
PDB; 3IDV; X-ray; 1.95 A; A=53-284.
PDBsum; 3IDV; -.
ProteinModelPortal; P13667; -.
SMR; P13667; -.
BioGrid; 114966; 74.
IntAct; P13667; 41.
MINT; P13667; -.
STRING; 9606.ENSP00000286091; -.
iPTMnet; P13667; -.
PhosphoSitePlus; P13667; -.
SwissPalm; P13667; -.
BioMuta; PDIA4; -.
DMDM; 119530; -.
OGP; P13667; -.
REPRODUCTION-2DPAGE; IPI00009904; -.
EPD; P13667; -.
MaxQB; P13667; -.
PaxDb; P13667; -.
PeptideAtlas; P13667; -.
PRIDE; P13667; -.
DNASU; 9601; -.
Ensembl; ENST00000286091; ENSP00000286091; ENSG00000155660.
GeneID; 9601; -.
KEGG; hsa:9601; -.
UCSC; uc003wff.3; human.
CTD; 9601; -.
DisGeNET; 9601; -.
EuPathDB; HostDB:ENSG00000155660.10; -.
GeneCards; PDIA4; -.
HGNC; HGNC:30167; PDIA4.
HPA; CAB017368; -.
HPA; HPA006139; -.
HPA; HPA006140; -.
neXtProt; NX_P13667; -.
OpenTargets; ENSG00000155660; -.
PharmGKB; PA142671190; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
HOGENOM; HOG000162459; -.
HOVERGEN; HBG005920; -.
InParanoid; P13667; -.
KO; K09582; -.
OMA; YRAATQF; -.
OrthoDB; EOG091G05J9; -.
PhylomeDB; P13667; -.
TreeFam; TF106382; -.
BRENDA; 5.3.4.1; 2681.
ChiTaRS; PDIA4; human.
EvolutionaryTrace; P13667; -.
GenomeRNAi; 9601; -.
PRO; PR:P13667; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000155660; -.
CleanEx; HS_PDIA4; -.
ExpressionAtlas; P13667; baseline and differential.
Genevisible; P13667; HS.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0009306; P:protein secretion; TAS:ProtInc.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR017068; Protein_diS-isomerase_A4.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 3.
PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
SUPFAM; SSF52833; SSF52833; 5.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 3.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 3.
PROSITE; PS51352; THIOREDOXIN_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Isomerase; Polymorphism; Redox-active center; Reference proteome;
Repeat; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 645 Protein disulfide-isomerase A4.
/FTId=PRO_0000034229.
DOMAIN 21 169 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 158 301 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 505 636 Thioredoxin 3. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 642 645 Prevents secretion from ER.
COMPBIAS 39 55 Asp/Glu-rich (acidic).
MOD_RES 366 366 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
DISULFID 91 94 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 206 209 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 555 558 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VARIANT 173 173 T -> M (in dbSNP:rs2290971).
/FTId=VAR_052580.
CONFLICT 102 102 E -> G (in Ref. 3; BAF83660).
{ECO:0000305}.
STRAND 59 61 {ECO:0000244|PDB:3IDV}.
STRAND 64 66 {ECO:0000244|PDB:3IDV}.
TURN 69 71 {ECO:0000244|PDB:3IDV}.
HELIX 72 76 {ECO:0000244|PDB:3IDV}.
STRAND 80 87 {ECO:0000244|PDB:3IDV}.
HELIX 92 109 {ECO:0000244|PDB:3IDV}.
STRAND 111 113 {ECO:0000244|PDB:3IDV}.
STRAND 117 121 {ECO:0000244|PDB:3IDV}.
TURN 122 124 {ECO:0000244|PDB:3IDV}.
HELIX 126 131 {ECO:0000244|PDB:3IDV}.
STRAND 136 144 {ECO:0000244|PDB:3IDV}.
STRAND 147 150 {ECO:0000244|PDB:3IDV}.
HELIX 157 168 {ECO:0000244|PDB:3IDV}.
STRAND 178 181 {ECO:0000244|PDB:3IDV}.
TURN 184 186 {ECO:0000244|PDB:3IDV}.
HELIX 187 193 {ECO:0000244|PDB:3IDV}.
STRAND 195 202 {ECO:0000244|PDB:3IDV}.
HELIX 208 211 {ECO:0000244|PDB:3IDV}.
HELIX 213 224 {ECO:0000244|PDB:3IDV}.
STRAND 226 228 {ECO:0000244|PDB:3IDV}.
STRAND 232 236 {ECO:0000244|PDB:3IDV}.
TURN 237 239 {ECO:0000244|PDB:3IDV}.
HELIX 241 246 {ECO:0000244|PDB:3IDV}.
STRAND 251 259 {ECO:0000244|PDB:3IDV}.
STRAND 262 265 {ECO:0000244|PDB:3IDV}.
HELIX 272 282 {ECO:0000244|PDB:3IDV}.
SEQUENCE 645 AA; 72932 MW; 1919C2AE12CD2684 CRC64;
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL


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E1497c ELISA Chicken,Endoplasmic reticulum resident protein 57,ER protein 57,ERp57,ERP57,Gallus gallus,Glucose-regulated thiol oxidoreductase 58 kDa protein,GRP58,PDIA3,Protein disulfide-isomerase A3 96T
U1061m CLIA Cellular thyroid hormone-binding protein,Endoplasmic reticulum resident protein 59,ER protein 59,ERp59,Mouse,Mus musculus,P4hb,p55,PDI,Pdia1,Prolyl 4-hydroxylase subunit beta,Protein disulfide-is 96T
E1061m ELISA Cellular thyroid hormone-binding protein,Endoplasmic reticulum resident protein 59,ER protein 59,ERp59,Mouse,Mus musculus,P4hb,p55,PDI,Pdia1,Prolyl 4-hydroxylase subunit beta,Protein disulfide-i 96T
EIAAB30587 Homo sapiens,HSPC190,Human,PACAP,pERp1,Plasma cell-induced resident endoplasmic reticulum protein,Plasma cell-induced resident ER protein,Proapoptotic caspase adapter protein
EIAAB30586 Bos taurus,Bovine,PACAP,pERp1,Plasma cell-induced resident endoplasmic reticulum protein,Plasma cell-induced resident ER protein,Proapoptotic caspase adapter protein


 

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