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Protein disulfide-isomerase A6 (EC 5.3.4.1) (Endoplasmic reticulum protein 5) (ER protein 5) (ERp5) (Protein disulfide isomerase P5) (Thioredoxin domain-containing protein 7)

 PDIA6_HUMAN             Reviewed;         440 AA.
Q15084; B3KY95; B5MCQ5; B7Z254; B7Z4M8; F8WA83; Q53RC7; Q6ZSH5;
Q99778;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
27-SEP-2017, entry version 193.
RecName: Full=Protein disulfide-isomerase A6;
EC=5.3.4.1 {ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936};
AltName: Full=Endoplasmic reticulum protein 5;
Short=ER protein 5;
Short=ERp5;
AltName: Full=Protein disulfide isomerase P5;
AltName: Full=Thioredoxin domain-containing protein 7;
Flags: Precursor;
Name=PDIA6; Synonyms=ERP5, P5, TXNDC7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=7590364; DOI=10.1016/0378-1119(95)00474-K;
Hayano T., Kikuchi M.;
"Cloning and sequencing of the cDNA encoding human P5.";
Gene 164:377-378(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5),
AND VARIANT ARG-214.
TISSUE=Amygdala, and Thalamus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-440 (ISOFORM 1), AND
VARIANT ARG-214.
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[7]
PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 20-38.
TISSUE=Leukemic T-cell;
PubMed=19892738; DOI=10.1073/pnas.0908958106;
Xu G., Shin S.B., Jaffrey S.R.;
"Global profiling of protease cleavage sites by chemoselective
labeling of protein N-termini.";
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
[8]
PROTEIN SEQUENCE OF 20-34, FUNCTION, ENZYME ACTIVITY, INTERACTION WITH
ITGB3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15466936; DOI=10.1182/blood-2004-02-0608;
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T.,
Authi K.S., Gibbins J.M.;
"A role for the thiol isomerase protein ERP5 in platelet function.";
Blood 105:1500-1507(2005).
[9]
PROTEIN SEQUENCE OF 103-138; 195-212; 217-231; 242-289; 314-328 AND
374-386.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[10]
FUNCTION, ENZYME ACTIVITY, AND MUTAGENESIS OF CYS-55; CYS-58; CYS-190
AND CYS-193.
PubMed=12204115; DOI=10.1093/oxfordjournals.jbchem.a003242;
Kikuchi M., Doi E., Tsujimoto I., Horibe T., Tsujimoto Y.;
"Functional analysis of human P5, a protein disulfide isomerase
homologue.";
J. Biochem. 132:451-455(2002).
[11]
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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
INTERACTION WITH MICA.
PubMed=17495932; DOI=10.1038/nature05768;
Kaiser B.K., Yim D., Chow I.-T., Gonzalez S., Dai Z., Mann H.H.,
Strong R.K., Groh V., Spies T.;
"Disulphide-isomerase-enabled shedding of tumour-associated NKG2D
ligands.";
Nature 447:482-486(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-428, AND
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).
[26]
PHOSPHORYLATION AT SER-156.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[27]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-19, AND
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).
[28]
STRUCTURE BY NMR OF 161-280.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the second thioredoxin-like domain of human
protein disulfide-isomerase A6.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: May function as a chaperone that inhibits aggregation of
misfolded proteins. Plays a role in platelet aggregation and
activation by agonists such as convulxin, collagen and thrombin.
{ECO:0000269|PubMed:12204115, ECO:0000269|PubMed:15466936}.
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins. {ECO:0000269|PubMed:12204115,
ECO:0000269|PubMed:15466936}.
-!- 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. Interacts with MICA on the surface of tumor
cells, leading to MICA disulfide bond reduction which is required
for its release from tumor cells. Interacts with ITGB3 following
platelet stimulation. {ECO:0000269|PubMed:15466936,
ECO:0000269|PubMed:17495932}.
-!- INTERACTION:
Q13162:PRDX4; NbExp=2; IntAct=EBI-1043087, EBI-2211957;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:15466936}. Cell membrane
{ECO:0000269|PubMed:15466936}. Melanosome
{ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV (PubMed:12643545).
{ECO:0000269|PubMed:12643545}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q15084-1; Sequence=Displayed;
Name=2;
IsoId=Q15084-2; Sequence=VSP_021803;
Name=3;
IsoId=Q15084-3; Sequence=VSP_054370;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q15084-4; Sequence=VSP_055173;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q15084-5; Sequence=VSP_055174;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in platelets (at protein level).
{ECO:0000269|PubMed:15466936}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
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EMBL; D49489; BAA08450.1; -; mRNA.
EMBL; AK127433; BAC86977.1; -; mRNA.
EMBL; AK131234; BAG54757.1; -; mRNA.
EMBL; AK289428; BAF82117.1; -; mRNA.
EMBL; AK294347; BAH11740.1; -; mRNA.
EMBL; AK297547; BAH12614.1; -; mRNA.
EMBL; AC092687; AAY24070.1; -; Genomic_DNA.
EMBL; CH471053; EAX00950.1; -; Genomic_DNA.
EMBL; BC001312; AAH01312.1; -; mRNA.
EMBL; U79278; AAB50217.1; -; mRNA.
CCDS; CCDS1675.1; -. [Q15084-1]
CCDS; CCDS62852.1; -. [Q15084-3]
CCDS; CCDS62853.1; -. [Q15084-4]
CCDS; CCDS62854.1; -. [Q15084-2]
CCDS; CCDS62855.1; -. [Q15084-5]
PIR; JC4369; JC4369.
RefSeq; NP_001269633.1; NM_001282704.1. [Q15084-2]
RefSeq; NP_001269634.1; NM_001282705.1. [Q15084-5]
RefSeq; NP_001269635.1; NM_001282706.1. [Q15084-4]
RefSeq; NP_001269636.1; NM_001282707.1. [Q15084-3]
RefSeq; NP_005733.1; NM_005742.3. [Q15084-1]
UniGene; Hs.212102; -.
UniGene; Hs.580464; -.
PDB; 1X5D; NMR; -; A=161-280.
PDB; 3VWW; X-ray; 1.93 A; A/B=25-140.
PDB; 3W8J; X-ray; 2.10 A; A/B=20-140.
PDB; 4EF0; X-ray; 1.50 A; A/B=27-140.
PDB; 4GWR; X-ray; 1.81 A; A/B=160-274.
PDBsum; 1X5D; -.
PDBsum; 3VWW; -.
PDBsum; 3W8J; -.
PDBsum; 4EF0; -.
PDBsum; 4GWR; -.
ProteinModelPortal; Q15084; -.
SMR; Q15084; -.
BioGrid; 115434; 98.
CORUM; Q15084; -.
IntAct; Q15084; 45.
MINT; MINT-3030897; -.
STRING; 9606.ENSP00000272227; -.
ChEMBL; CHEMBL2146308; -.
iPTMnet; Q15084; -.
PhosphoSitePlus; Q15084; -.
SwissPalm; Q15084; -.
DMDM; 2501205; -.
OGP; Q15084; -.
REPRODUCTION-2DPAGE; IPI00644989; -.
REPRODUCTION-2DPAGE; Q15084; -.
EPD; Q15084; -.
PaxDb; Q15084; -.
PeptideAtlas; Q15084; -.
PRIDE; Q15084; -.
DNASU; 10130; -.
Ensembl; ENST00000272227; ENSP00000272227; ENSG00000143870. [Q15084-1]
Ensembl; ENST00000381611; ENSP00000371024; ENSG00000143870. [Q15084-4]
Ensembl; ENST00000404371; ENSP00000385385; ENSG00000143870. [Q15084-2]
Ensembl; ENST00000404824; ENSP00000384459; ENSG00000143870. [Q15084-5]
Ensembl; ENST00000540494; ENSP00000438778; ENSG00000143870. [Q15084-3]
Ensembl; ENST00000617249; ENSP00000481892; ENSG00000143870. [Q15084-2]
GeneID; 10130; -.
KEGG; hsa:10130; -.
UCSC; uc002rau.5; human. [Q15084-1]
CTD; 10130; -.
DisGeNET; 10130; -.
EuPathDB; HostDB:ENSG00000143870.12; -.
GeneCards; PDIA6; -.
HGNC; HGNC:30168; PDIA6.
HPA; CAB034347; -.
HPA; HPA034652; -.
HPA; HPA034653; -.
MIM; 611099; gene.
neXtProt; NX_Q15084; -.
OpenTargets; ENSG00000143870; -.
PharmGKB; PA134977905; -.
eggNOG; KOG0191; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133723; -.
HOGENOM; HOG000012631; -.
HOVERGEN; HBG053548; -.
InParanoid; Q15084; -.
KO; K09584; -.
OMA; PHILDCD; -.
OrthoDB; EOG091G07Z0; -.
PhylomeDB; Q15084; -.
TreeFam; TF315231; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; PDIA6; human.
EvolutionaryTrace; Q15084; -.
GenomeRNAi; 10130; -.
PRO; PR:Q15084; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143870; -.
CleanEx; HS_PDIA6; -.
ExpressionAtlas; Q15084; baseline and differential.
Genevisible; Q15084; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISS:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0043277; P:apoptotic cell clearance; IBA:GO_Central.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 2.
SUPFAM; SSF52833; SSF52833; 3.
TIGRFAMs; TIGR01126; pdi_dom; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Chaperone;
Complete proteome; Direct protein sequencing; Disulfide bond;
Endoplasmic reticulum; Isomerase; Membrane; Phosphoprotein;
Polymorphism; Redox-active center; Reference proteome; Repeat; Signal.
SIGNAL 1 19 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:15466936,
ECO:0000269|PubMed:19892738}.
CHAIN 20 440 Protein disulfide-isomerase A6.
/FTId=PRO_0000034236.
DOMAIN 20 133 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 154 287 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 437 440 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
COMPBIAS 422 434 Asp/Glu-rich (acidic).
ACT_SITE 55 55 Nucleophile. {ECO:0000250}.
ACT_SITE 58 58 Nucleophile. {ECO:0000250}.
ACT_SITE 190 190 Nucleophile. {ECO:0000250}.
ACT_SITE 193 193 Nucleophile. {ECO:0000250}.
SITE 56 56 Contributes to redox potential value.
{ECO:0000250}.
SITE 57 57 Contributes to redox potential value.
{ECO:0000250}.
SITE 118 118 Lowers pKa of C-terminal Cys of first
active site. {ECO:0000250}.
SITE 191 191 Contributes to redox potential value.
{ECO:0000250}.
SITE 192 192 Contributes to redox potential value.
{ECO:0000250}.
SITE 256 256 Lowers pKa of C-terminal Cys of second
active site. {ECO:0000250}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 156 156 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
DISULFID 55 58 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 190 193 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 1 6 MALLVL -> MRRDLREKLVWVCRPLAPVEVPANISSDFQP
CSPTSPAHSLSRKSPIMYPSTTMANAP (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_021803.
VAR_SEQ 1 6 MALLVL -> MYPSTTMANAP (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055173.
VAR_SEQ 1 6 MALLVL -> MRIITAPASKVSRGSNELMILARRSDRGSPT
SPAHSLSRKSPIMYPSTTMANAP (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055174.
VAR_SEQ 1 5 MALLV -> MI (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054370.
VARIANT 214 214 K -> R (in dbSNP:rs4807).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9110174}.
/FTId=VAR_022152.
MUTAGEN 55 55 C->S: 50% decrease in enzyme activity;
when associated with S-58. Abolishes
enzyme activity; when associated with S-
58; S-190 and S-193.
{ECO:0000269|PubMed:12204115}.
MUTAGEN 58 58 C->S: 50% decrease in enzyme activity;
when associated with S-55. 90% decrease
in enzyme activity; when associated with
S-193. Abolishes enzyme activity; when
associated with S-55; S-190 and S-193.
{ECO:0000269|PubMed:12204115}.
MUTAGEN 190 190 C->S: 25% decrease in enzyme activity;
when associated with S-193. Abolishes
enzyme activity; when associated with S-
55; S-58 and S-193.
{ECO:0000269|PubMed:12204115}.
MUTAGEN 193 193 C->S: 90% decrease in enzyme activity;
when associated with S-58. 25% decrease
in enzyme activity; when associated with
S-190. Abolishes enzyme activity; when
associated with S-55; S-58 and S-190.
{ECO:0000269|PubMed:12204115}.
CONFLICT 64 64 E -> K (in Ref. 2; BAH12614).
{ECO:0000305}.
CONFLICT 187 187 A -> V (in Ref. 2; BAH12614).
{ECO:0000305}.
STRAND 28 30 {ECO:0000244|PDB:4EF0}.
TURN 32 34 {ECO:0000244|PDB:4EF0}.
HELIX 35 38 {ECO:0000244|PDB:4EF0}.
TURN 39 41 {ECO:0000244|PDB:4EF0}.
STRAND 46 51 {ECO:0000244|PDB:4EF0}.
HELIX 56 71 {ECO:0000244|PDB:4EF0}.
TURN 72 75 {ECO:0000244|PDB:4EF0}.
STRAND 76 82 {ECO:0000244|PDB:4EF0}.
TURN 83 85 {ECO:0000244|PDB:4EF0}.
HELIX 87 92 {ECO:0000244|PDB:4EF0}.
STRAND 100 104 {ECO:0000244|PDB:4EF0}.
STRAND 112 114 {ECO:0000244|PDB:3VWW}.
HELIX 120 139 {ECO:0000244|PDB:4EF0}.
STRAND 162 164 {ECO:0000244|PDB:4GWR}.
TURN 167 169 {ECO:0000244|PDB:4GWR}.
HELIX 170 173 {ECO:0000244|PDB:4GWR}.
TURN 174 176 {ECO:0000244|PDB:4GWR}.
STRAND 178 186 {ECO:0000244|PDB:4GWR}.
HELIX 191 211 {ECO:0000244|PDB:4GWR}.
STRAND 214 221 {ECO:0000244|PDB:4GWR}.
HELIX 222 224 {ECO:0000244|PDB:4GWR}.
HELIX 226 231 {ECO:0000244|PDB:4GWR}.
STRAND 236 243 {ECO:0000244|PDB:4GWR}.
STRAND 247 252 {ECO:0000244|PDB:1X5D}.
HELIX 258 271 {ECO:0000244|PDB:4GWR}.
SEQUENCE 440 AA; 48121 MW; 06895409F0265D7C CRC64;
MALLVLGLVS CTFFLAVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR
LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT IKIFGSNKNR PEDYQGGRTG
EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRSDSSSKK DVIELTDDSF DKNVLDSEDV
WMVEFYAPWC GHCKNLEPEW AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI
KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKRT CEEHQLCVVA
VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG IGGFGYPAMA
AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GAFPTIVERE PWDGRDGELP
VEDDIDLSDV ELDDLGKDEL


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