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Database: UniProt
Entry: P07237
LinkDB: P07237
Original site: P07237 
ID   PDIA1_HUMAN             Reviewed;         508 AA.
AC   P07237; B2RDQ2; P30037; P32079; Q15205; Q6LDE5;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   02-JUN-2021, entry version 257.
DE   RecName: Full=Protein disulfide-isomerase;
DE            Short=PDI;
DE            EC=5.3.4.1;
DE   AltName: Full=Cellular thyroid hormone-binding protein;
DE   AltName: Full=Prolyl 4-hydroxylase subunit beta;
DE   AltName: Full=p55;
DE   Flags: Precursor;
GN   Name=P4HB; Synonyms=ERBA2L, PDI, PDIA1, PO4DB;
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].
RX   PubMed=3034602; DOI=10.1002/j.1460-2075.1987.tb04803.x;
RA   Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L.,
RA   Koivu J., Kivirikko K.I.;
RT   "Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This
RT   subunit and protein disulphide isomerase are products of the same gene.";
RL   EMBO J. 6:643-649(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3611107;
RA   Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E.,
RA   Merlino G.T., Pastan I.;
RT   "The nucleotide sequence of a human cellular thyroid hormone binding
RT   protein present in endoplasmic reticulum.";
RL   J. Biol. Chem. 262:11221-11227(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=2846539;
RA   Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T.;
RT   "Characterization of the human gene for a polypeptide that acts both as the
RT   beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase.";
RL   J. Biol. Chem. 263:16218-16224(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Synovium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, Lung, and Skin;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX   PubMed=1597478;
RA   Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T.;
RT   "Promoter of the gene for the multifunctional protein disulfide isomerase
RT   polypeptide. Functional significance of the six CCAAT boxes and other
RT   promoter elements.";
RL   J. Biol. Chem. 267:11513-11519(1992).
RN   [8]
RP   PROTEIN SEQUENCE OF 18-41.
RC   TISSUE=Colon carcinoma;
RX   PubMed=9150948; DOI=10.1002/elps.1150180344;
RA   Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT   "A two-dimensional gel database of human colon carcinoma proteins.";
RL   Electrophoresis 18:605-613(1997).
RN   [9]
RP   PROTEIN SEQUENCE OF 18-30.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [10]
RP   PROTEIN SEQUENCE OF 18-29.
RC   TISSUE=Liver;
RA   Frutiger S., Hughes G.J.;
RL   Submitted (FEB-1996) to UniProtKB.
RN   [11]
RP   PROTEIN SEQUENCE OF 18-26.
RX   PubMed=2079031; DOI=10.1002/elps.1150111019;
RA   Ward L.D., Hong J., Whitehead R.H., Simpson R.J.;
RT   "Development of a database of amino acid sequences for human colon
RT   carcinoma proteins separated by two-dimensional polyacrylamide gel
RT   electrophoresis.";
RL   Electrophoresis 11:883-891(1990).
RN   [12]
RP   PRELIMINARY PROTEIN SEQUENCE OF 19-28.
RC   TISSUE=Liver;
RX   PubMed=1286669; DOI=10.1002/elps.11501301201;
RA   Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA   Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA   Appel R.D., Hughes G.J.;
RT   "Human liver protein map: a reference database established by
RT   microsequencing and gel comparison.";
RL   Electrophoresis 13:992-1001(1992).
RN   [13]
RP   PROTEIN SEQUENCE OF 19-28.
RX   PubMed=9399589; DOI=10.1093/oxfordjournals.jbchem.a021830;
RA   Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
RT   "Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu
RT   (QEDL) motifs of microsomal ER-60 protease.";
RL   J. Biochem. 122:834-842(1997).
RN   [14]
RP   PROTEIN SEQUENCE OF 201-207; 223-230; 286-308 AND 402-409, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
RX   PubMed=3342239; DOI=10.1016/0167-4781(88)90080-2;
RA   Morris J.I., Varandani P.T.;
RT   "Characterization of a cDNA for human glutathione-insulin transhydrogenase
RT   (protein-disulfide isomerase/oxidoreductase).";
RL   Biochim. Biophys. Acta 949:169-180(1988).
RN   [16]
RP   PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
RX   PubMed=1699755; DOI=10.1002/elps.1150110703;
RA   Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
RA   Gesser B., Celis J.E., Vandekerckhove J.;
RT   "Two-dimensional gel electrophoresis, protein electroblotting and
RT   microsequencing: a direct link between proteins and genes.";
RL   Electrophoresis 11:528-536(1990).
RN   [17]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10636893; DOI=10.1074/jbc.275.3.1920;
RA   Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P.,
RA   Miquelis R.;
RT   "Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent
RT   thyroglobulin/PDI interactions determine a novel PDI function in the post-
RT   endoplasmic reticulum of thyrocytes.";
RL   J. Biol. Chem. 275:1920-1929(2000).
RN   [18]
RP   INTERACTION WITH ERO1B.
RX   PubMed=11707400; DOI=10.1093/emboj/20.22.6288;
RA   Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R.;
RT   "Manipulation of oxidative protein folding and PDI redox state in mammalian
RT   cells.";
RL   EMBO J. 20:6288-6296(2001).
RN   [19]
RP   REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11181151; DOI=10.1086/318823;
RA   Fenouillet E., Barbouche R., Courageot J., Miquelis R.;
RT   "The catalytic activity of protein disulfide isomerase is involved in human
RT   immunodeficiency virus envelope-mediated membrane fusion after CD4 cell
RT   binding.";
RL   J. Infect. Dis. 183:744-752(2001).
RN   [20]
RP   FUNCTION.
RX   PubMed=12485997; DOI=10.1093/emboj/cdf685;
RA   Lumb R.A., Bulleid N.J.;
RT   "Is protein disulfide isomerase a redox-dependent molecular chaperone?";
RL   EMBO J. 21:6763-6770(2002).
RN   [21]
RP   INTERACTION WITH UBQLN1.
RX   PubMed=12095988; DOI=10.1074/jbc.m203412200;
RA   Ko H.S., Uehara T., Nomura Y.;
RT   "Role of ubiquilin associated with protein-disulfide isomerase in the
RT   endoplasmic reticulum in stress-induced apoptotic cell death.";
RL   J. Biol. Chem. 277:35386-35392(2002).
RN   [22]
RP   REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
RX   PubMed=12218051; DOI=10.1074/jbc.m204547200;
RA   Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A.,
RA   Ryser H.J.;
RT   "Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide
RT   bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry.";
RL   J. Biol. Chem. 277:50579-50588(2002).
RN   [23]
RP   REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
RX   PubMed=12218052; DOI=10.1074/jbc.m205467200;
RA   Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
RT   "Protein-disulfide isomerase-mediated reduction of two disulfide bonds of
RT   HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for
RT   fusion.";
RL   J. Biol. Chem. 278:3131-3136(2003).
RN   [24]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=12643545; DOI=10.1021/pr025562r;
RA   Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA   Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA   Appella E.;
RT   "Proteomic analysis of early melanosomes: identification of novel
RT   melanosomal proteins.";
RL   J. Proteome Res. 2:69-79(2003).
RN   [25]
RP   REVIEW.
RX   PubMed=15158710; DOI=10.1016/j.bbapap.2004.02.017;
RA   Wilkinson B., Gilbert H.F.;
RT   "Protein disulfide isomerase.";
RL   Biochim. Biophys. Acta 1699:35-44(2004).
RN   [26]
RP   REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
RX   PubMed=14592831; DOI=10.1182/blood-2003-05-1390;
RA   Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M.,
RA   Weiss C.D., Broder C.C., Strebel K., Clouse K.A.;
RT   "Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1
RT   envelope-mediated T-cell fusion during viral entry.";
RL   Blood 103:1586-1594(2004).
RN   [27]
RP   REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
RX   PubMed=15644496; DOI=10.1124/mol.104.008276;
RA   Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.;
RT   "Glycosaminoglycans and protein disulfide isomerase-mediated reduction of
RT   HIV Env.";
RL   Mol. Pharmacol. 67:1111-1118(2005).
RN   [28]
RP   INTERACTION WITH MTTP.
RX   PubMed=16478722; DOI=10.1074/jbc.m512823200;
RA   Rava P., Ojakian G.K., Shelness G.S., Hussain M.M.;
RT   "Phospholipid transfer activity of microsomal triacylglycerol transfer
RT   protein is sufficient for the assembly and secretion of apolipoprotein B
RT   lipoproteins.";
RL   J. Biol. Chem. 281:11019-11027(2006).
RN   [29]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [30]
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   [31]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION AS RECEPTOR FOR LGALS9, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=21670307; DOI=10.1073/pnas.1017954108;
RA   Bi S., Hong P.W., Lee B., Baum L.G.;
RT   "Galectin-9 binding to cell surface protein disulfide isomerase regulates
RT   the redox environment to enhance T-cell migration and HIV entry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011).
RN   [32]
RP   INTERACTION WITH MTTP, AND SUBCELLULAR LOCATION.
RX   PubMed=23475612; DOI=10.1194/jlr.m031658;
RA   Khatun I., Walsh M.T., Hussain M.M.;
RT   "Loss of both phospholipid and triglyceride transfer activities of
RT   microsomal triglyceride transfer protein in abetalipoproteinemia.";
RL   J. Lipid Res. 54:1541-1549(2013).
RN   [33]
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   [34]
RP   PHOSPHORYLATION AT SER-357.
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   [35]
RP   INVOLVEMENT IN CLCRP1, VARIANT CLCRP1 CYS-393, AND CHARACTERIZATION OF
RP   VARIANT CLCRP1 CYS-393.
RX   PubMed=25683117; DOI=10.1016/j.ajhg.2014.12.027;
RA   Rauch F., Fahiminiya S., Majewski J., Carrot-Zhang J., Boudko S.,
RA   Glorieux F., Mort J.S., Baechinger H.P., Moffatt P.;
RT   "Cole-Carpenter syndrome is caused by a heterozygous missense mutation in
RT   P4HB.";
RL   Am. J. Hum. Genet. 96:425-431(2015).
RN   [36]
RP   INTERACTION WITH MTTP.
RX   PubMed=26224785; DOI=10.1161/circgenetics.115.001106;
RA   Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E.,
RA   Guenduez M., Tarugi P., Hussain M.M.;
RT   "A novel abetalipoproteinemia missense mutation highlights the importance
RT   of N-Terminal beta-barrel in microsomal triglyceride transfer protein
RT   function.";
RL   Circ. Cardiovasc. Genet. 8:677-687(2015).
RN   [37]
RP   CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, AND
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   [38]
RP   STRUCTURE BY NMR OF 18-137.
RX   PubMed=8580850; DOI=10.1002/pro.5560041216;
RA   Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E.;
RT   "Nuclear magnetic resonance characterization of the N-terminal thioredoxin-
RT   like domain of protein disulfide isomerase.";
RL   Protein Sci. 4:2587-2593(1995).
RN   [39]
RP   STRUCTURE BY NMR OF 18-137, AND DISULFIDE BOND.
RX   PubMed=8672469; DOI=10.1021/bi960335m;
RA   Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E.;
RT   "Structure determination of the N-terminal thioredoxin-like domain of
RT   protein disulfide isomerase using multidimensional heteronuclear 13C/15N
RT   NMR spectroscopy.";
RL   Biochemistry 35:7684-7691(1996).
RN   [40]
RP   STRUCTURE BY NMR OF 136-245.
RX   PubMed=10383197; DOI=10.1023/a:1008341820489;
RA   Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M.,
RA   Darby N.J.;
RT   "The structure in solution of the B domain of protein disulfide
RT   isomerase.";
RL   J. Biomol. NMR 13:357-368(1999).
RN   [41]
RP   STRUCTURE BY NMR OF 368-477.
RG   RIKEN structural genomics initiative (RSGI);
RT   "The solution structure of the second thioredoxin-like domain of human
RT   protein disulfide-isomerase.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: This multifunctional protein catalyzes the formation,
CC       breakage and rearrangement of disulfide bonds. At the cell surface,
CC       seems to act as a reductase that cleaves disulfide bonds of proteins
CC       attached to the cell. May therefore cause structural modifications of
CC       exofacial proteins. Inside the cell, seems to form/rearrange disulfide
CC       bonds of nascent proteins. At high concentrations, functions as a
CC       chaperone that inhibits aggregation of misfolded proteins. At low
CC       concentrations, facilitates aggregation (anti-chaperone activity). May
CC       be involved with other chaperones in the structural modification of the
CC       TG precursor in hormone biogenesis. Also acts a structural subunit of
CC       various enzymes such as prolyl 4-hydroxylase and microsomal
CC       triacylglycerol transfer protein MTTP. Receptor for LGALS9; the
CC       interaction retains P4HB at the cell surface of Th2 T helper cells,
CC       increasing disulfide reductase activity at the plasma membrane,
CC       altering the plasma membrane redox state and enhancing cell migration
CC       (PubMed:21670307). {ECO:0000269|PubMed:10636893,
CC       ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1;
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with the protein microsomal
CC       triglyceride transfer MTTP (PubMed:23475612, PubMed:26224785,
CC       PubMed:16478722). Homodimer. Monomers and homotetramers may also occur.
CC       Also constitutes the structural subunit of prolyl 4-hydroxylase and of
CC       the microsomal triacylglycerol transfer protein MTTP in mammalian
CC       cells. Stabilizes both enzymes and retain them in the ER without
CC       contributing to the catalytic activity (By similarity). Binds UBQLN1
CC       (PubMed:12095988). Interacts with ERO1B (PubMed:11707400). Binds to
CC       CD4, and upon HIV-1 binding to the cell membrane, is part of a
CC       P4HB/PDI-CD4-CXCR4-gp120 complex. {ECO:0000250,
CC       ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:12095988,
CC       ECO:0000269|PubMed:16478722, ECO:0000269|PubMed:23475612,
CC       ECO:0000269|PubMed:26224785}.
CC   -!- INTERACTION:
CC       P07237; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-395883, EBI-8464238;
CC       P07237; Q96RK4: BBS4; NbExp=3; IntAct=EBI-395883, EBI-1805814;
CC       P07237; O43521: BCL2L11; NbExp=3; IntAct=EBI-395883, EBI-526406;
CC       P07237; P17655: CAPN2; NbExp=3; IntAct=EBI-395883, EBI-1028956;
CC       P07237; Q8TAB7: CCDC26; NbExp=3; IntAct=EBI-395883, EBI-10271580;
CC       P07237; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-395883, EBI-742887;
CC       P07237; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-395883, EBI-11953200;
CC       P07237; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-395883, EBI-2321769;
CC       P07237; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-395883, EBI-741032;
CC       P07237; P09228: CST2; NbExp=3; IntAct=EBI-395883, EBI-8832659;
CC       P07237; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-395883, EBI-742054;
CC       P07237; Q96HE7: ERO1A; NbExp=2; IntAct=EBI-395883, EBI-2564539;
CC       P07237; Q8NEG0: FAM71C; NbExp=3; IntAct=EBI-395883, EBI-752049;
CC       P07237; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-395883, EBI-3957005;
CC       P07237; Q9ULW2: FZD10; NbExp=3; IntAct=EBI-395883, EBI-8803802;
CC       P07237; P62873: GNB1; NbExp=3; IntAct=EBI-395883, EBI-357130;
CC       P07237; P28799: GRN; NbExp=4; IntAct=EBI-395883, EBI-747754;
CC       P07237; Q8TCT9: HM13; NbExp=3; IntAct=EBI-395883, EBI-347472;
CC       P07237; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-395883, EBI-10973851;
CC       P07237; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-395883, EBI-739890;
CC       P07237; P02538: KRT6A; NbExp=3; IntAct=EBI-395883, EBI-702198;
CC       P07237; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-395883, EBI-11953334;
CC       P07237; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-395883, EBI-11953846;
CC       P07237; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-395883, EBI-10302392;
CC       P07237; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-395883, EBI-3958099;
CC       P07237; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-395883, EBI-11958364;
CC       P07237; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-395883, EBI-10245913;
CC       P07237; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-395883, EBI-10246750;
CC       P07237; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-395883, EBI-10246358;
CC       P07237; P80188: LCN2; NbExp=3; IntAct=EBI-395883, EBI-11911016;
CC       P07237; Q6PJG9: LRFN4; NbExp=3; IntAct=EBI-395883, EBI-7910762;
CC       P07237; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-395883, EBI-6979889;
CC       P07237; O94818-2: NOL4; NbExp=3; IntAct=EBI-395883, EBI-10190763;
CC       P07237; Q9P121-3: NTM; NbExp=3; IntAct=EBI-395883, EBI-12027160;
CC       P07237; Q14990: ODF1; NbExp=3; IntAct=EBI-395883, EBI-10234557;
CC       P07237; O15534: PER1; NbExp=3; IntAct=EBI-395883, EBI-2557276;
CC       P07237; Q63HM9: PLCXD3; NbExp=3; IntAct=EBI-395883, EBI-12105500;
CC       P07237; O00444: PLK4; NbExp=3; IntAct=EBI-395883, EBI-746202;
CC       P07237; Q13162: PRDX4; NbExp=2; IntAct=EBI-395883, EBI-2211957;
CC       P07237; Q09028: RBBP4; NbExp=3; IntAct=EBI-395883, EBI-620823;
CC       P07237; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-395883, EBI-346595;
CC       P07237; Q86WV1-2: SKAP1; NbExp=3; IntAct=EBI-395883, EBI-11995314;
CC       P07237; Q8WUG5: SLC22A17; NbExp=3; IntAct=EBI-395883, EBI-11722858;
CC       P07237; Q03518: TAP1; NbExp=4; IntAct=EBI-395883, EBI-747259;
CC       P07237; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-395883, EBI-12833746;
CC       P07237; P01137: TGFB1; NbExp=3; IntAct=EBI-395883, EBI-779636;
CC       P07237; Q9UC07-2: ZNF69; NbExp=3; IntAct=EBI-395883, EBI-12310821;
CC       P07237; Q2GL86: APH_0248; Xeno; NbExp=3; IntAct=EBI-395883, EBI-26435798;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:23475612}. Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:23475612}. Melanosome
CC       {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cell
CC       membrane {ECO:0000269|PubMed:21670307}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be
CC       also secreted or associated with the plasma membrane, where it
CC       undergoes constant shedding and replacement from intracellular sources
CC       (Probable). Localizes near CD4-enriched regions on lymphoid cell
CC       surfaces (PubMed:11181151). Identified by mass spectrometry in
CC       melanosome fractions from stage I to stage IV (PubMed:10636893).
CC       Colocalizes with MTTP in the endoplasmic reticulum (PubMed:23475612).
CC       {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:11181151,
CC       ECO:0000269|PubMed:23475612, ECO:0000305}.
CC   -!- DISEASE: Cole-Carpenter syndrome 1 (CLCRP1) [MIM:112240]: A form of
CC       Cole-Carpenter syndrome, a disorder characterized by features of
CC       osteogenesis imperfecta such as bone deformities and severe bone
CC       fragility with frequent fractures, in association with
CC       craniosynostosis, ocular proptosis, hydrocephalus, growth failure and
CC       distinctive facial features. Craniofacial findings include marked
CC       frontal bossing, midface hypoplasia, and micrognathia. Despite the
CC       craniosynostosis and hydrocephalus, intellectual development is normal.
CC       CLCRP1 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:25683117}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Reduces and may activate fusogenic properties of HIV-1
CC       gp120 surface protein, thereby enabling HIV-1 entry into the cell.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; X05130; CAA28775.1; -; mRNA.
DR   EMBL; J02783; AAA61169.1; -; mRNA.
DR   EMBL; M22806; AAC13652.1; -; Genomic_DNA.
DR   EMBL; M22803; AAC13652.1; JOINED; Genomic_DNA.
DR   EMBL; M22804; AAC13652.1; JOINED; Genomic_DNA.
DR   EMBL; M22805; AAC13652.1; JOINED; Genomic_DNA.
DR   EMBL; AK315631; BAG37999.1; -; mRNA.
DR   EMBL; CH471099; EAW89690.1; -; Genomic_DNA.
DR   EMBL; BC010859; AAH10859.1; -; mRNA.
DR   EMBL; BC029617; AAH29617.1; -; mRNA.
DR   EMBL; BC071892; AAH71892.1; -; mRNA.
DR   EMBL; S37207; AAB22262.2; -; Genomic_DNA.
DR   EMBL; X07077; CAA30112.1; -; mRNA.
DR   CCDS; CCDS11787.1; -.
DR   PIR; A31913; ISHUSS.
DR   RefSeq; NP_000909.2; NM_000918.3.
DR   PDB; 1BJX; NMR; -; A=136-245.
DR   PDB; 1MEK; NMR; -; A=18-137.
DR   PDB; 1X5C; NMR; -; A=368-475.
DR   PDB; 2BJX; NMR; -; A=136-245.
DR   PDB; 2K18; NMR; -; A=135-357.
DR   PDB; 3BJ5; X-ray; 2.20 A; A=230-368.
DR   PDB; 3UEM; X-ray; 2.29 A; A=137-479.
DR   PDB; 4EKZ; X-ray; 2.51 A; A=18-479.
DR   PDB; 4EL1; X-ray; 2.88 A; A/B=18-479.
DR   PDB; 4JU5; X-ray; 2.28 A; A/B=135-367.
DR   PDB; 6I7S; X-ray; 2.50 A; A/B=18-508.
DR   PDBsum; 1BJX; -.
DR   PDBsum; 1MEK; -.
DR   PDBsum; 1X5C; -.
DR   PDBsum; 2BJX; -.
DR   PDBsum; 2K18; -.
DR   PDBsum; 3BJ5; -.
DR   PDBsum; 3UEM; -.
DR   PDBsum; 4EKZ; -.
DR   PDBsum; 4EL1; -.
DR   PDBsum; 4JU5; -.
DR   PDBsum; 6I7S; -.
DR   BMRB; P07237; -.
DR   SMR; P07237; -.
DR   BioGRID; 111073; 275.
DR   CORUM; P07237; -.
DR   DIP; DIP-32979N; -.
DR   IntAct; P07237; 173.
DR   MINT; P07237; -.
DR   STRING; 9606.ENSP00000327801; -.
DR   BindingDB; P07237; -.
DR   ChEMBL; CHEMBL5422; -.
DR   DrugBank; DB11638; Artenimol.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB03615; Ribostamycin.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   iPTMnet; P07237; -.
DR   MetOSite; P07237; -.
DR   PhosphoSitePlus; P07237; -.
DR   SwissPalm; P07237; -.
DR   BioMuta; P4HB; -.
DR   DMDM; 2507460; -.
DR   DOSAC-COBS-2DPAGE; P07237; -.
DR   OGP; P07237; -.
DR   REPRODUCTION-2DPAGE; IPI00010796; -.
DR   REPRODUCTION-2DPAGE; P07237; -.
DR   SWISS-2DPAGE; P07237; -.
DR   EPD; P07237; -.
DR   jPOST; P07237; -.
DR   MassIVE; P07237; -.
DR   MaxQB; P07237; -.
DR   PaxDb; P07237; -.
DR   PeptideAtlas; P07237; -.
DR   PRIDE; P07237; -.
DR   ProteomicsDB; 51976; -.
DR   TopDownProteomics; P07237; -.
DR   Antibodypedia; 3250; 544 antibodies.
DR   DNASU; 5034; -.
DR   Ensembl; ENST00000331483; ENSP00000327801; ENSG00000185624.
DR   GeneID; 5034; -.
DR   KEGG; hsa:5034; -.
DR   UCSC; uc002kbn.2; human.
DR   CTD; 5034; -.
DR   DisGeNET; 5034; -.
DR   GeneCards; P4HB; -.
DR   HGNC; HGNC:8548; P4HB.
DR   HPA; ENSG00000185624; Tissue enhanced (liver, pancreas).
DR   MalaCards; P4HB; -.
DR   MIM; 112240; phenotype.
DR   MIM; 176790; gene.
DR   neXtProt; NX_P07237; -.
DR   OpenTargets; ENSG00000185624; -.
DR   Orphanet; 2050; Cole-Carpenter syndrome.
DR   PharmGKB; PA32876; -.
DR   VEuPathDB; HostDB:ENSG00000185624.14; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00940000157351; -.
DR   InParanoid; P07237; -.
DR   OMA; HTRIFEF; -.
DR   OrthoDB; 462118at2759; -.
DR   PhylomeDB; P07237; -.
DR   TreeFam; TF106381; -.
DR   BioCyc; MetaCyc:HS06845-MONOMER; -.
DR   BRENDA; 5.3.4.1; 2681.
DR   PathwayCommons; P07237; -.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
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-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-8866423; VLDL assembly.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-HSA-8963888; Chylomicron assembly.
DR   Reactome; R-HSA-9020591; Interleukin-12 signaling.
DR   Reactome; R-HSA-9020933; Interleukin-23 signaling.
DR   BioGRID-ORCS; 5034; 21 hits in 1006 CRISPR screens.
DR   ChiTaRS; P4HB; human.
DR   EvolutionaryTrace; P07237; -.
DR   GeneWiki; P4HB; -.
DR   GenomeRNAi; 5034; -.
DR   Pharos; P07237; Tbio.
DR   PRO; PR:P07237; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P07237; protein.
DR   Bgee; ENSG00000185624; Expressed in stromal cell of endometrium and 245 other tissues.
DR   ExpressionAtlas; P07237; baseline and differential.
DR   Genevisible; P07237; HS.
DR   GO; GO:0005856; C:cytoskeleton; IDA:ARUK-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:ARUK-UCL.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
DR   GO; GO:0003779; F:actin binding; IPI:ARUK-UCL.
DR   GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR   GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; TAS:ProtInc.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:FlyBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0016972; F:thiol oxidase activity; IDA:FlyBase.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR   GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
DR   GO; GO:0030199; P:collagen fibril organization; TAS:Reactome.
DR   GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038155; P:interleukin-23-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:ARUK-UCL.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:ARUK-UCL.
DR   GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
DR   GO; GO:0034379; P:very-low-density lipoprotein particle assembly; TAS:Reactome.
DR   Gene3D; 3.40.30.10; -; 4.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   SUPFAM; SSF52833; SSF52833; 4.
DR   TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Chaperone; Craniosynostosis;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   Endoplasmic reticulum; Isomerase; Membrane; Osteogenesis imperfecta;
KW   Phosphoprotein; Redox-active center; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:2079031, ECO:0000269|PubMed:9150948,
FT                   ECO:0000269|Ref.10, ECO:0007744|PubMed:25944712"
FT   CHAIN           18..508
FT                   /note="Protein disulfide-isomerase"
FT                   /id="PRO_0000034195"
FT   DOMAIN          18..134
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          349..475
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          471..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           505..508
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        476..508
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT   ACT_SITE        56
FT                   /note="Nucleophile"
FT   ACT_SITE        397
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        400
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            54
FT                   /note="Contributes to redox potential value"
FT   SITE            55
FT                   /note="Contributes to redox potential value"
FT   SITE            120
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT   SITE            398
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            399
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            461
FT                   /note="Lowers pKa of C-terminal Cys of second active site"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         200
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09103"
FT   MOD_RES         222
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09103"
FT   MOD_RES         271
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09103"
FT   MOD_RES         357
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   DISULFID        53..56
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT                   ECO:0000269|PubMed:8672469"
FT   DISULFID        397..400
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VARIANT         393
FT                   /note="Y -> C (in CLCRP1; impairs ability to act as a
FT                   disulfide isomerase enzyme; dbSNP:rs786204843)"
FT                   /evidence="ECO:0000269|PubMed:25683117"
FT                   /id="VAR_073440"
FT   CONFLICT        10..11
FT                   /note="AV -> PW (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="E -> D (in Ref. 13; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24
FT                   /note="D -> V (in Ref. 13; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44..45
FT                   /note="LL -> PP (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="Y -> H (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="P -> R (in Ref. 2; AAA61169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360..362
FT                   /note="LPE -> RAG (in Ref. 2; AAA61169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="L -> P (in Ref. 2; AAA61169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="S -> G (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="K -> G (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="E -> Q (in Ref. 15; CAA30112)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="D -> V (in Ref. 1; CAA28775)"
FT                   /evidence="ECO:0000305"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:4EKZ"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:4EKZ"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:4EL1"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   HELIX           54..71
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   STRAND          76..83
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   HELIX           88..93
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   STRAND          98..105
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:4EL1"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:4EL1"
FT   HELIX           122..133
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   HELIX           143..151
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:6I7S"
FT   HELIX           167..178
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          180..182
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   HELIX           190..195
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          199..209
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   HELIX           222..232
FT                   /evidence="ECO:0007829|PDB:4JU5"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           245..249
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          250..252
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          255..260
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           268..280
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   TURN            281..285
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           299..304
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          313..319
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:4EKZ"
FT   HELIX           336..347
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   HELIX           362..364
FT                   /evidence="ECO:0007829|PDB:3BJ5"
FT   STRAND          367..372
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   TURN            374..376
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   HELIX           377..381
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   STRAND          387..393
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   HELIX           398..413
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   TURN            414..416
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   STRAND          418..426
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   TURN            427..429
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   STRAND          439..446
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   STRAND          448..451
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   HELIX           463..470
FT                   /evidence="ECO:0007829|PDB:3UEM"
FT   TURN            471..473
FT                   /evidence="ECO:0007829|PDB:3UEM"
SQ   SEQUENCE   508 AA;  57116 MW;  906CE6D9900B8FCE CRC64;
     MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA
     PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR
     EADDIVNWLK KRTGPAATTL PDGAAAESLV ESSEVAVIGF FKDVESDSAK QFLQAAEAID
     DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF
     TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR
     ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL
     PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI
     VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD
     DDDLEDLEEA EEPDMEEDDD QKAVKDEL
//
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