Reviewed, UniProtKB/Swiss-Prot P07237 (PDIA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase
      Short name=PDI
    EC=5.3.4.1
Alternative name(s):
    Prolyl 4-hydroxylase subunit beta
    Cellular thyroid hormone-binding protein
    p55

Gene names

Name:	P4HB
Synonyms:	ERBA2L, PDI, PDIA1, PO4DB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Ref.15 Ref.17
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity By similarity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex.
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Cell membrane; Peripheral membrane protein Potential. Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources Probable. Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Miscellaneous	Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Redox-active center Repeat Signal
Molecular function	Chaperone Isomerase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro peptidyl-proline hydroxylation to 4-hydroxy-L-proline Inferred from direct assay. Source: MGI
Cellular component	ER-Golgi intermediate compartment Inferred from direct assay. Source: UniProtKB cell surface Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Non-traceable author statement. Source: UniProtKB extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	procollagen-proline 4-dioxygenase activity Ref.3 Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: IntAct protein disulfide isomerase activity Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CD2BP2	O95400	1	EBI-395883,EBI-768015
CUL2	Q13617	1	EBI-395883,EBI-456179
EIF4A2	Q14240	1	EBI-395883,EBI-73473
ELF3	P78545	1	EBI-395883,EBI-1057285
PUF60	Q9UHX1	1	EBI-395883,EBI-1053259
TAP1	Q03518	3	EBI-395883,EBI-747259
TRIP6	Q15654	1	EBI-395883,EBI-742327

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.6 Ref.7 Ref.8 Ref.9

Chain

18 – 508

491

Protein disulfide-isomerase

PRO_0000034195

Regions

Domain

18 – 134

117

Thioredoxin 1

Domain

349 – 475

127

Thioredoxin 2

Motif

505 – 508

4

Prevents secretion from ER

Sites

Active site

53

1

Nucleophile

Active site

56

1

Nucleophile

Active site

397

1

Nucleophile By similarity

Active site

400

1

Nucleophile By similarity

Site

54

1

Contributes to redox potential value

Site

55

1

Contributes to redox potential value

Site

120

1

Lowers pKa of C-terminal Cys of first active site

Site

398

1

Contributes to redox potential value By similarity

Site

399

1

Contributes to redox potential value By similarity

Site

461

1

Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond

53 ↔ 56

Redox-active Ref.28

Disulfide bond

397 ↔ 400

Redox-active By similarity

Experimental info

Sequence conflict

10 – 11

2

AV → PW in CAA28775. Ref.1

Sequence conflict

21

1

E → D AA sequence Ref.11

Sequence conflict

24

1

D → V AA sequence Ref.11

Sequence conflict

44 – 45

2

LL → PP in CAA28775. Ref.1

Sequence conflict

49

1

Y → H in CAA28775. Ref.1

Sequence conflict

141

1

P → R in AAA61169. Ref.2

Sequence conflict

360 – 362

3

LPE → RAG in AAA61169. Ref.2

Sequence conflict

372

1

L → P in AAA61169. Ref.2

Sequence conflict

439

1

S → G in CAA28775. Ref.1

Sequence conflict

444

1

K → G in CAA28775. Ref.1

Sequence conflict

460

1

E → Q in CAA30112. Ref.13

Sequence conflict

481

1

D → V in CAA28775. Ref.1

Secondary structure

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508

Helix Strand Turn

Details...

Beta strand

26 – 28

3

Turn

31 – 33

3

Helix

34 – 40

7

Beta strand

42 – 49

8

Helix

60 – 68

9

Turn

69 – 73

5

Beta strand

80 – 83

4

Turn

84 – 86

3

Helix

91 – 94

4

Beta strand

98 – 108

11

Beta strand

110 – 112

3

Helix

122 – 130

9

Beta strand

137 – 139

3

Helix

143 – 152

10

Beta strand

153 – 160

8

Turn

162 – 165

4

Helix

167 – 178

12

Beta strand

180 – 182

3

Beta strand

184 – 187

4

Helix

191 – 195

5

Beta strand

202 – 213

12

Helix

222 – 232

11

Helix

246 – 249

4

Beta strand

251 – 253

3

Beta strand

255 – 263

9

Beta strand

265 – 267

3

Helix

268 – 281

14

Turn

282 – 285

4

Beta strand

286 – 292

7

Turn

295 – 298

4

Helix

299 – 305

7

Beta strand

314 – 327

14

Helix

335 – 347

13

Beta strand

368 – 372

5

Turn

374 – 376

3

Helix

377 – 380

4

Beta strand

387 – 393

7

Helix

398 – 411

14

Helix

412 – 414

3

Beta strand

418 – 426

9

Turn

427 – 429

3

Beta strand

439 – 446

8

Helix

463 – 472

10

Sequences

	Sequence		Length	Mass (Da)
	P07237-1 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: 906CE6D9900B8FCE	FASTA	508	57,116
	10 20 30 40 50 60 MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA 70 80 90 100 110 120 PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR 130 140 150 160 170 180 EADDIVNWLK KRTGPAATTL PDGAAAESLV ESSEVAVIGF FKDVESDSAK QFLQAAEAID 190 200 210 220 230 240 DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF 250 260 270 280 290 300 TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR 310 320 330 340 350 360 ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL 370 380 390 400 410 420 PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI 430 440 450 460 470 480 VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD 490 500 DDDLEDLEEA EEPDMEEDDD QKAVKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene." Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L., Koivu J., Kivirikko K.I. EMBO J. 6:643-649(1987) [PubMed: 3034602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum." Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E., Merlino G.T., Pastan I. J. Biol. Chem. 262:11221-11227(1987) [PubMed: 3611107] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase." Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T. J. Biol. Chem. 263:16218-16224(1988) [PubMed: 2846539] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Lung and Skin.
[5]	"Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements." Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T. J. Biol. Chem. 267:11513-11519(1992) [PubMed: 1597478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[6]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-41. Tissue: Colon carcinoma.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-30. Tissue: Platelet.
[8]	Frutiger S., Hughes G.J. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 18-29. Tissue: Liver.
[9]	"Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis." Ward L.D., Hong J., Whitehead R.H., Simpson R.J. Electrophoresis 11:883-891(1990) [PubMed: 2079031] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-26.
[10]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-28. Tissue: Liver.
[11]	"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease." Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M. J. Biochem. 122:834-842(1997) [PubMed: 9399589] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-28.
[12]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 201-207; 223-230; 286-308 AND 402-409, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]	"Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)." Morris J.I., Varandani P.T. Biochim. Biophys. Acta 949:169-180(1988) [PubMed: 3342239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
[14]	"Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes." Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 11:528-536(1990) [PubMed: 1699755] [Abstract] Cited for: PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
[15]	"Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes." Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P., Miquelis R. J. Biol. Chem. 275:1920-1929(2000) [PubMed: 10636893] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding." Fenouillet E., Barbouche R., Courageot J., Miquelis R. J. Infect. Dis. 183:744-752(2001) [PubMed: 11181151] [Abstract] Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, SUBCELLULAR LOCATION.
[17]	"Is protein disulfide isomerase a redox-dependent molecular chaperone?" Lumb R.A., Bulleid N.J. EMBO J. 21:6763-6770(2002) [PubMed: 12485997] [Abstract] Cited for: FUNCTION.
[18]	"Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death." Ko H.S., Uehara T., Nomura Y. J. Biol. Chem. 277:35386-35392(2002) [PubMed: 12095988] [Abstract] Cited for: INTERACTION WITH UBQLN1.
[19]	"Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry." Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J. J. Biol. Chem. 277:50579-50588(2002) [PubMed: 12218051] [Abstract] Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[20]	"Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion." Barbouche R., Miquelis R., Jones I.M., Fenouillet E. J. Biol. Chem. 278:3131-3136(2003) [PubMed: 12218052] [Abstract] Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[21]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." 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. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]	"Protein disulfide isomerase." Wilkinson B., Gilbert H.F. Biochim. Biophys. Acta 1699:35-44(2004) [PubMed: 15158710] [Abstract] Cited for: REVIEW.
[23]	"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry." Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M., Weiss C.D., Broder C.C., Strebel K., Clouse K.A. Blood 103:1586-1594(2004) [PubMed: 14592831] [Abstract] Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[24]	"Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env." Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E. Mol. Pharmacol. 67:1111-1118(2005) [PubMed: 15644496] [Abstract] Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
[25]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[26]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[27]	"Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase." Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E. Protein Sci. 4:2587-2593(1995) [PubMed: 8580850] [Abstract] Cited for: STRUCTURE BY NMR OF 18-137.
[28]	"Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy." Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E. Biochemistry 35:7684-7691(1996) [PubMed: 8672469] [Abstract] Cited for: STRUCTURE BY NMR OF 18-137, DISULFIDE BOND.
[29]	"The structure in solution of the B domain of protein disulfide isomerase." Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M., Darby N.J. J. Biomol. NMR 13:357-368(1999) [PubMed: 10383197] [Abstract] Cited for: STRUCTURE BY NMR OF 136-245.
[30]	"The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 368-477.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05130 mRNA. Translation: CAA28775.1.
J02783 mRNA. Translation: AAA61169.1.
M22806 , M22803, M22804, M22805 Genomic DNA. Translation: AAC13652.1.
BC010859 mRNA. Translation: AAH10859.1.
BC029617 mRNA. Translation: AAH29617.1.
BC071892 mRNA. Translation: AAH71892.1.
S37207 Genomic DNA. Translation: AAB22262.2.
X07077 mRNA. Translation: CAA30112.1.

IPI

IPI00010796.

PIR

ISHUSS. A31913.

RefSeq

NP_000909.2.

UniGene

Hs.464336

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJX	NMR	-	A	136-245	[»]
1MEK	NMR	-	A	18-137	[»]
1X5C	NMR	-	A	368-475	[»]
2BJX	NMR	-	A	136-245	[»]
2K18	NMR	-	A	135-357	[»]
3BJ5	X-ray	2.20	A	230-368	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P07237. 20 interactions.

STRING

P07237.

PTM databases

PhosphoSite

P07237.

2-D gel databases

SWISS-2DPAGE

P07237.

Aarhus/Ghent-2DPAGE

8412. IEF.

Cornea-2DPAGE

P07237.

DOSAC-COBS-2DPAGE

P07237.

OGP

P07237.

REPRODUCTION-2DPAGE

IPI00010796.
P07237.

Siena-2DPAGE

P07237.

Proteomic databases

PeptideAtlas

P07237.

PRIDE

P07237.

Genome annotation databases

Ensembl

ENST00000331483; ENSP00000327801; ENSG00000185624; Homo sapiens. [Genome view]
ENST00000415593; ENSP00000388117; ENSG00000185624; Homo sapiens. [Genome view]
ENST00000436463; ENSP00000391471; ENSG00000185624; Homo sapiens. [Genome view]
ENST00000439918; ENSP00000388374; ENSG00000185624; Homo sapiens. [Genome view]
ENST00000450722; ENSP00000396494; ENSG00000185624; Homo sapiens. [Genome view]

GeneID

5034.

KEGG

hsa:5034.

NMPDR

fig|9606.3.peg.14582.

UCSC

uc002kbn.1. human.

Organism-specific databases

CTD

5034.

GeneCards

GC17M077394.

H-InvDB

HIX0014256.
HIX0048655.

HGNC

HGNC:8548. P4HB.

HPA

CAB012463.
HPA018884.

MIM

176790. gene.

PharmGKB

PA32876.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P07237.

HOVERGEN

P07237.

OMA

EYTAGRE.

Enzyme and pathway databases

BRENDA

5.3.4.1. 247.

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P07237.

Bgee

P07237.

CleanEx

HS_P4HB.

Genevestigator

P07237.

GermOnline

ENSG00000185624. Homo sapiens.

Family and domain databases

InterPro

IPR005788. Disulphide_isomerase.
IPR000886. ER_target_seq_motif.
IPR005792. Prot_disulphide_isomerase.
IPR017936. Thioredoxin-like.
IPR006662. Thioredoxin-like_subdom.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.

Pfam

PF00085. Thioredoxin. 2 hits.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

TIGRFAMs

TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

19398.

PMAP-CutDB

P07237.

SOURCE

Search...

Entry information

Entry name

PDIA1_HUMAN

Accession

Primary (citable) accession number: P07237
Secondary accession number(s): P30037 , P32079, Q15205, Q6LDE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 142 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.