Reviewed, UniProtKB/Swiss-Prot P08003 (PDIA4_MOUSE)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase A4
    EC=5.3.4.1
Alternative name(s):
    Protein ERp-72
      Short name=ERp72

Gene names

Name:	Pdia4
Synonyms:	Cai, Erp72

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	638 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)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.
Subcellular location	Endoplasmic reticulum lumen. Melanosome By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 3 thioredoxin domains.
Sequence caution	The sequence CAA68777.1 differs from that shown. Reason: Frameshift at position 544.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Acetylation Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein disulfide isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 638

618

Protein disulfide-isomerase A4

PRO_0000034230

Regions

Domain

21 – 162

142

Thioredoxin 1

Domain

162 – 294

133

Thioredoxin 2

Domain

498 – 629

132

Thioredoxin 3

Motif

635 – 638

4

Prevents secretion from ER

Compositional bias

39 – 50

12

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

359

1

N6-acetyllysine By similarity

Glycosylation

36

1

N-linked (GlcNAc...) Potential

Disulfide bond

84 ↔ 87

Redox-active By similarity

Disulfide bond

199 ↔ 202

Redox-active By similarity

Disulfide bond

548 ↔ 551

Redox-active By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

638

Helix Strand Turn

Details...

Beta strand

152 – 154

3

Turn

158 – 160

3

Turn

162 – 164

3

Helix

165 – 167

3

Beta strand

169 – 176

8

Beta strand

465 – 468

4

Turn

471 – 473

3

Helix

474 – 478

5

Beta strand

483 – 489

7

Sequences

	Sequence		Length	Mass (Da)
	P08003-1 [UniParc]. Last modified May 1, 1991. Version 2. Checksum: FA06D250D06A27BB	FASTA	638	71,973
	10 20 30 40 50 60 MKLRKAWLLV LLLALTQLLA AASAGDAQED TSDTENATEE EEEEDDDDLE VKEENGVWVL 70 80 90 100 110 120 NDGNFDNFVA DKDTVLLEFY APWCGHCKQF APEYEKIAST LKDNDPPIAV AKIDATSASM 130 140 150 160 170 180 LASKFDVSGY PTIKILKKGQ AVDYDGSRTQ EEIVAKVREV SQPDWTPPPE VTLSLTKDNF 190 200 210 220 230 240 DDVVNNADII LVEFYAPWCG HCKKLAPEYE KAAKELSKRS PPIPLAKVDA TEQTDLAKRF 250 260 270 280 290 300 DVSGYPTLKI FRKGRPFDYN GPREKYGIVD YMIEQSGPPS KEILTLKQVQ EFLKDGDDVV 310 320 330 340 350 360 IIGLFQGDGD PAYLQYQDAA NNLREDYKFH HTFSPEIAKF LKVSLGKLVL THPEKFQSKY 370 380 390 400 410 420 EPRFHVMDVQ GSTEASAIKD YVVKHALPLV GHRKTSNDAK RYSKRPLVVV YYSVDFSFDY 430 440 450 460 470 480 RAATQFWRNK VLEVAKDFPE YTFAIADEED YATEVKDLGL SESGEDVNAA ILDESGKKFA 490 500 510 520 530 540 MEPEEFDSDT LREFVTAFKK GKLKPVIKSQ PVPKNNKGPV KVVVGKTFDA IVMDPKKDVL 550 560 570 580 590 600 IEFYAPWCGH CKQLEPIYTS LGKKYKGQKD LVIAKMDATA NDITNDQYKV EGFPTIYFAP 610 620 630 SGDKKNPIKF EGGNRDLEHL SKFIDEHATK RSRTKEEL

References

[1]	"ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase." Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M. J. Biol. Chem. 265:1094-1101(1990) [PubMed: 2295602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"An mRNA sharing sequences with a variant granulocyte-macrophage colony stimulating factor cDNA clone." Gough N.M., King J.A., Dunn A.R. Nucleic Acids Res. 15:10584-10584(1987) [PubMed: 3320970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638. Strain: BALB/c. Tissue: T-cell.
[3]	"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[4]	"The solution structure of thioredoxin domains of mouse protein disulfide-isomerase A4." RIKEN structural genomics initiative (RSGI) Submitted (SEP-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 46-277 AND 516-638.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05186 mRNA. Translation: AAA39907.1.
Y00884 mRNA. Translation: CAA68777.1. Frameshift.

IPI

IPI00271951.

PIR

ISMSER. B34930.
S06318.

UniGene

Mm.2442

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DJ1	NMR	-	A	46-172	[»]
2DJ2	NMR	-	A	171-277	[»]
2DJ3	NMR	-	A	518-638	[»]

SMR

P08003. Positions 53-219, 170-632.

ModBase

Search...

Protein-protein interaction databases

STRING

P08003.

PTM databases

PhosphoSite

P08003.

Proteomic databases

PRIDE

P08003.

Genome annotation databases

Ensembl

ENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823; Mus musculus. [Genome view]

Organism-specific databases

MGI

MGI:104864. Pdia4.

Phylogenomic databases

eggNOG

roNOG09466.

HOVERGEN

P08003.

InParanoid

P08003.

Enzyme and pathway databases

BRENDA

5.3.4.1. 244.

Gene expression databases

ArrayExpress

P08003.

Bgee

P08003.

CleanEx

MM_PDIA4.

Genevestigator

P08003.

GermOnline

ENSMUSG00000025823. Mus musculus.

Family and domain databases

InterPro

IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR006662. Thioredoxin-like_subdom.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.

Pfam

PF00085. Thioredoxin. 3 hits.
[Graphical view]

PIRSF

PIRSF036862. Disulphide_isom_A4. 1 hit.

PRINTS

PR00421. THIOREDOXIN.

TIGRFAMs

TIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

PDIA4_MOUSE

Accession

Primary (citable) accession number: P08003
Secondary accession number(s): P15841

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	May 1, 1991
Last modified:	February 9, 2010
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)