P08003 (PDIA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase A4
EC=5.3.4.1

Alternative name(s):
Endoplasmic reticulum resident protein 72
Short name=ER protein 72
Short name=ERp-72
Short name=ERp72

Gene names

Name:	Pdia4
Synonyms:	Cai, Erp72

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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 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.
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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro protein folding Inferred from electronic annotation. Source: GOC
Cellular_component	cell surface Inferred from direct assay PubMed 19995400. Source: MGI endoplasmic reticulum Inferred from direct assay PubMed 9493907. Source: MGI endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
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

Experimental info

Sequence conflict

28

1

H → Q in AAA39907. Ref.1

Sequence conflict

28

1

H → Q in BAE27045. Ref.2

Sequence conflict

28

1

H → Q in AAI41079. Ref.3

Sequence conflict

39

1

E → EEEE in BAC25863. Ref.2

Sequence conflict

39

1

E → EEEE in BAE41134. Ref.2

Sequence conflict

39

1

E → EEEE in BAE36446. Ref.2

Sequence conflict

39

1

E → EEEE in BAE29664. Ref.2

Sequence conflict

468

1

N → S in BAC25863. Ref.2

Secondary structure

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638

Helix Strand Turn

Details...

Beta strand

52 – 54

3

Beta strand

57 – 59

3

Turn

62 – 64

3

Helix

65 – 69

5

Beta strand

73 – 79

7

Helix

85 – 88

4

Helix

91 – 102

12

Beta strand

103 – 106

4

Beta strand

109 – 113

5

Turn

115 – 117

3

Helix

119 – 124

6

Beta strand

129 – 137

9

Beta strand

140 – 143

4

Helix

150 – 161

12

Beta strand

162 – 164

3

Beta strand

171 – 173

3

Turn

177 – 179

3

Turn

181 – 183

3

Helix

184 – 186

3

Beta strand

188 – 195

8

Helix

200 – 218

19

Beta strand

219 – 221

3

Beta strand

225 – 229

5

Turn

230 – 232

3

Helix

234 – 239

6

Beta strand

244 – 254

11

Beta strand

256 – 258

3

Helix

265 – 277

13

Beta strand

519 – 522

4

Turn

525 – 527

3

Helix

528 – 532

5

Beta strand

537 – 543

7

Helix

550 – 565

16

Beta strand

568 – 576

9

Turn

578 – 580

3

Beta strand

591 – 599

9

Helix

619 – 627

9

Beta strand

628 – 630

3

Sequences

	Sequence		Length	Mass (Da)
	P08003 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 2DDE2CE80BD77F6E	FASTA	638	71,982
	10 20 30 40 50 60 MKLRKAWLLV LLLALTQLLA AASAGDAHED 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

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Amnion, Bone marrow, Head, Ovary and Uterus.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain and Embryonic germ cell.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638. Strain: BALB/c. Tissue: T-cell.
[5]	"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] [Europe PMC] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[6]	"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.
AK028292 mRNA. Translation: BAC25863.1.
AK146288 mRNA. Translation: BAE27045.1.
AK150566 mRNA. Translation: BAE29664.1.
AK161534 mRNA. Translation: BAE36446.1.
AK169387 mRNA. Translation: BAE41134.1.
BC066857 mRNA. Translation: AAH66857.1.
BC141078 mRNA. Translation: AAI41079.1.
Y00884 mRNA. Translation: CAA68777.1. Frameshift.

IPI

IPI00271951.

PIR

ISMSER. B34930.
S06318.

RefSeq

NP_033917.2. NM_009787.2.

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	[»]

ProteinModelPortal

P08003.

SMR

P08003. Positions 47-507, 516-638.

ModBase

Search...

PTM databases

PhosphoSite

P08003.

Proteomic databases

PaxDb

P08003.

PRIDE

P08003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823.

GeneID

12304.

KEGG

mmu:12304.

Organism-specific databases

CTD

9601.

MGI

MGI:104864. Pdia4.

Phylogenomic databases

eggNOG

COG0526.

GeneTree

ENSGT00700000104218.

HOGENOM

HOG000162459.

HOVERGEN

HBG005920.

InParanoid

Q6NXW4.

KO

K09582.

OrthoDB

EOG405S0R.

Gene expression databases

Bgee

P08003.

CleanEx

MM_PDIA4.

Genevestigator

P08003.

GermOnline

ENSMUSG00000025823. Mus musculus.

Family and domain databases

Gene3D

3.40.30.10. 4 hits.

InterPro

IPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR017068. Protein_diS-isomerase_A4.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 3 hits.
[Graphical view]

PIRSF

PIRSF036862. Disulphide_isom_A4. 1 hit.

PRINTS

PR00421. THIOREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 5 hits.

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

ChiTaRS

PDIA4. mouse.

EvolutionaryTrace

P08003.

NextBio

280830.

SOURCE

Search...

Entry information

Entry name

PDIA4_MOUSE

Accession

Primary (citable) accession number: P08003
Secondary accession number(s): P15841 , Q3TT79, Q3UJW0, Q6NXW4, Q8BMT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 30, 2010
Last modified:	April 3, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program