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P13667 (PDIA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase A4

EC=5.3.4.1
Alternative name(s):
Endoplasmic reticulum resident protein 70
Short name=ER protein 70
Short name=ERp70
Endoplasmic reticulum resident protein 72
Short name=ER protein 72
Short name=ERp-72
Short name=ERp72
Gene names
Name:PDIA4
Synonyms:ERP70, ERP72
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8 Ref.9

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 3 thioredoxin domains.

Caution

Was originally (Ref.1) thought to be a deoxycytidine kinase.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q763533EBI-1054653,EBI-6248077From a different organism.
PPIBP232843EBI-1054653,EBI-8771982

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 645625Protein disulfide-isomerase A4
PRO_0000034229

Regions

Domain21 – 169149Thioredoxin 1
Domain158 – 301144Thioredoxin 2
Domain505 – 636132Thioredoxin 3
Motif642 – 6454Prevents secretion from ER
Compositional bias39 – 5517Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue3661N6-acetyllysine Ref.10
Disulfide bond91 ↔ 94Redox-active By similarity
Disulfide bond206 ↔ 209Redox-active By similarity
Disulfide bond555 ↔ 558Redox-active By similarity

Natural variations

Natural variant1731T → M.
Corresponds to variant rs2290971 [ dbSNP | Ensembl ].
VAR_052580

Experimental info

Sequence conflict1021E → G in BAF83660. Ref.3

Secondary structure

................................................. 645
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13667 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 1919C2AE12CD2684

FASTA64572,932
        10         20         30         40         50         60 
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE 

        70         80         90        100        110        120 
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI 

       130        140        150        160        170        180 
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL 

       190        200        210        220        230        240 
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE 

       250        260        270        280        290        300 
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL 

       310        320        330        340        350        360 
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP 

       370        380        390        400        410        420 
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS 

       430        440        450        460        470        480 
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD 

       490        500        510        520        530        540 
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM 

       550        560        570        580        590        600 
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF 

       610        620        630        640 
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL 

« Hide

References

« Hide 'large scale' references
[1]"Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity."
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
J. Biol. Chem. 264:14762-14768(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]Erratum
Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.
J. Biol. Chem. 266:5353-5353(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Lung and Muscle.
[7]"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.
[8]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05016 mRNA. Translation: AAA58460.1.
AK290971 mRNA. Translation: BAF83660.1.
AC093743 Genomic DNA. Translation: AAQ96863.1.
CH471146 Genomic DNA. Translation: EAW80065.1.
CH471146 Genomic DNA. Translation: EAW80066.1.
BC000425 mRNA. Translation: AAH00425.1.
BC001928 mRNA. Translation: AAH01928.1.
BC006344 mRNA. Translation: AAH06344.1.
BC011754 mRNA. Translation: AAH11754.1.
PIRA23723.
RefSeqNP_004902.1. NM_004911.4.
UniGeneHs.93659.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDVX-ray1.95A53-284[»]
ProteinModelPortalP13667.
SMRP13667. Positions 54-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114966. 52 interactions.
IntActP13667. 16 interactions.
MINTMINT-4999858.
STRING9606.ENSP00000286091.

PTM databases

PhosphoSiteP13667.

Polymorphism databases

DMDM119530.

2D gel databases

OGPP13667.
REPRODUCTION-2DPAGEIPI00009904.

Proteomic databases

PaxDbP13667.
PeptideAtlasP13667.
PRIDEP13667.

Protocols and materials databases

DNASU9601.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286091; ENSP00000286091; ENSG00000155660.
GeneID9601.
KEGGhsa:9601.
UCSCuc003wff.2. human.

Organism-specific databases

CTD9601.
GeneCardsGC07M148700.
HGNCHGNC:30167. PDIA4.
HPACAB017368.
HPA006139.
HPA006140.
neXtProtNX_P13667.
PharmGKBPA142671190.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
HOVERGENHBG005920.
InParanoidP13667.
KOK09582.
OMAHHTFSTE.
OrthoDBEOG7VHSX1.
PhylomeDBP13667.
TreeFamTF106382.

Enzyme and pathway databases

BRENDA5.3.4.1. 2681.

Gene expression databases

ArrayExpressP13667.
BgeeP13667.
CleanExHS_PDIA4.
GenevestigatorP13667.

Family and domain databases

Gene3D3.40.30.10. 4 hits.
InterProIPR005788. 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]
PfamPF00085. Thioredoxin. 3 hits.
[Graphical view]
PIRSFPIRSF036862. Disulphide_isom_A4. 1 hit.
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 5 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDIA4. human.
EvolutionaryTraceP13667.
GenomeRNAi9601.
NextBio36019.
PROP13667.

Entry information

Entry namePDIA4_HUMAN
AccessionPrimary (citable) accession number: P13667
Secondary accession number(s): A8K4K6, Q549T6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM