P13667 (PDIA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 139.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 645 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 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Coding sequence diversity | Polymorphism |
| Domain | Redox-active center Repeat Signal |
| Molecular function | Isomerase |
| PTM | Acetylation Disulfide bond |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic processInferred from electronic annotation. Source: InterPro protein secretionTraceable author statement. Source: ProtInc |
| Cellular component | endoplasmic reticulum lumen Traceable author statement. Source: ProtInc melanosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activityInferred from electronic annotation. Source: EC protein disulfide oxidoreductase activityInferred 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 – 645 | 625 | Protein disulfide-isomerase A4 | PRO_0000034229 | |||||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 21 – 169 | 149 | Thioredoxin 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 158 – 301 | 144 | Thioredoxin 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 505 – 636 | 132 | Thioredoxin 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Motif | 642 – 645 | 4 | Prevents secretion from ER | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Compositional bias | 39 – 55 | 17 | Asp/Glu-rich (acidic) | ||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 366 | 1 | N6-acetyllysine Ref.10 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 91 ↔ 94 | Redox-active By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 206 ↔ 209 | Redox-active By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 555 ↔ 558 | Redox-active By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 173 | 1 | T → M. Corresponds to variant rs2290971 [ dbSNP | Ensembl ]. | VAR_052580 | |||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 102 | 1 | E → G in BAF83660. Ref.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 69 – 71 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 72 – 76 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 87 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 94 – 109 | 16 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 113 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 121 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 122 – 124 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 126 – 131 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 139 – 144 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 148 – 150 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 157 – 168 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 178 – 181 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 184 – 186 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 187 – 193 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 195 – 202 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 209 – 211 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 213 – 224 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 226 – 228 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 232 – 236 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 237 – 239 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 241 – 246 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 254 – 259 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 263 – 265 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 276 – 282 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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: 2549034] [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: 2002068] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [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. 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: 15489334] [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: 12475965] [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: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, MASS SPECTROMETRY. |
| [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: 21269460] [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. | ||||||||||||
| IPI | IPI00009904. | ||||||||||||
| PIR | A23723. | ||||||||||||
| RefSeq | NP_004902.1. NM_004911.4. | ||||||||||||
| UniGene | Hs.93659. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P13667. | ||||||||||||
| SMR | P13667. Positions 54-645. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P13667. 3 interactions. | ||||||||||||
| MINT | MINT-4999858. | ||||||||||||
| STRING | P13667. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P13667. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 119530. | ||||||||||||
2D gel databases | |||||||||||||
| OGP | P13667. | ||||||||||||
| REPRODUCTION-2DPAGE | IPI00009904. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | P13667. | ||||||||||||
| PRIDE | P13667. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000286091; ENSP00000286091; ENSG00000155660. | ||||||||||||
| GeneID | 9601. | ||||||||||||
| KEGG | hsa:9601. | ||||||||||||
| UCSC | uc003wff.2. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 9601. | ||||||||||||
| GeneCards | GC07M148700. | ||||||||||||
| H-InvDB | HIX0007183. | ||||||||||||
| HGNC | HGNC:30167. PDIA4. | ||||||||||||
| HPA | CAB017368. HPA006139. HPA006140. | ||||||||||||
| neXtProt | NX_P13667. | ||||||||||||
| PharmGKB | PA142671190. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG09813. | ||||||||||||
| GeneTree | ENSGT00590000082864. | ||||||||||||
| HOGENOM | HBG627841. | ||||||||||||
| HOVERGEN | HBG005920. | ||||||||||||
| InParanoid | P13667. | ||||||||||||
| OMA | ATQFWRN. | ||||||||||||
| OrthoDB | EOG405S0R. | ||||||||||||
| PhylomeDB | P13667. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 5.3.4.1. 2681. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P13667. | ||||||||||||
| Bgee | P13667. | ||||||||||||
| CleanEx | HS_PDIA4. | ||||||||||||
| Genevestigator | P13667. | ||||||||||||
| GermOnline | ENSG00000155660. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| 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] | ||||||||||||
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 4 hits. | ||||||||||||
| KO | K09582. | ||||||||||||
| 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 | |||||||||||||
| NextBio | 36019. | ||||||||||||
Entry information
| Entry name | PDIA4_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P13667 Secondary accession number(s): A8K4K6, Q549T6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with