ERO1-like protein beta

Details

Name
ERO1-like protein beta
Synonyms
  • 1.8.4.-
  • Endoplasmic reticulum oxidoreductase beta
  • Endoplasmic reticulum oxidoreductin-1-like protein B
  • ERO1-L-beta
  • ERO1LB
  • Oxidoreductin-1-L-beta
Gene Name
ERO1B
Organism
Humans
Amino acid sequence
>lcl|BSEQ0009495|ERO1-like protein beta
MSQGVRRAGAGQGVAAAVQLLVTLSFLRSVVEAQVTGVLDDCLCDIDSIDNFNTYKIFPK
IKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGHSNKYLKM
ANNTKELEDCEQANKLGAINSTLSNQSKEAFIDWARYDDSRDHFCELDDERSPAAQYVDL
LLNPERYTGYKGTSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLC
LEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFKHRFDPVETKGEGPRRL
KNLYFLYLIELRALSKVAPYFERSIVDLYTGNAEEDADTKTLLLNIFQDTKSFPMHFDEK
SMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEI
QKLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRDLQNFKVLLQHSR
Number of residues
467
Molecular Weight
53542.62
Theoretical pI
Not Available
GO Classification
Functions
oxidoreductase activity / oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor / protein disulfide isomerase activity / protein disulfide oxidoreductase activity / unfolded protein binding
Processes
4-hydroxyproline metabolic process / cell redox homeostasis / extracellular matrix organization / glucose homeostasis / insulin processing / protein folding / protein maturation by protein folding
Components
endoplasmic reticulum / endoplasmic reticulum membrane
General Function
Unfolded protein binding
Specific Function
Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0019592|ERO1-like protein beta (ERO1B)
ATGAGCCAAGGGGTCCGCCGGGCAGGCGCTGGGCAGGGGGTAGCGGCCGCGGTGCAGCTG
CTGGTCACCCTGAGCTTCCTGCGGAGCGTCGTCGAGGCGCAGGTCACTGGAGTTCTGGAT
GATTGCTTGTGTGATATTGACAGCATCGATAACTTCAATACCTACAAAATCTTCCCCAAA
ATAAAAAAATTGCAAGAGAGAGACTATTTTCGTTATTACAAGGTTAATCTGAAGCGACCT
TGTCCTTTCTGGGCAGAAGATGGCCACTGTTCAATAAAAGACTGTCATGTGGAGCCCTGT
CCAGAGAGTAAAATTCCGGTTGGAATAAAAGCTGGGCATTCTAATAAGTACTTGAAAATG
GCAAACAATACCAAAGAATTAGAAGATTGTGAGCAAGCTAATAAACTGGGAGCAATTAAC
AGCACATTAAGTAATCAAAGCAAAGAAGCTTTCATTGACTGGGCAAGATATGATGATTCA
CGGGATCACTTTTGTGAACTTGATGATGAGAGATCTCCAGCTGCTCAGTATGTAGACCTA
TTGCTGAACCCAGAGCGTTACACTGGCTATAAAGGGACCTCTGCATGGAGAGTGTGGAAC
AGCATCTATGAAGAGAACTGTTTCAAGCCTCGATCTGTTTATCGTCCTTTAAATCCTCTG
GCGCCTAGCCGAGGCGAAGATGATGGAGAATCATTCTACACATGGCTAGAAGGTTTGTGT
CTGGAGAAAAGAGTCTTCTATAAGCTTATATCGGGACTTCATGCTAGCATCAATTTACAT
CTATGCGCAAATTATCTTTTGGAAGAAACCTGGGGTAAGCCCAGTTGGGGACCTAATATT
AAAGAATTCAAACACCGCTTTGACCCTGTGGAAACCAAGGGAGAAGGTCCAAGAAGGCTC
AAGAATCTTTACTTTTTATACTTGATTGAGCTTCGAGCTTTGTCAAAGGTGGCTCCATAT
TTTGAGCGCTCAATTGTCGATCTTTACACTGGAAATGCAGAAGAAGATGCTGACACAAAA
ACTCTTCTACTGAATATCTTTCAAGATACAAAGTCCTTTCCCATGCACTTTGATGAGAAA
TCCATGTTTGCAGGTGACAAAAAAGGGGCCAAGTCACTAAAGGAGGAATTCCGATTACAT
TTCAAGAATATCTCCCGTATAATGGACTGTGTTGGATGTGACAAATGCAGATTATGGGGA
AAATTACAGACTCAGGGTTTAGGAACTGCCCTGAAGATATTATTCTCTGAAAAAGAAATC
CAAAAGCTTCCAGAGAATAGTCCATCTAAAGGCTTCCAACTCACCCGACAGGAAATAGTT
GCTCTTTTAAATGCTTTTGGAAGGCTTTCTACAAGTATAAGAGACTTACAGAATTTTAAA
GTCTTATTACAACACAGTAGGTAA
Chromosome Location
1
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ86YB8
UniProtKB Entry NameERO1B_HUMAN
HGNC IDHGNC:14355
General References
  1. Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R: Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem. 2000 Aug 4;275(31):23685-92. [Article]
  2. 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, 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
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  5. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R: Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001 Nov 15;20(22):6288-96. [Article]
  6. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R: ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. [Article]
  7. Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A: The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem. 2003 May;270(10):2228-35. [Article]
  8. Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R: Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. J Biol Chem. 2004 Jul 30;279(31):32667-73. Epub 2004 May 25. [Article]
  9. Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ, Benham AM: Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta. J Biol Chem. 2005 Sep 23;280(38):33066-75. Epub 2005 Jul 12. [Article]
  10. Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [Article]
  11. Wang L, Zhu L, Wang CC: The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation. Biochem J. 2011 Feb 15;434(1):113-21. doi: 10.1042/BJ20101357. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB019021-Ethyl-Pyrrolidine-2,5-DioneexperimentalunknownDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails