Tag | Content |
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CPLM ID | CPLM-017869 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ERO1-like protein alpha |
Protein Synonyms/Alias | ERO1-L; ERO1-L-alpha; Endoplasmic oxidoreductin-1-like protein; Global ischemia-induced protein 11; Oxidoreductin-1-L-alpha |
Gene Name | Ero1l |
Gene Synonyms/Alias | Giig11 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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67 | RLFPRLQKLLESDYF | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins (By similarity). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1 (By similarity). |
Sequence Annotation | BINDING 186 186 FAD (By similarity). BINDING 188 188 FAD (By similarity). BINDING 199 199 FAD (By similarity). BINDING 248 248 FAD (By similarity). BINDING 251 251 FAD (By similarity). BINDING 283 283 FAD (By similarity). BINDING 296 296 FAD (By similarity). MOD_RES 142 142 Phosphoserine (By similarity). CARBOHYD 276 276 N-linked (GlcNAc...) (Potential). CARBOHYD 380 380 N-linked (GlcNAc...) (Potential). DISULFID 35 48 By similarity. DISULFID 37 46 By similarity. DISULFID 85 387 By similarity. DISULFID 94 130 Alternate; alternate (By similarity). DISULFID 94 99 Redox-active; alternate (By similarity). DISULFID 99 104 Alternate (By similarity). DISULFID 207 237 By similarity. DISULFID 390 393 Redox-active (By similarity). |
Keyword | Alternative splicing; Apoptosis; Complete proteome; Disulfide bond; Electron transport; Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome; Signal; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 464 AA |
Protein Sequence | MGRGWGLLVG LLGVVWLLRS GQGEEQQQET AAQRCFCQVS GYLDDCTCDV ETIDKFNNYR 60 LFPRLQKLLE SDYFRYYKVN LRKPCPFWND INQCGRRDCA VKPCHSDEVP DGIKSASYKY 120 SKEANLLEEC EQAERLGAVD ESLSEETQKA VLQWTKHDDS SDSFCEVDDI QSPDAEYVDL 180 LLNPERYTGY KGPDAWRIWS VIYEENCFKP QTIQRPLASG QGKHKENTFY SWLEGLCVEK 240 RAFYRLISGL HASINVHLSA RYLLQDNWLE KKWGHNVTEF QQRFDGVLTE GEGPRRLKNL 300 YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDVENKELL LEILHEVKSF PLHFDENSFF 360 AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ TQGLGTALKI LFSEKLIANM 420 PESGPSYEFQ LTRQEIVSLF NAFGRISTSV RELENFRHLL QNVH 464 |
Gene Ontology | GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro. GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro. GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB. GO:0006457; P:protein folding; IEA:GOC. GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB. |
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SMART | |
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PRINTS | |