ERO1A_XENLA
ID ERO1A_XENLA Reviewed; 465 AA.
AC Q6DD71;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ERO1-like protein alpha;
DE Short=ERO1-L;
DE Short=ERO1-L-alpha;
DE EC=1.8.4.-;
DE AltName: Full=Endoplasmic reticulum oxidoreductase alpha {ECO:0000250|UniProtKB:Q96HE7};
DE AltName: Full=Endoplasmic reticulum oxidoreductin-1-like protein;
DE AltName: Full=Oxidoreductin-1-L-alpha;
DE Flags: Precursor;
GN Name=ero1a {ECO:0000250|UniProtKB:Q96HE7}; Synonyms=ero1l, ero1lb;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidoreductase involved in disulfide bond formation in the
CC endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme
CC catalyzing protein disulfide formation, in order to allow P4HB to
CC sustain additional rounds of disulfide formation. Following P4HB
CC reoxidation, passes its electrons to molecular oxygen via FAD, leading
CC to the production of reactive oxygen species (ROS) in the cell.
CC Required for the folding of immunoglobulins (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q96HE7};
CC -!- ACTIVITY REGULATION: Enzyme activity is tightly regulated to prevent
CC the accumulation of reactive oxygen species in the endoplasmic
CC reticulum. Reversibly down-regulated by the formation of disulfide
CC bonds between the active site Cys-90 and Cys-129, and between Cys-95
CC and Cys-100. Glutathione may be required to regulate its activity in
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Predominantly monomer. May function both as a monomer and a
CC homodimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}.
CC -!- PTM: The Cys-90/Cys-95 and Cys-392/Cys-395 disulfide bonds constitute
CC the redox-active center. The Cys-90/Cys-95 disulfide bond may accept
CC electron from protein disulfide isomerase (PDI) and funnel them to the
CC active site disulfide Cys-392/Cys-395 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
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DR EMBL; BC077754; AAH77754.1; -; mRNA.
DR AlphaFoldDB; Q6DD71; -.
DR SMR; Q6DD71; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0016972; F:thiol oxidase activity; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:InterPro.
DR InterPro; IPR007266; Ero1.
DR InterPro; IPR037192; ERO1-like_sf.
DR PANTHER; PTHR12613; PTHR12613; 1.
DR Pfam; PF04137; ERO1; 1.
DR PIRSF; PIRSF017205; ERO1; 1.
DR SUPFAM; SSF110019; SSF110019; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Electron transport; Endoplasmic reticulum; FAD;
KW Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; Redox-active center;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..465
FT /note="ERO1-like protein alpha"
FT /id="PRO_0000368276"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 198
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 250
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..44
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 33..42
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 81..389
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 90..129
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 90..95
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 95..100
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 206..239
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 392..395
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 465 AA; 53739 MW; C9F905CD4EE69CA6 CRC64;
MSSYGSVLFL FSLLVWGTIA QEAPASAAQR CFCQVTGYLD DCTCDVETID RFNNHGLFPK
LQQLVASDYF RYYKVNLKKS CPFWEDNSHC GVRDCAVNPC SSDEVPGFKP PGFKYTEEAN
HVHEDVDDCE KEKRLSAVDE SLSVETQEAM LKWNRHDDSS DNFCEVDDEE SPDAEYVDLL
KNPERFTGYK GADTWRIWNS IYEENCFKPK AVQRPLNPLT SSRGENEGNM FYNWLDGLCV
EKRAFYRLIS GLHASINIHL CATYLLKDTW MDKIWGHNVA EFQKRFDATL THGEGPKRLR
NLYFIYLIEL RAISKVLPFF ERSNFLLYTG NETKDKETKK ILLDVLQDAR DFPLHFDENS
LFSGDKKEAA KLKEDFRQHF RNISKIMDCV GCFKCRLWGK LQTQGLGTAL KILFSEKQIE
NLSESNQPSA FHLTRQEIVA LFNAFGRIST SVQELENFRK LLEKV
