ERO1A_XENTR
ID ERO1A_XENTR Reviewed; 474 AA.
AC B1H1F9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Neurula, and Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) 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-99 and Cys-138, and between Cys-104
CC and Cys-109. 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-99/Cys-104 and Cys-401/Cys-404 disulfide bonds constitute
CC the redox-active center. The Cys-99/Cys-104 disulfide bond may accept
CC electron from protein disulfide isomerase (PDI) and funnel them to the
CC active site disulfide Cys-401/Cys-404 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC160591; AAI60591.1; -; mRNA.
DR EMBL; BC170922; AAI70922.1; -; mRNA.
DR EMBL; BC170928; AAI70928.1; -; mRNA.
DR RefSeq; NP_001016058.1; NM_001016058.2.
DR AlphaFoldDB; B1H1F9; -.
DR SMR; B1H1F9; -.
DR STRING; 8364.ENSXETP00000061870; -.
DR PaxDb; B1H1F9; -.
DR PRIDE; B1H1F9; -.
DR GeneID; 548812; -.
DR KEGG; xtr:548812; -.
DR CTD; 30001; -.
DR Xenbase; XB-GENE-978124; ero1a.
DR eggNOG; KOG2608; Eukaryota.
DR InParanoid; B1H1F9; -.
DR OrthoDB; 1181226at2759; -.
DR Reactome; R-XTR-3299685; Detoxification of Reactive Oxygen Species.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0016972; F:thiol oxidase activity; IEA:InterPro.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..474
FT /note="ERO1-like protein alpha"
FT /id="PRO_0000368277"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 259
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..53
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 42..51
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 90..398
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 99..138
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 99..104
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 104..109
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 215..248
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 401..404
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 474 AA; 54721 MW; 0FC77D5B0F897525 CRC64;
MVSGCCRLDM SSYVSVLVLC SLLLWGSNSQ QEQSSAAQRC FCQVTGYLDD CTCDVETIDH
FNNYGLFPKL QQLVASDYFR YYKANLKKPC PFWEDNSHCG VKDCAVKPCP TDEVPGLKPP
GFKYTEEANR AHEEIDDCEK EKRLSAVDES LSVEAQEAML KWNRHDDSAD NFCELDDEES
PDAEYVDLLK NPERYTGYKG ADTWRIWNSI YEENCFKPKA VQRPLNPLTS TRGENEGKVF
YNWLDGLCVE KRAFYRLISG LHASINIHLC ANYLLKDTWM DKIWGHNTAE FQKRFDATLT
QGEGPKRLKN LYFIYLIELR AISKVLPFFE RSSFLLYTGN ETKDTETKKL LLDVLLDARD
FPLHFDENSL FSGDKKEAAK LKEDFRQHFR NISKIMDCVG CFKCRLWGKL QTQGLGTALK
ILFSERQIEN LSESNQPSEF HLTRQEIVAL FNAFARISTS VKELENFRTL LEKV
