ERO1A_DANRE
ID ERO1A_DANRE Reviewed; 489 AA.
AC Q7T3D1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) 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-86 and Cys-123, and between Cys-91
CC and Cys-96. Glutathione may be required to regulate its activity in the
CC 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-86/Cys-91 and Cys-385/Cys-388 disulfide bonds constitute
CC the redox-active center. The Cys-86/Cys-91 disulfide bond may accept
CC electron from protein disulfide isomerase (PDI) and funnel them to the
CC active site disulfide Cys-385/Cys-388 (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; BC053166; AAH53166.1; -; mRNA.
DR AlphaFoldDB; Q7T3D1; -.
DR SMR; Q7T3D1; -.
DR STRING; 7955.ENSDARP00000015478; -.
DR PaxDb; Q7T3D1; -.
DR ZFIN; ZDB-GENE-040426-1312; ero1a.
DR eggNOG; KOG2608; Eukaryota.
DR InParanoid; Q7T3D1; -.
DR PhylomeDB; Q7T3D1; -.
DR Reactome; R-DRE-264876; Insulin processing.
DR Reactome; R-DRE-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q7T3D1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..489
FT /note="ERO1-like protein alpha"
FT /id="PRO_0000368275"
FT BINDING 179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 192
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..40
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 29..38
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 77..382
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 86..123
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 86..91
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 91..96
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 200..232
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 385..388
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 489 AA; 56589 MW; 2C5E6C356C6EB929 CRC64;
METCVLLLGL FLTSVHVTTA GSAAHRCFCQ VTGTLDDCAC DVETIDKFNN KDIFPKLQKL
LSSDYFRFYK VNLNNGCPFW TDHSQCGLKY CAVKPCSPDE VPEGLKSSSY KYSEKASHDT
EECEKAEKLG AVNGSLSDET RQALEEWKKY DDESDRFCML DDEDSPESQY VDLLLNPERF
TGYKGAEAWR IWNSIYEENC FKPYSVNRPL NPLASNSGDD GQGFYRWLEG LCVEKRAFFR
LISGLHASIN IHLSARYLLD ENWFEMKWGH NVSEFQQRFD EDLTKGEGPK RLRNLYFLYL
IELRALAKIL PYFERSTFQL YTGQDTQDDQ NKKLLLELLH VAKSFPLHFD ETALFAGNNK
EAMKLKEDFK LTFKNISRIM DCVECFKCRL WGKLQTQGLG TALKILFSER QIEAMPNKQH
QSIISAQSAG NCVFVQRFRK NLHKCQRVEE LQIVVVETQT VTVKMFQERA TVQTDMHKHM
TFPMFGYIQ
