ERO1A_BOVIN
ID ERO1A_BOVIN Reviewed; 468 AA.
AC A5PJN2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ERO1-like protein alpha;
DE Short=ERO1-L;
DE Short=ERO1-L-alpha;
DE EC=1.8.4.- {ECO:0000250|UniProtKB:Q96HE7};
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 proper folding of immunoglobulins. Plays an important
CC role in ER stress-induced, CHOP-dependent apoptosis by activating the
CC inositol 1,4,5-trisphosphate receptor IP3R1.
CC {ECO:0000250|UniProtKB:Q96HE7}.
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-94 and Cys-131, and between Cys-99
CC and Cys-104. 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. Interacts with PDILT. Interacts with ERP44; the interaction
CC results in retention of ERO1A in the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q96HE7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side
CC {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen
CC {ECO:0000250|UniProtKB:Q96HE7}. Secreted
CC {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is
CC essential for its retention in the endoplasmic reticulum (By
CC similarity). In neurons, it localizes to dendrites (By similarity).
CC {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000250|UniProtKB:Q96HE7}.
CC -!- PTM: The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute
CC the redox-active center. The Cys-94/Cys-99 disulfide bond may accept
CC electron from P4HB and funnel them to the active site disulfide Cys-
CC 394/Cys-397. The regulatory Cys-99/Cys-104 disulfide bond stabilizes
CC the other regulatory bond Cys-94/Cys-131 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-145 by FAM20C in the Golgi which increases
CC its enzymatic activity (By similarity). Phosphorylation is induced by
CC lactation (By similarity). It is also induced by hypoxia and reductive
CC stress (By similarity). {ECO:0000250|UniProtKB:Q8R180,
CC ECO:0000250|UniProtKB:Q96HE7}.
CC -!- SIMILARITY: Belongs to the EROs family. {ECO:0000305}.
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DR EMBL; BC142179; AAI42180.1; -; mRNA.
DR RefSeq; NP_001096818.1; NM_001103348.1.
DR AlphaFoldDB; A5PJN2; -.
DR SMR; A5PJN2; -.
DR STRING; 9913.ENSBTAP00000020878; -.
DR PaxDb; A5PJN2; -.
DR PeptideAtlas; A5PJN2; -.
DR PRIDE; A5PJN2; -.
DR Ensembl; ENSBTAT00000020878; ENSBTAP00000020878; ENSBTAG00000015716.
DR GeneID; 100125317; -.
DR KEGG; bta:100125317; -.
DR CTD; 30001; -.
DR VEuPathDB; HostDB:ENSBTAG00000015716; -.
DR VGNC; VGNC:28594; ERO1A.
DR eggNOG; KOG2608; Eukaryota.
DR GeneTree; ENSGT00390000007753; -.
DR HOGENOM; CLU_023061_2_2_1; -.
DR InParanoid; A5PJN2; -.
DR OMA; PDAWRIW; -.
DR OrthoDB; 1181226at2759; -.
DR TreeFam; TF314471; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000015716; Expressed in milk and 106 other tissues.
DR ExpressionAtlas; A5PJN2; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
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:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
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 Apoptosis; Cell projection; Disulfide bond; Electron transport;
KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Golgi apparatus;
KW Membrane; Oxidoreductase; Phosphoprotein; Redox-active center;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..468
FT /note="ERO1-like protein alpha"
FT /id="PRO_0000368273"
FT BINDING 187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT BINDING 300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..48
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 37..46
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 85..391
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 94..131
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 94..99
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 99..104
FT /note="Alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 208..241
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
FT DISULFID 394..397
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q96HE7"
SQ SEQUENCE 468 AA; 54297 MW; 5D4502E22B6105BE CRC64;
MGRRWGFLIG FLVAVGLLGL GHGEQQPSET AAQRCFCQVS GYLDDCTCDV ETIDKFNNYR
LFPRLQKLLE SDYFRYYKVN LKRPCPFWND INQCGRRDCA VKPCHSDEVP DGIKSASYKY
SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEVDD IQSPDAEYVD
LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGKSEE NTFYSWLEGL
CVEKRAFYRL ISGLHASINV HLSARYLLQD TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR
LKNLYFLYLI ELRALSKVVP FFERPDFQLF TGNKDQDAEN KMLLLEILHE IKSFPLHFDE
NSFFAGNKKE ANKLKEDFRL HFRNISRIMD CVGCLKCRLW GKLQTQGLGT ALKILFSEKL
IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH
