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ERO1A_PIG
ID   ERO1A_PIG               Reviewed;         468 AA.
AC   B6CVD7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Long Q., Yang Z.;
RL   Submitted (MAR-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 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; EU552934; ACD13001.1; -; mRNA.
DR   RefSeq; NP_001131099.1; NM_001137627.1.
DR   AlphaFoldDB; B6CVD7; -.
DR   SMR; B6CVD7; -.
DR   STRING; 9823.ENSSSCP00000005415; -.
DR   PaxDb; B6CVD7; -.
DR   PeptideAtlas; B6CVD7; -.
DR   PRIDE; B6CVD7; -.
DR   Ensembl; ENSSSCT00015055699; ENSSSCP00015022385; ENSSSCG00015040725.
DR   Ensembl; ENSSSCT00040027162; ENSSSCP00040011486; ENSSSCG00040019923.
DR   Ensembl; ENSSSCT00060047212; ENSSSCP00060020226; ENSSSCG00060034808.
DR   Ensembl; ENSSSCT00070061633; ENSSSCP00070052554; ENSSSCG00070030612.
DR   GeneID; 100192435; -.
DR   KEGG; ssc:100192435; -.
DR   CTD; 30001; -.
DR   eggNOG; KOG2608; Eukaryota.
DR   HOGENOM; CLU_023061_2_2_1; -.
DR   InParanoid; B6CVD7; -.
DR   OMA; PDAWRIW; -.
DR   OrthoDB; 1181226at2759; -.
DR   TreeFam; TF314471; -.
DR   Reactome; R-SSC-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 1.
DR   Genevisible; B6CVD7; SS.
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_0000368274"
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;  54281 MW;  3D05F9C9D946F98A CRC64;
     MGHRWGFLIV FLGAVGLLGS GYGRQQPSET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR
     LFPRLQKLLE SDYFRYYKVN LKRPCPFWND INQCGRRDCA VKPCQSDEIP DGIKSASYKY
     SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPDAEYVD
     LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGKSEE NTFYSWLEGL
     CVEKRAFYRL ISGLHASINV HLSARYLLQD TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR
     LKNLYFLYLI ELRALSKVVP FFERPDFQLF TGNKVQDAEN KMLLLDILHE IKSFPLHFDE
     NSFFAGDKKE ANKLKEDFRL HFRNISRIMD CVGCLKCRLW GKLQTQGLGT ALKILFSEKL
     IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH
 
 
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