ID   PDIA3_PAPHA             Reviewed;          39 AA.
AC   P81246;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein disulfide-isomerase A3;
DE            EC=5.3.4.1 {ECO:0000250|UniProtKB:P30101};
DE   AltName: Full=58 kDa glucose-regulated protein;
DE   AltName: Full=58 kDa microsomal protein;
DE            Short=p58;
DE   Flags: Fragments;
GN   Name=PDIA3; Synonyms=GRP58;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Hepatocyte;
RX   PubMed=9660200; DOI=10.1046/j.1432-1327.1998.2540420.x;
RA   Bonfils C.;
RT   "Purification of a 58-kDa protein (ER58) from monkey liver microsomes and
RT   comparison with protein-disulfide isomerase.";
RL   Eur. J. Biochem. 254:420-427(1998).
CC   -!- FUNCTION: Disulfide isomerase which catalyzes the formation,
CC       isomerization, and reduction or oxidation of disulfide bonds (By
CC       similarity). Associates with calcitriol, the active form of vitamin D3
CC       which mediates the action of this vitamin on cells (By similarity).
CC       Association with calcitriol does not affect its enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P30101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P30101};
CC   -!- SUBUNIT: Interacts with ERP27 and CANX. Interacts with MZB1 in a
CC       calcium-dependent manner. Interacts with SERPINA2 and with the S and Z
CC       variants of SERPINA1. Interacts with ATP2A2.
CC       {ECO:0000250|UniProtKB:P27773, ECO:0000250|UniProtKB:P30101}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen
CC       {ECO:0000250}. Melanosome {ECO:0000250|UniProtKB:P30101}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver. Low in brain,
CC       testis and colon. Not detectable in pancreas and skeletal muscle.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P81246; -.
DR   SMR; P81246; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW   Redox-active center.
FT   CHAIN           1..>39
FT                   /note="Protein disulfide-isomerase A3"
FT                   /id="PRO_0000120176"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000305"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
FT   NON_TER         39
SQ   SEQUENCE   39 AA;  4086 MW;  4BDFEA7932B563CC CRC64;
     SDVLELTDDN FESRVSDTGS AGLVEFFAPD ATANDVPSP