ID   PDIA3_MESAU             Reviewed;         208 AA.
AC   P86235;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Protein disulfide-isomerase A3 {ECO:0000250|UniProtKB:P30101};
DE            EC=5.3.4.1 {ECO:0000250|UniProtKB:P30101};
DE   Flags: Fragments;
GN   Name=PDIA3 {ECO:0000250|UniProtKB:P30101};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
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: Subunit of the TAP complex, also known as the peptide loading
CC       complex (PLC). Can form disulfide-linked heterodimers with TAPBP.
CC       Interacts with ERP27 and CANX (By similarity). Interacts with MZB1 in a
CC       calcium-dependent manner (By similarity). Interacts with SERPINA2 and
CC       with the S and Z variants of SERPINA1. Interacts with ATP2A2 (By
CC       similarity). {ECO:0000250|UniProtKB:P27773,
CC       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: In the caput epididymal spermatozoa, detected in
CC       the mid-peice and at low levels in the principal piece. In the cauda
CC       epididymal spermatozoa, detected at very low levels in the principal
CC       piece and not in the mid-piece (at protein level).
CC       {ECO:0000269|PubMed:20400973}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86235; -.
DR   SMR; P86235; -.
DR   Proteomes; UP000189706; Unplaced.
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.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Disulfide bond; Endoplasmic reticulum; Isomerase;
KW   Phosphoprotein; Redox-active center; Reference proteome; Repeat.
FT   CHAIN           <1..>208
FT                   /note="Protein disulfide-isomerase A3"
FT                   /id="PRO_0000394742"
FT   DOMAIN          <1..>44
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          151..>208
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   SITE            34
FT                   /note="Lowers pKa of C-terminal Cys of first active site"
FT                   /evidence="ECO:0000250|UniProtKB:P07237"
FT   MOD_RES         44
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27773"
FT   MOD_RES         49
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27773"
FT   MOD_RES         133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P30101"
FT   MOD_RES         163
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P27773"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        70..71
FT                   /evidence="ECO:0000305"
FT   NON_CONS        105..106
FT                   /evidence="ECO:0000305"
FT   NON_CONS        118..119
FT                   /evidence="ECO:0000305"
FT   NON_CONS        143..144
FT                   /evidence="ECO:0000305"
FT   NON_CONS        152..153
FT                   /evidence="ECO:0000305"
FT   NON_CONS        180..181
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         208
SQ   SEQUENCE   208 AA;  23388 MW;  46D8A6DFC622165B CRC64;
     RLAPEYEAAA TRYGVSGYPT LKDGEEAGAY DGPRTADGIV SHLKFISDKD ASVVGFFRDL
     FSDGHSEFLK FAHTNVESLV KEYDDNGEGI TLFRPSHLAN KFEDKDLLTA YYDVDYEKKT
     FSHELSDFGL ESTTGEVPVV AIRFVMQEEF SRFLQDYFDG NLKRYLKSEP IPETNDGPVK
     MDATANDVPS PYEVKGFPTI YFSPANKK