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Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) (HIP-70) (Q-2)

 PDIA3_RAT               Reviewed;         505 AA.
P11598;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 176.
RecName: Full=Protein disulfide-isomerase A3;
EC=5.3.4.1;
AltName: Full=58 kDa glucose-regulated protein;
AltName: Full=58 kDa microsomal protein;
Short=p58;
AltName: Full=Disulfide isomerase ER-60;
AltName: Full=Endoplasmic reticulum resident protein 57;
Short=ER protein 57;
Short=ERp57;
AltName: Full=Endoplasmic reticulum resident protein 60;
Short=ER protein 60;
Short=ERp60;
AltName: Full=HIP-70;
AltName: Full=Q-2;
Flags: Precursor;
Name=Pdia3; Synonyms=Erp60, Grp58;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3398923; DOI=10.1038/334268a0;
Bennett C.F., Balcarek J.M., Varrichio A., Crooke S.T.;
"Molecular cloning and complete amino-acid sequence of form-I
phosphoinositide-specific phospholipase C.";
Nature 334:268-270(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Kito M., Urade R.;
"Role of novel microsomal cysteine proteases.";
Proc. Jpn. Acad., B, Phys. Biol. Sci. 71:189-192(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1650195; DOI=10.1016/0006-291X(91)90161-Y;
Martin J.L., Pumford N.R., Larosa A.C., Martin B.M., Gonzaga H.M.S.,
Beaven M.A., Pohl L.R.;
"A metabolite of halothane covalently binds to an endoplasmic
reticulum protein that is highly homologous to phosphatidylinositol-
specific phospholipase C-alpha but has no activity.";
Biochem. Biophys. Res. Commun. 178:679-685(1991).
[5]
PROTEIN SEQUENCE OF 26-43.
TISSUE=Brain, and Pituitary;
PubMed=2181662; DOI=10.1126/science.2181662;
Mobbs C.V., Fink G., Pfaff D.W.;
"HIP-70: a protein induced by estrogen in the brain and LH-RH in the
pituitary.";
Science 247:1477-1479(1990).
[6]
PROTEIN SEQUENCE OF 25-54; 258-269; 285-310; 347-350; 412-419 AND
434-463.
TISSUE=Liver;
PubMed=1657921;
Srivastava S.P., Chen N.Q., Liu Y.X., Holtzman J.L.;
"Purification and characterization of a new isozyme of thiol:protein-
disulfide oxidoreductase from rat hepatic microsomes. Relationship of
this isozyme to cytosolic phosphatidylinositol-specific phospholipase
C form 1A.";
J. Biol. Chem. 266:20337-20344(1991).
[7]
PROTEIN SEQUENCE OF 26-34; 174-193; 433-446 AND 448-458.
PubMed=1321829;
Urade R., Nasu M., Moriyama T., Wada K., Kito M.;
"Protein degradation by the phosphoinositide-specific phospholipase C-
alpha family from rat liver endoplasmic reticulum.";
J. Biol. Chem. 267:15152-15159(1992).
[8]
PROTEIN SEQUENCE OF 105-119; 148-161; 184-214; 259-271; 306-329;
336-344; 352-363; 449-460 AND 472-482, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (DEC-2006) to UniProtKB.
[9]
MUTAGENESIS OF 502-GLN--LEU-505.
PubMed=9399589; DOI=10.1093/oxfordjournals.jbchem.a021830;
Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-
Leu (QEDL) motifs of microsomal ER-60 protease.";
J. Biochem. 122:834-842(1997).
[10]
INHIBITION BY PHOSPHOLIPIDS.
PubMed=1330685; DOI=10.1016/0014-5793(92)81415-I;
Urade R., Kito M.;
"Inhibition by acidic phospholipids of protein degradation by ER-60
protease, a novel cysteine protease, of endoplasmic reticulum.";
FEBS Lett. 312:83-86(1992).
[11]
TISSUE SPECIFICITY.
PubMed=20400973; DOI=10.1038/aja.2010.19;
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
Shivaji S.;
"Glucose-regulated protein precursor (GRP78) and tumor rejection
antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
Asian J. Androl. 12:344-355(2010).
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins.
-!- ENZYME REGULATION: Seems to be inhibited by acidic phospholipids.
-!- SUBUNIT: Subunit of the TAP complex, also known as the peptide
loading complex (PLC). Can form disulfide-linked heterodimers with
TAPBP. Interacts with ERP27 and CANX (By similarity). Interacts
with MZB1 in a calcium-dependent manner (By similarity). Interacts
with SERPINA2 and with the S and Z variants of SERPINA1. Interacts
with ATP2A2 (By similarity). {ECO:0000250|UniProtKB:P27773,
ECO:0000250|UniProtKB:P30101}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen
{ECO:0000250}. Melanosome {ECO:0000250|UniProtKB:P30101}.
-!- TISSUE SPECIFICITY: In caput epididymal spermatozoa, detected in
the head, mid and principal pieces. In cauda epididymal
spermatozoa detected only in the acrosome (at protein level).
{ECO:0000269|PubMed:20400973}.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a phosphatidyl-inositol 4,5-
bisphosphate phosphodiesterase type I (phospholipase C-alpha) then
was thought (PubMed:1321829 and PubMed:1330685) to be a thiol
protease. {ECO:0000305|PubMed:3398923}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X12355; CAA30916.1; -; mRNA.
EMBL; D63378; BAA09695.1; -; mRNA.
EMBL; BC062393; AAH62393.1; -; mRNA.
PIR; A28807; A28807.
PIR; A61354; A61354.
RefSeq; NP_059015.1; NM_017319.1.
UniGene; Rn.11527; -.
ProteinModelPortal; P11598; -.
SMR; P11598; -.
BioGrid; 248111; 4.
IntAct; P11598; 6.
MINT; MINT-4575564; -.
STRING; 10116.ENSRNOP00000020478; -.
iPTMnet; P11598; -.
PhosphoSitePlus; P11598; -.
World-2DPAGE; 0004:P11598; -.
PaxDb; P11598; -.
PRIDE; P11598; -.
GeneID; 29468; -.
KEGG; rno:29468; -.
UCSC; RGD:68430; rat.
CTD; 2923; -.
RGD; 68430; Pdia3.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000162459; -.
HOVERGEN; HBG005920; -.
InParanoid; P11598; -.
KO; K08056; -.
OrthoDB; EOG091G05J9; -.
PhylomeDB; P11598; -.
TreeFam; TF106382; -.
PRO; PR:P11598; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P11598; RN.
GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0042825; C:TAP complex; IDA:RGD.
GO; GO:0042288; F:MHC class I protein binding; IDA:RGD.
GO; GO:0008233; F:peptidase activity; IDA:RGD.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; ISO:RGD.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IMP:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:1904148; P:cellular response to nonylphenol; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IDA:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:1903334; P:positive regulation of protein folding; IDA:RGD.
GO; GO:1901423; P:response to benzene; IEP:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0044321; P:response to leptin; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 2.
SUPFAM; SSF52833; SSF52833; 4.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 2.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Isomerase; Methylation;
Phosphoprotein; Redox-active center; Reference proteome; Repeat;
Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:1657921}.
CHAIN 25 505 Protein disulfide-isomerase A3.
/FTId=PRO_0000034227.
DOMAIN 25 133 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 343 485 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 502 505 Prevents secretion from ER.
ACT_SITE 57 57 Nucleophile. {ECO:0000250}.
ACT_SITE 60 60 Nucleophile. {ECO:0000250}.
ACT_SITE 406 406 Nucleophile. {ECO:0000250}.
ACT_SITE 409 409 Nucleophile. {ECO:0000250}.
SITE 58 58 Contributes to redox potential value.
{ECO:0000250}.
SITE 59 59 Contributes to redox potential value.
{ECO:0000250}.
SITE 119 119 Lowers pKa of C-terminal Cys of first
active site. {ECO:0000250}.
SITE 407 407 Contributes to redox potential value.
{ECO:0000250}.
SITE 408 408 Contributes to redox potential value.
{ECO:0000250}.
SITE 471 471 Lowers pKa of C-terminal Cys of second
active site. {ECO:0000250}.
MOD_RES 61 61 N6-methyllysine.
{ECO:0000250|UniProtKB:P30101}.
MOD_RES 129 129 N6-succinyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 218 218 N6-succinyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 319 319 Phosphothreonine.
{ECO:0000250|UniProtKB:P30101}.
MOD_RES 362 362 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27773}.
DISULFID 57 60 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 57 57 Interchain (with C-115 in TAPBP); in
linked form. {ECO:0000250}.
DISULFID 85 92 {ECO:0000250}.
DISULFID 406 409 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MUTAGEN 502 505 QEDL->AAGL: Failure to prevent secretion
from ER. {ECO:0000269|PubMed:9399589}.
MUTAGEN 502 505 Missing: Failure to prevent secretion
from ER. {ECO:0000269|PubMed:9399589}.
CONFLICT 1 13 MRFSCLALLPGVA -> MPSAALRCSRAWR (in Ref.
1). {ECO:0000305}.
CONFLICT 98 98 S -> T (in Ref. 1; CAA30916).
{ECO:0000305}.
CONFLICT 232 240 IKKFIQESI -> SRSLFRKA (in Ref. 1;
CAA30916). {ECO:0000305}.
CONFLICT 476 476 F -> L (in Ref. 2; BAA09695).
{ECO:0000305}.
SEQUENCE 505 AA; 56623 MW; EAC7F0C0BD4F1471 CRC64;
MRFSCLALLP GVALLLASAL LASASDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC
KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT
ADGIVSHLKK QAGPASVPLR TEDEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD
NYRFAHTNVE SLVKEYDDNG EGITIFRPLH LANKFEDKIV AYTEKKMTSG KIKKFIQESI
FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNTKGSNYWR NRVMMVAKTF LDAGHKLNFA
VASRKTFSHE LSDFGLESTT GEIPVVAIRT AKGEKFVMQE EFSRDGKALE RFLQEYFDGN
LKRYLKSEPI PETNEGPVKV VVAESFDDIV NAEDKDVLIE FYAPWCGHCK NLEPKYKELG
EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL
QREATNPPII QEEKPKKKKK AQEDL


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