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Protein disulfide-isomerase A4 (EC 5.3.4.1) (Calcium-binding protein 2) (CaBP2) (Endoplasmic reticulum resident protein 70) (ER protein 70) (ERp70) (Endoplasmic reticulum resident protein 72) (ER protein 72) (ERp-72) (ERp72)

 PDIA4_RAT               Reviewed;         643 AA.
P38659; Q6P7S5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
23-MAY-2018, entry version 157.
RecName: Full=Protein disulfide-isomerase A4;
EC=5.3.4.1;
AltName: Full=Calcium-binding protein 2;
Short=CaBP2;
AltName: Full=Endoplasmic reticulum resident protein 70;
Short=ER protein 70;
Short=ERp70;
AltName: Full=Endoplasmic reticulum resident protein 72;
Short=ER protein 72;
Short=ERp-72;
Short=ERp72;
Flags: Precursor;
Name=Pdia4; Synonyms=Cabp2, Erp70;
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].
STRAIN=Wistar; TISSUE=Liver;
PubMed=8477750; DOI=10.1111/j.1432-1033.1993.tb17821.x;
Van P.N., Rupp K., Lampen A., Soeling H.-D.;
"CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase
activity.";
Eur. J. Biochem. 213:789-795(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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).
[3]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 283-523.
PubMed=19446521; DOI=10.1016/j.str.2009.02.016;
Kozlov G., Maattanen P., Schrag J.D., Hura G.L., Gabrielli L.,
Cygler M., Thomas D.Y., Gehring K.;
"Structure of the noncatalytic domains and global fold of the protein
disulfide isomerase ERp72.";
Structure 17:651-659(2009).
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX.
-!- INTERACTION:
P24368:Ppib; NbExp=2; IntAct=EBI-917435, EBI-916926;
Q9VVJ7:Sep15 (xeno); NbExp=2; IntAct=EBI-917435, EBI-128899;
P06882:Tg; NbExp=3; IntAct=EBI-917435, EBI-1549657;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000250|UniProtKB:P13667}. Melanosome
{ECO:0000250|UniProtKB:P13667}.
-!- INDUCTION: Upon glucose starvation, as well as treatment with
tunicamycin.
-!- PTM: O-glycosylated.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
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EMBL; M86870; AAA19217.1; -; mRNA.
EMBL; BC061535; AAH61535.1; -; mRNA.
PIR; S32476; S32476.
RefSeq; NP_446301.1; NM_053849.1.
UniGene; Rn.39305; -.
PDB; 3EC3; X-ray; 1.92 A; A/B=283-523.
PDBsum; 3EC3; -.
ProteinModelPortal; P38659; -.
SMR; P38659; -.
BioGrid; 250512; 5.
IntAct; P38659; 10.
STRING; 10116.ENSRNOP00000008728; -.
iPTMnet; P38659; -.
PhosphoSitePlus; P38659; -.
PaxDb; P38659; -.
PRIDE; P38659; -.
GeneID; 116598; -.
KEGG; rno:116598; -.
UCSC; RGD:619835; rat.
CTD; 9601; -.
RGD; 619835; Pdia4.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000162459; -.
HOVERGEN; HBG005920; -.
InParanoid; P38659; -.
KO; K09582; -.
PhylomeDB; P38659; -.
BRENDA; 5.3.4.1; 5301.
EvolutionaryTrace; P38659; -.
PRO; PR:P38659; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:1903334; P:positive regulation of protein folding; IDA:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR017068; Protein_diS-isomerase_A4.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 3.
PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
SUPFAM; SSF52833; SSF52833; 5.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 3.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 3.
PROSITE; PS51352; THIOREDOXIN_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Isomerase; Redox-active center;
Reference proteome; Repeat; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 643 Protein disulfide-isomerase A4.
/FTId=PRO_0000034231.
DOMAIN 21 167 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 167 299 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 503 634 Thioredoxin 3. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 640 643 Prevents secretion from ER.
MOD_RES 364 364 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13667}.
DISULFID 89 92 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 204 207 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 553 556 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
CONFLICT 43 43 D -> E (in Ref. 1; AAA19217).
{ECO:0000305}.
CONFLICT 391 391 A -> D (in Ref. 1; AAA19217).
{ECO:0000305}.
CONFLICT 497 497 Q -> R (in Ref. 1; AAA19217).
{ECO:0000305}.
STRAND 284 287 {ECO:0000244|PDB:3EC3}.
HELIX 291 300 {ECO:0000244|PDB:3EC3}.
STRAND 305 309 {ECO:0000244|PDB:3EC3}.
HELIX 316 328 {ECO:0000244|PDB:3EC3}.
TURN 329 331 {ECO:0000244|PDB:3EC3}.
STRAND 334 337 {ECO:0000244|PDB:3EC3}.
HELIX 340 346 {ECO:0000244|PDB:3EC3}.
STRAND 350 356 {ECO:0000244|PDB:3EC3}.
HELIX 359 361 {ECO:0000244|PDB:3EC3}.
STRAND 370 373 {ECO:0000244|PDB:3EC3}.
HELIX 380 390 {ECO:0000244|PDB:3EC3}.
STRAND 395 398 {ECO:0000244|PDB:3EC3}.
TURN 400 402 {ECO:0000244|PDB:3EC3}.
HELIX 403 406 {ECO:0000244|PDB:3EC3}.
STRAND 409 417 {ECO:0000244|PDB:3EC3}.
TURN 423 425 {ECO:0000244|PDB:3EC3}.
HELIX 426 440 {ECO:0000244|PDB:3EC3}.
STRAND 446 452 {ECO:0000244|PDB:3EC3}.
TURN 453 456 {ECO:0000244|PDB:3EC3}.
HELIX 457 462 {ECO:0000244|PDB:3EC3}.
STRAND 473 477 {ECO:0000244|PDB:3EC3}.
STRAND 483 485 {ECO:0000244|PDB:3EC3}.
HELIX 493 504 {ECO:0000244|PDB:3EC3}.
SEQUENCE 643 AA; 72720 MW; C5BC8536834543ED CRC64;
MKLRKAWLLV LLLALTQLLA AASAEDAHED ASDSENPIED DDDEEEDEED EDDLEVKEEN
GVWVLNDENF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE KIASTLKDND PPIAVAKIDA
TSASMLASKF DVSGYPTIKI LKKGQAVDYD GSRTQEEIVA KVREVSQPDW TPPPEVTLTL
TKENFDDVVN NADIILVEFY APWCGHCKKL APEYEKAAKE LSKRSPPIPL AKVDATEQTD
LAKRFDVSGY PTLKIFRKGR PFDYNGPREK YGIVDYMVEQ SGPPSKEILT LKQVQEFLKD
GDDVVILGVF QGVGDPGYLQ YQDAANTLRE DYKFHHTFST EIAKFLKVSL GKLVLMQPEK
FQSKYEPRMH VMDVQGSTEA SAIKDYVVKH ALPLVGHRKT SNDAKRYSKR PLVVVYYSVD
FSFDYRTATQ FWRNKVLEVA KDFPEYTFAI ADEEDYATEV KDLGLSESGE DVNAAILDES
GKKFAMEPEE FDSDALQEFV MAFKKGKLKP VIKSQPVPKN NKGPVRVVVG KTFDAIVMDP
KKDVLIEFYA PWCGHCKQLE PVYTSLGKKY KGQKDLVIAK MDATANDITN DRYKVEGFPT
IYFAPSGDKK NPIKFEGGNR DLEHLSKFID EHATKRSRTK EEL


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