PDIA4_RAT
ID PDIA4_RAT Reviewed; 643 AA.
AC P38659; Q6P7S5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein disulfide-isomerase A4;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P08003};
DE AltName: Full=Calcium-binding protein 2;
DE Short=CaBP2;
DE AltName: Full=Endoplasmic reticulum resident protein 70;
DE Short=ER protein 70;
DE Short=ERp70;
DE AltName: Full=Endoplasmic reticulum resident protein 72;
DE Short=ER protein 72;
DE Short=ERp-72;
DE Short=ERp72;
DE Flags: Precursor;
GN Name=Pdia4; Synonyms=Cabp2, Erp70;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8477750; DOI=10.1111/j.1432-1033.1993.tb17821.x;
RA Van P.N., Rupp K., Lampen A., Soeling H.-D.;
RT "CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase
RT activity.";
RL Eur. J. Biochem. 213:789-795(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 283-523.
RX PubMed=19446521; DOI=10.1016/j.str.2009.02.016;
RA Kozlov G., Maattanen P., Schrag J.D., Hura G.L., Gabrielli L., Cygler M.,
RA Thomas D.Y., Gehring K.;
RT "Structure of the noncatalytic domains and global fold of the protein
RT disulfide isomerase ERp72.";
RL Structure 17:651-659(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P08003};
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. Component of a complex containing at least CRELD2, MANF,
CC MATN3 and PDIA4 (By similarity). {ECO:0000250|UniProtKB:P08003}.
CC -!- INTERACTION:
CC P38659; P24368: Ppib; NbExp=2; IntAct=EBI-917435, EBI-916926;
CC P38659; P06882: Tg; NbExp=3; IntAct=EBI-917435, EBI-1549657;
CC P38659; Q9VVJ7: Sep15; Xeno; NbExp=2; IntAct=EBI-917435, EBI-128899;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P13667}. Melanosome
CC {ECO:0000250|UniProtKB:P13667}.
CC -!- INDUCTION: Upon glucose starvation, as well as treatment with
CC tunicamycin.
CC -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; M86870; AAA19217.1; -; mRNA.
DR EMBL; BC061535; AAH61535.1; -; mRNA.
DR PIR; S32476; S32476.
DR RefSeq; NP_446301.1; NM_053849.1.
DR PDB; 3EC3; X-ray; 1.92 A; A/B=283-523.
DR PDBsum; 3EC3; -.
DR AlphaFoldDB; P38659; -.
DR SMR; P38659; -.
DR BioGRID; 250512; 5.
DR IntAct; P38659; 11.
DR STRING; 10116.ENSRNOP00000008728; -.
DR iPTMnet; P38659; -.
DR PhosphoSitePlus; P38659; -.
DR jPOST; P38659; -.
DR PaxDb; P38659; -.
DR PRIDE; P38659; -.
DR GeneID; 116598; -.
DR KEGG; rno:116598; -.
DR UCSC; RGD:619835; rat.
DR CTD; 9601; -.
DR RGD; 619835; Pdia4.
DR eggNOG; KOG0190; Eukaryota.
DR InParanoid; P38659; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; P38659; -.
DR BRENDA; 5.3.4.1; 5301.
DR EvolutionaryTrace; P38659; -.
DR PRO; PR:P38659; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:1903334; P:positive regulation of protein folding; IDA:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR041866; PDIA4_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Isomerase; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..643
FT /note="Protein disulfide-isomerase A4"
FT /id="PRO_0000034231"
FT DOMAIN 21..167
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 167..299
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 503..634
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..92
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:P08003"
FT MOTIF 553..556
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:P08003"
FT MOTIF 640..643
FT /note="Prevents secretion from ER"
FT COMPBIAS 32..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13667"
FT DISULFID 89..92
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P08003,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 204..207
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 553..556
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P08003,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 43
FT /note="D -> E (in Ref. 1; AAA19217)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> D (in Ref. 1; AAA19217)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="Q -> R (in Ref. 1; AAA19217)"
FT /evidence="ECO:0000305"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:3EC3"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:3EC3"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:3EC3"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 426..440
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:3EC3"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:3EC3"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:3EC3"
FT HELIX 493..504
FT /evidence="ECO:0007829|PDB:3EC3"
SQ 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
