ID PDIA1_MACFU Reviewed; 510 AA. AC Q2HWU2; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Protein disulfide-isomerase; DE Short=PDI; DE EC=5.3.4.1; DE AltName: Full=Prolyl 4-hydroxylase subunit beta; DE Flags: Precursor; GN Name=P4HB; Synonyms=PDI, PDIA1; OS Macaca fuscata fuscata (Japanese macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9543; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=17214666; DOI=10.1111/j.1600-0684.2006.00186.x; RA Higashino A., Fukuhara R., Tezuka T., Kageyama T.; RT "Molecular cloning and gene expression of endoplasmic reticulum stress RT proteins in Japanese monkey, Macaca fuscata."; RL J. Med. Primatol. 35:376-383(2006). CC -!- FUNCTION: This multifunctional protein catalyzes the formation, CC breakage and rearrangement of disulfide bonds. At the cell CC surface, seems to act as a reductase that cleaves disulfide bonds CC of proteins attached to the cell. May therefore cause structural CC modifications of exofacial proteins. Inside the cell, seems to CC form/rearrange disulfide bonds of nascent proteins. At high CC concentrations, functions as a chaperone that inhibits aggregation CC of misfolded proteins. At low concentrations, facilitates CC aggregation (anti-chaperone activity). May be involved with other CC chaperones in the structural modification of the TG precursor in CC hormone biogenesis. Also acts a structural subunit of various CC enzymes such as prolyl 4-hydroxylase and microsomal CC triacylglycerol transfer protein MTTP (By similarity). CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in CC proteins. CC -!- SUBUNIT: Homodimer. Monomers and homotetramers may also occur. CC Also constitutes the structural subunit of prolyl 4-hydroxylase CC and of the microsomal triacylglycerol transfer protein MTTP in CC mammalian cells. Stabilizes both enzymes and retain them in the ER CC without contributing to the catalytic activity. Binds UBQLN1 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC Melanosome (By similarity). Cell membrane; Peripheral membrane CC protein (Potential). Note=Highly abundant. In some cell types, CC seems to be also secreted or associated with the plasma membrane, CC where it undergoes constant shedding and replacement from CC intracellular sources. Localizes near CD4-enriched regions on CC lymphoid cell surfaces (By similarity). CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family. CC -!- SIMILARITY: Contains 2 thioredoxin domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB232156; BAE79726.1; -; mRNA. DR SMR; Q2HWU2; 20-139, 138-247, 370-473. DR HOVERGEN; Q2HWU2; -. DR BRENDA; 5.3.4.1; 276174. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR InterPro; IPR005788; Disulphide_isomerase. DR InterPro; IPR000886; ER_targeting_sequence. DR InterPro; IPR005792; Prot_disulphide_isomerase. DR InterPro; IPR017936; Thioredoxin-like. DR InterPro; IPR006662; Thioredoxin-like_subdom. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2. DR Pfam; PF00085; Thioredoxin; 2. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1. DR TIGRFAMs; TIGR01126; pdi_dom; 2. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 2. DR PROSITE; PS51352; THIOREDOXIN_2; 2. PE 2: Evidence at transcript level; KW Cell membrane; Chaperone; Disulfide bond; Endoplasmic reticulum; KW Isomerase; Membrane; Redox-active center; Repeat; Signal. FT SIGNAL 1 19 By similarity. FT CHAIN 20 510 Protein disulfide-isomerase. FT /FTId=PRO_0000246155. FT DOMAIN 20 136 Thioredoxin 1. FT DOMAIN 351 477 Thioredoxin 2. FT MOTIF 507 510 Prevents secretion from ER (By FT similarity). FT ACT_SITE 55 55 Nucleophile (By similarity). FT ACT_SITE 58 58 Nucleophile (By similarity). FT ACT_SITE 399 399 Nucleophile (By similarity). FT ACT_SITE 402 402 Nucleophile (By similarity). FT SITE 56 56 Contributes to redox potential value (By FT similarity). FT SITE 57 57 Contributes to redox potential value (By FT similarity). FT SITE 122 122 Lowers pKa of C-terminal Cys of first FT active site (By similarity). FT SITE 400 400 Contributes to redox potential value (By FT similarity). FT SITE 401 401 Contributes to redox potential value (By FT similarity). FT SITE 463 463 Lowers pKa of C-terminal Cys of second FT active site (By similarity). FT DISULFID 55 58 Redox-active (By similarity). FT DISULFID 399 402 Redox-active (By similarity). SQ SEQUENCE 510 AA; 57304 MW; 5F917B017F418BE2 CRC64; MLRRALLCLA VAAAPGLYAD APEEEDHVLV LRKSNFAEAL AAHKYLLVEF YAPWCGHCKA LAPEYAKAAG KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFRNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLPDGAAAES LVESSEVAVI GFFKDVESDS AKQFLQAAEA IDDIPFGITS NSDVFSKYQL DKDGVVLFKK FDEGRNNFEG EVTKENLLDF IKYNQLPLVI EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSNFKTA AESFKGKILF IFIDSDHTDN QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAER ITEFCHRFLE GKIKPHLMSQ ELPEDWDKQP VKVLVGKNFE EVAFDENKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE NIVIAKMDST ANEVEAIKVH SFPTLKFFPA SVDRTVIDYN GERTLDGFKK FLESGGQDGA GDDDDLEDLE EAEEPDMEED DDQKAVKDEL //