Tag | Content |
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CPLM ID | CPLM-002156 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein disulfide-isomerase |
Protein Synonyms/Alias | PDI; Cellular thyroid hormone-binding protein; Prolyl 4-hydroxylase subunit beta |
Gene Name | P4hb |
Gene Synonyms/Alias | Pdia1 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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67 | ALAPEYAKAAAKLKA | acetylation | [1] | 73 | AKAAAKLKAEGSEIR | acetylation | [1] | 83 | GSEIRLAKVDATEES | acetylation | [1] | 105 | VRGYPTIKFFKNGDT | acetylation | [1] | 108 | YPTIKFFKNGDTASP | acetylation | [1] | 132 | DDIVNWLKKRTGPAA | acetylation | [1] | 202 | FSKYQLDKDGVVLFK | acetylation | [1] | 210 | DGVVLFKKFDEGRNN | acetylation | [1] | 224 | NFEGEITKEKLLDFI | acetylation | [1] | 226 | EGEITKEKLLDFIKH | acetylation | [1] | 273 | SVSDYDGKLSNFKKA | acetylation | [1] | 278 | DGKLSNFKKAAEGFK | acetylation | [1] | 310 | ILEFFGLKKEECPAV | acetylation | [1] | 328 | TLEEEMTKYKPESDE | acetylation | [1] | 330 | EEEMTKYKPESDELT | acetylation | [1] | 354 | HFLEGKIKPHLMSQE | acetylation | [1] | 368 | ELPEDWDKQPVKVLV | acetylation | [1] | 377 | PVKVLVGKNFEEVAF | acetylation | [1] | 387 | EEVAFDEKKNVFVEF | acetylation | [1] | 411 | QLAPIWDKLGETYKD | acetylation | [1] | 438 | ANEVEAVKVHSFPTL | acetylation | [1] | 469 | ERTLDGFKKFLESGG | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP (By similarity). |
Sequence Annotation | DOMAIN 20 136 Thioredoxin 1. DOMAIN 335 477 Thioredoxin 2. MOTIF 506 509 Prevents secretion from ER. ACT_SITE 55 55 Nucleophile (By similarity). ACT_SITE 58 58 Nucleophile (By similarity). ACT_SITE 399 399 Nucleophile (By similarity). ACT_SITE 402 402 Nucleophile (By similarity). DISULFID 55 58 Redox-active (By similarity). DISULFID 399 402 Redox-active (By similarity). |
Keyword | Cell membrane; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Isomerase; Membrane; Redox-active center; Reference proteome; Repeat; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 509 AA |
Protein Sequence | MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFAEAL AAHNYLLVEF YAPWCGHCKA 60 LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA 120 GREADDIVNW LKKRTGPAAT TLSDTAAAES LVDSSEVTVI GFFKDAGSDS AKQFLLAAEA 180 VDDIPFGITS NSDVFSKYQL DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI 240 EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSNFKKA AEGFKGKILF IFIDSDHTDN 300 QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITQFCHHFLE GKIKPHLMSQ 360 ELPEDWDKQP VKVLVGKNFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE 420 NIVIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA 480 GDNDDLDLEE ALEPDMEEDD DQKAVKDEL 509 |
Gene Ontology | GO:0009986; C:cell surface; IEA:Compara. GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara. GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0009055; F:electron carrier activity; IEA:InterPro. GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:Compara. GO:0003756; F:protein disulfide isomerase activity; IMP:RGD. GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. GO:0045454; P:cell redox homeostasis; IEA:InterPro. GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IEA:Compara. |
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PROSITE | |
PRINTS | |