Search Results

Overview

Uniprot IDP30101
Protein NameProtein disulfide-isomerase A3
Gene NamePDIA3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 VSGYPTLKIFRDGEE
129 DGIVSHLKKQAGPAS
130 GIVSHLKKQAGPASV
146 LRTEEEFKKFISDKD
214 RPSHLTNKFEDKTVA
218 LTNKFEDKTVAYTEQ
226 TVAYTEQKMTSGKIK
231 EQKMTSGKIKKFIQE
274 VDYEKNAKGSNYWRN
288 NRVMMVAKKFLDAGH
289 RVMMVAKKFLDAGHK
296 KFLDAGHKLNFAVAS
305 NFAVASRKTFSHELS
335 IRTAKGEKFVMQEEF
362 DYFDGNLKRYLKSEP
366 GNLKRYLKSEPIPES
417 KNLEPKYKELGEKLS
425 ELGEKLSKDPNIVIA
460 IYFSPANKKLNPKKY
461 YFSPANKKLNPKKYE
494 PPVIQEEKPKKKKKA
496 VIQEEKPKKKKKAQE
75 EAAATRLKGIVPLAK
82 KGIVPLAKVDCTANT
94 ANTNTCNKYGVSGYP

Function

Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323)

Protein Sequence

10 MRLRRLALFP 20 GVALLLAAAR 30 LAAASDVLEL 40 TDDNFESRIS 50 DTGSAGLMLV 60 EFFAPWCGHC 70 KRLAPEYEAA 80 ATRLKGIVPL 90 AKVDCTANTN 100 TCNKYGVSGY 110 PTLKIFRDGE 120 EAGAYDGPRT 130 ADGIVSHLKK 140 QAGPASVPLR 150 TEEEFKKFIS 160 DKDASIVGFF 170 DDSFSEAHSE 180 FLKAASNLRD 190 NYRFAHTNVE 200 SLVNEYDDNG 210 EGIILFRPSH 220 LTNKFEDKTV 230 AYTEQKMTSG 240 KIKKFIQENI 250 FGICPHMTED 260 NKDLIQGKDL 270 LIAYYDVDYE 280 KNAKGSNYWR 290 NRVMMVAKKF 300 LDAGHKLNFA 310 VASRKTFSHE 320 LSDFGLESTA 330 GEIPVVAIRT 340 AKGEKFVMQE 350 EFSRDGKALE 360 RFLQDYFDGN 370 LKRYLKSEPI 380 PESNDGPVKV 390 VVAENFDEIV 400 NNENKDVLIE 410 FYAPWCGHCK 420 NLEPKYKELG 430 EKLSKDPNIV 440 IAKMDATAND 450 VPSPYEVRGF 460 PTIYFSPANK 470 KLNPKKYEGG 480 RELSDFISYL 490 QREATNPPVI 500 QEEKPKKKKK AQEDL

Gene Ontology

Classification GO ID Description
Molecular Function GO:0004197 cysteine-type endopeptidase activity
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0042470 melanosome
Cellular Component GO:0042824 MHC class I peptide loading complex
Cellular Component GO:0005634 nucleus
Cellular Component GO:0045335 phagocytic vesicle
Cellular Component GO:0055038 recycling endosome membrane
Molecular Function GO:0004629 C-type glycerophospholipase activity
Molecular Function GO:0015036 disulfide oxidoreductase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0106222 lncRNA binding
Molecular Function GO:0003756 protein disulfide isomerase activity
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0015035 protein-disulfide reductase activity
Molecular Function GO:0003723 RNA binding
Biological Process GO:0002250 adaptive immune response
Biological Process GO:0002502 peptide antigen assembly with MHC class I protein complex
Biological Process GO:0006457 protein folding
Biological Process GO:0034975 protein folding in endoplasmic reticulum
Biological Process GO:0034976 response to endoplasmic reticulum stress

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[8] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.