Search Results

Overview

Uniprot IDP01009
Protein NameAlpha-1-antitrypsin
Gene NameSERPINA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
153 EGLKLVDKFLEDVKK
159 DKFLEDVKKLYHSEA
160 KFLEDVKKLYHSEAF
178 FGDTEEAKKQINDYV
179 GDTEEAKKQINDYVE
187 QINDYVEKGTQGKIV
192 VEKGTQGKIVDLVKE
198 GKIVDLVKELDRDTV
217 NYIFFKGKWERPFEV
257 MFNIQHCKKLSSWVL
258 FNIQHCKKLSSWVLL
298 LTHDIITKFLENEDR
314 SASLHLPKLSITGTY
352 VTEEAPLKLSKAVHK
355 EAPLKLSKAVHKAVL
359 KLSKAVHKAVLTIDE
411 KSPLFMGKVVNPTQK

Function

Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin

Protein Sequence

10 MPSSVSWGIL 20 LLAGLCCLVP 30 VSLAEDPQGD 40 AAQKTDTSHH 50 DQDHPTFNKI 60 TPNLAEFAFS 70 LYRQLAHQSN 80 STNIFFSPVS 90 IATAFAMLSL 100 GTKADTHDEI 110 LEGLNFNLTE 120 IPEAQIHEGF 130 QELLRTLNQP 140 DSQLQLTTGN 150 GLFLSEGLKL 160 VDKFLEDVKK 170 LYHSEAFTVN 180 FGDTEEAKKQ 190 INDYVEKGTQ 200 GKIVDLVKEL 210 DRDTVFALVN 220 YIFFKGKWER 230 PFEVKDTEEE 240 DFHVDQVTTV 250 KVPMMKRLGM 260 FNIQHCKKLS 270 SWVLLMKYLG 280 NATAIFFLPD 290 EGKLQHLENE 300 LTHDIITKFL 310 ENEDRRSASL 320 HLPKLSITGT 330 YDLKSVLGQL 340 GITKVFSNGA 350 DLSGVTEEAP 360 LKLSKAVHKA 370 VLTIDEKGTE 380 AAGAMFLEAI 390 PMSIPPEVKF 400 NKPFVFLMIE 410 QNTKSPLFMG KVVNPTQK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030134 COPII-coated ER to Golgi transport vesicle
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0031093 platelet alpha granule lumen
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0002020 protease binding
Molecular Function GO:0004867 serine-type endopeptidase inhibitor activity
Biological Process GO:0006953 acute-phase response
Biological Process GO:0007596 blood coagulation

Reference

[1] 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.

[2] 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.

[3] 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.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[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] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.