Search Results

Overview

Uniprot IDP52907
Protein NameF-actin-capping protein subunit alpha-1
Gene NameCAPZA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 FKFDHLRKEASDPQP
166 ESHQFQPKNFWNGRW
19 EKVRIAAKFITHAPP
268 QLPVTRTKIDWNKIL
278 WNKILSYKIGKEMQN
97 PRNKISFKFDHLRKE

Function

F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (PubMed:22891260). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)

Protein Sequence

10 MADFDDRVSD 20 EEKVRIAAKF 30 ITHAPPGEFN 40 EVFNDVRLLL 50 NNDNLLREGA 60 AHAFAQYNMD 70 QFTPVKIEGY 80 EDQVLITEHG 90 DLGNSRFLDP 100 RNKISFKFDH 110 LRKEASDPQP 120 EEADGGLKSW 130 RESCDSALRA 140 YVKDHYSNGF 150 CTVYAKTIDG 160 QQTIIACIES 170 HQFQPKNFWN 180 GRWRSEWKFT 190 ITPPTAQVVG 200 VLKIQVHYYE 210 DGNVQLVSHK 220 DVQDSLTVSN 230 EAQTAKEFIK 240 IIENAENEYQ 250 TAISENYQTM 260 SDTTFKALRR 270 QLPVTRTKID 280 WNKILSYKIG KEMQNA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0030863 cortical cytoskeleton
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0008290 F-actin capping protein complex
Cellular Component GO:0071203 WASH complex
Molecular Function GO:0003779 actin binding
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0051016 barbed-end actin filament capping
Biological Process GO:0034329 cell junction assembly
Biological Process GO:0065003 protein-containing complex assembly

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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] 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.

[5] 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.

[6] 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.