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Overview

Uniprot IDQ7Z2W4
Protein NameZinc finger CCCH-type antiviral protein 1
Gene NameZC3HAV1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
296 PVDDLTRKFTYLGSQ
314 RPPSGSSKATDLGGT
374 NDQGARRKTVFSPTL
401 PEAVTTRKGTGLLSS
448 STRSLNYKSTSSGHR
76 RARVCRRKYCQRPCD

Function

Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs (PubMed:32866210). Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae, including human immunodeficiency virus type 1, filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation

Protein Sequence

10 MADPEVCCFI 20 TKILCAHGGR 30 MALDALLQEI 40 ALSEPQLCEV 50 LQVAGPDRFV 60 VLETGGEAGI 70 TRSVVATTRA 80 RVCRRKYCQR 90 PCDNLHLCKL 100 NLLGRCNYSQ 110 SERNLCKYSH 120 EVLSEENFKV 130 LKNHELSGLN 140 KEELAVLLLQ 150 SDPFFMPEIC 160 KSYKGEGRQQ 170 ICNQQPPCSR 180 LHICDHFTRG 190 NCRFPNCLRS 200 HNLMDRKVLA 210 IMREHGLNPD 220 VVQNIQDICN 230 SKHMQKNPPG 240 PRAPSSHRRN 250 MAYRARSKSR 260 DRFFQGSQEF 270 LASASASAER 280 SCTPSPDQIS 290 HRASLEDAPV 300 DDLTRKFTYL 310 GSQDRARPPS 320 GSSKATDLGG 330 TSQAGTSQRF 340 LENGSQEDLL 350 HGNPGSTYLA 360 SNSTSAPNWK 370 SLTSWTNDQG 380 ARRKTVFSPT 390 LPAARSSLGS 400 LQTPEAVTTR 410 KGTGLLSSDY 420 RIINGKSGTQ 430 DIQPGPLFNN 440 NADGVATDIT 450 STRSLNYKST 460 SSGHREISSP 470 RIQDAGPASR 480 DVQATGRIAD 490 DADPRVALVN 500 DSLSDVTSTT 510 SSRVDDHDSE 520 EICLDHLCKG 530 CPLNGSCSKV 540 HFHLPYRWQM 550 LIGKTWTDFE 560 HMETIEKGYC 570 NPGIHLCSVG 580 SYTINFRVMS 590 CDSFPIRRLS 600 TPSSVTKPAN 610 SVFTTKWIWY 620 WKNESGTWIQ 630 YGEEKDKRKN 640 SNVDSSYLES 650 LYQSCPRGVV 660 PFQAGSRNYE 670 LSFQGMIQTN 680 IASKTQKDVI 690 RRPTFVPQWY 700 VQQMKRGPDH 710 QPAKTSSVSL 720 TATFRPQEDF 730 CFLSSKKYKL 740 SEIHHLHPEY 750 VRVSEHFKAS 760 MKNFKIEKIK 770 KIENSELLDK 780 FTWKKSQMKE 790 EGKLLFYATS 800 RAYVESICSN 810 NFDSFLHETH 820 ENKYGKGIYF 830 AKDAIYSHKN 840 CPYDAKNVVM 850 FVAQVLVGKF 860 TEGNITYTSP 870 PPQFDSCVDT 880 RSNPSVFVIF 890 QKDQVYPQYV 900 IEYTEDKACV IS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005770 late endosome
Cellular Component GO:0005764 lysosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0051607 defense response to virus
Biological Process GO:0045087 innate immune response
Biological Process GO:0045071 negative regulation of viral genome replication
Biological Process GO:0043123 positive regulation of canonical NF-kappaB signal transduction
Biological Process GO:0032727 positive regulation of interferon-alpha production
Biological Process GO:0032728 positive regulation of interferon-beta production
Biological Process GO:0061014 positive regulation of mRNA catabolic process
Biological Process GO:1900246 positive regulation of RIG-I signaling pathway
Biological Process GO:0009615 response to virus

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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[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.