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Overview

Uniprot ID	Q7RTP6
Protein Name	[F-actin]-monooxygenase MICAL3
Gene Name	MICAL3
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
1387	LKPLSIPKRLGLPKP
1579	EGTLQPQKRGLPLVS
1748	KSVFSGYKKDKKKKA

Function

Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission

Protein Sequence

10 MEERKHETMN 20 PAHVLFDRFV 30 QATTCKGTLK 40 AFQELCDHLE 50 LKPKDYRSFY 60 HKLKSKLNYW 70 KAKALWAKLD 80 KRGSHKDYKK 90 GKACTNTKCL 100 IIGAGPCGLR 110 TAIDLSLLGA 120 KVVVIEKRDA 130 FSRNNVLHLW 140 PFTIHDLRGL 150 GAKKFYGKFC 160 AGAIDHISIR 170 QLQLILLKVA 180 LILGIEIHVN 190 VEFQGLIQPP 200 EDQENERIGW 210 RALVHPKTHP 220 VSEYEFEVII 230 GGDGRRNTLE 240 GFRRKEFRGK 250 LAIAITANFI 260 NRNTTAEAKV 270 EEISGVAFIF 280 NQKFFQELRE 290 ATGIDLENIV 300 YYKDDTHYFV 310 MTAKKQSLLD 320 KGVILHDYAD 330 TELLLSRENV 340 DQEALLSYAR 350 EAADFSTQQQ 360 LPSLDFAINH 370 YGQPDVAMFD 380 FTCMYASENA 390 ALVREQNGHQ 400 LLVALVGDSL 410 LEPFWPMGTG 420 IARGFLAAMD 430 SAWMVRSWSL 440 GTSPLEVLAE 450 RESIYRLLPQ 460 TTPENVSKNF 470 SQYSIDPVTR 480 YPNINVNFLR 490 PSQVRHLYDT 500 GETKDIHLEM 510 ESLVNSRTTP 520 KLTRNESVAR 530 SSKLLGWCQR 540 QTDGYAGVNV 550 TDLTMSWKSG 560 LALCAIIHRY 570 RPDLIDFDSL 580 DEQNVEKNNQ 590 LAFDIAEKEL 600 GISPIMTGKE 610 MASVGEPDKL 620 SMVMYLTQFY 630 EMFKDSLPSS 640 DTLDLNAEEK 650 AVLIASTRSP 660 ISFLSKLGQT 670 ISRKRSPKDK 680 KEKDLDGAGK 690 RRKTSQSEEE 700 EAPRGHRGER 710 PTLVSTLTDR 720 RMDVAVGNQN 730 KVKYMATQLL 740 AKFEENAPAQ 750 SIGIRRQGSM 760 KKEFPQNLGG 770 SDTCYFCQKR 780 VYVMERLSAE 790 GKFFHRSCFK 800 CEYCATTLRL 810 SAYAYDIEDG 820 KFYCKPHYCY 830 RLSGYAQRKR 840 PAVAPLSGKE 850 AKGPLQDGAT 860 TDANGRANAV 870 ASSTERTPGS 880 GVNGLEEPSI 890 AKRLRGTPER 900 IELENYRLSL 910 RQAEALQEVP 920 EETQAEHNLS 930 SVLDTGAEED 940 VASSSSESEM 950 EEEGEEEEEE 960 PRLPPSDLGG 970 VPWKEAVRIH 980 ALLKGKSEEE 990 LEASKSFGPG 1000 NEEEEEEEEE 1010 YEEEEEEDYD 1020 EEEEESSEAG 1030 NQRLQQVMHA 1040 ADPLEIQADV 1050 HWTHIREREE 1060 EERMAPASES 1070 SASGAPLDEN 1080 DLEEDVDSEP 1090 AEIEGEAAED 1100 GDPGDTGAEL 1110 DDDQHWSDSP 1120 SDADRELRLP 1130 CPAEGEAELE 1140 LRVSEDEEKL 1150 PASPKHQERG 1160 PSQATSPIRS 1170 PQESALLFIP 1180 VHSPSTEGPQ 1190 LPPVPAATQE 1200 KSPEERLFPE 1210 PLLPKEKPKA 1220 DAPSDLKAVH 1230 SPIRSQPVTL 1240 PEARTPVSPG 1250 SPQPQPPVAA 1260 STPPPSPLPI 1270 CSQPQPSTEA 1280 TVPSPTQSPI 1290 RFQPAPAKTS 1300 TPLAPLPVQS 1310 QSDTKDRLGS 1320 PLAVDEALRR 1330 SDLVEEFWMK 1340 SAEIRRSLGL 1350 TPVDRSKGPE 1360 PSFPTPAFRP 1370 VSLKSYSVEK 1380 SPQDEGLHLL 1390 KPLSIPKRLG 1400 LPKPEGEPLS 1410 LPTPRSPSDR 1420 ELRSAQEERR 1430 ELSSSSGLGL 1440 HGSSSNMKTL 1450 GSQSFNTSDS 1460 AMLTPPSSPP 1470 PPPPPGEEPA 1480 TLRRKLREAE 1490 PNASVVPPPL 1500 PATWMRPPRE 1510 PAQPPREEVR 1520 KSFVESVEEI 1530 PFADDVEDTY 1540 DDKTEDSSLQ 1550 EKFFTPPSCW 1560 PRPEKPRHPP 1570 LAKENGRLPA 1580 LEGTLQPQKR 1590 GLPLVSAEAK 1600 ELAEERMRAR 1610 EKSVKSQALR 1620 DAMARQLSRM 1630 QQMELASGAP 1640 RPRKASSAPS 1650 QGKERRPDSP 1660 TRPTLRGSEE 1670 PTLKHEATSE 1680 EVLSPPSDSG 1690 GPDGSFTSSE 1700 GSSGKSKKRS 1710 SLFSPRRNKK 1720 EKKSKGEGRP 1730 PEKPSSNLLE 1740 EAAAKPKSLW 1750 KSVFSGYKKD 1760 KKKKADDKSC 1770 PSTPSSGATV 1780 DSGKHRVLPV 1790 VRAELQLRRQ 1800 LSFSEDSDLS 1810 SDDVLEKSSQ 1820 KSRREPRTYT 1830 EEELNAKLTR 1840 RVQKAARRQA 1850 KQEELKRLHR 1860 AQIIQRQLQQ 1870 VEERQRRLEE 1880 RGVAVEKALR 1890 GEAGMGKKDD 1900 PKLMQEWFKL 1910 VQEKNAMVRY 1920 ESELMIFARE 1930 LELEDRQSRL 1940 QQELRERMAV 1950 EDHLKTEEEL 1960 SEEKQILNEM 1970 LEVVEQRDSL 1980 VALLEEQRLR 1990 EREEDKDLEA 2000 AMLSKGFSLN WS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005938	cell cortex
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0090543	Flemming body
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0005819	spindle
Molecular Function	GO:0003779	actin binding
Molecular Function	GO:0120501	F-actin monooxygenase activity
Molecular Function	GO:0071949	FAD binding
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0060090	molecular adaptor activity
Molecular Function	GO:0016709	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
Biological Process	GO:0030036	actin cytoskeleton organization
Biological Process	GO:0030042	actin filament depolymerization
Biological Process	GO:0051301	cell division
Biological Process	GO:0007010	cytoskeleton organization
Biological Process	GO:0006887	exocytosis

Reference

[1] 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.