Search Results

Overview

Uniprot ID	O94851
Protein Name	[F-actin]-monooxygenase MICAL2
Gene Name	MICAL2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
681	DMNKRRRKGFTNLDE

Function

Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (PubMed:24440334, PubMed:29343822). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network (PubMed:34106209). Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (PubMed:24440334)

Protein Sequence

10 MGENEDEKQA 20 QAGQVFENFV 30 QASTCKGTLQ 40 AFNILTRHLD 50 LDPLDHRNFY 60 SKLKSKVTTW 70 KAKALWYKLD 80 KRGSHKEYKR 90 GKSCTNTKCL 100 IVGGGPCGLR 110 TAIELAYLGA 120 KVVVVEKRDS 130 FSRNNVLHLW 140 PFTIHDLRGL 150 GAKKFYGKFC 160 AGSIDHISIR 170 QLQLILFKVA 180 LMLGVEIHVN 190 VEFVKVLEPP 200 EDQENQKIGW 210 RAEFLPTDHS 220 LSEFEFDVII 230 GADGRRNTLE 240 GFRRKEFRGK 250 LAIAITANFI 260 NRNSTAEAKV 270 EEISGVAFIF 280 NQKFFQDLKE 290 ETGIDLENIV 300 YYKDCTHYFV 310 MTAKKQSLLD 320 KGVIINDYID 330 TEMLLCAENV 340 NQDNLLSYAR 350 EAADFATNYQ 360 LPSLDFAMNH 370 YGQPDVAMFD 380 FTCMYASENA 390 ALVRERQAHQ 400 LLVALVGDSL 410 LEPFWPMGTG 420 CARGFLAAFD 430 TAWMVKSWNQ 440 GTPPLELLAE 450 RESLYRLLPQ 460 TTPENINKNF 470 EQYTLDPGTR 480 YPNLNSHCVR 490 PHQVKHLYIT 500 KELEHYPLER 510 LGSVRRSVNL 520 SRKESDIRPS 530 KLLTWCQQQT 540 EGYQHVNVTD 550 LTTSWRSGLA 560 LCAIIHRFRP 570 ELINFDSLNE 580 DDAVENNQLA 590 FDVAEREFGI 600 PPVTTGKEMA 610 SAQEPDKLSM 620 VMYLSKFYEL 630 FRGTPLRPVD 640 SWRKNYGENA 650 DLSLAKSSIS 660 NNYLNLTFPR 670 KRTPRVDGQT 680 GENDMNKRRR 690 KGFTNLDEPS 700 NFSSRSLGSN 710 QECGSSKEGG 720 NQNKVKSMAN 730 QLLAKFEEST 740 RNPSLMKQER 750 RVSGIGKPVL 760 CSSSGPPVHS 770 CCPKPEEATP 780 SPSPPLKRQF 790 PSVVVTGHVL 800 RELKQVSAGS 810 ECLSRPWRAR 820 AKSDLQLGGT 830 ENFATLPSTR 840 PRAQALSGVL 850 WRLQQVEEKI 860 LQKRAQNLAN 870 REFHTKNIKE 880 KAAHLASMFG 890 HGDFPQNKLL 900 SKGLSHTHPP 910 SPPSRLPSPD 920 PAASSSPSTV 930 DSASPARKEK 940 KSPSGFHFHP 950 SHLRTVHPQL 960 TVGKVSSGIG 970 AAAEVLVNLY 980 MNDHRPKAQA 990 TSPDLESMRK 1000 SFPLNLGGSD 1010 TCYFCKKRVY 1020 VMERLSAEGH 1030 FFHRECFRCS 1040 ICATTLRLAA 1050 YTFDCDEGKF 1060 YCKPHFIHCK 1070 TNSKQRKRRA 1080 ELKQQREEEA 1090 TWQEQEAPRR 1100 DTPTESSCAV 1110 AAIGTLEGSP 1120 PDEPTSPKRP 1130 KSISEPQHSD 1140 AEGDAASPLP 1150 SEWTSVRISP 1160 GEEAAGQDVL 1170 AVRVLVTSED 1180 SSSDTESDYG 1190 GSEGSHTEPC 1200 EEKPWRPGSP 1210 HLPHTSLGEA 1220 LSRAVSPQCP 1230 EEPRAVHAAL 1240 QRANSFQSPT 1250 PSKYQNWRRE 1260 FWWSLTPVNK 1270 RTMSPPKDPS 1280 PSLPLPSSSS 1290 HSSSPPSSSS 1300 TSVSGNAPDG 1310 SSPPQMTASE 1320 PLSQVSRGHP 1330 SPPTPNFRRR 1340 AVAQGAPREI 1350 PLYLPHHPKP 1360 EWAEYCLVSP 1370 GEDGLSDPAE 1380 MTSDECQPAE 1390 APLGDIGSNH 1400 RDPHPIWGKD 1410 RSWTGQELSP 1420 LAGEDREKGS 1430 TGARKEEEGG 1440 PVLVKEKLGL 1450 KKLVLTQEQK 1460 TMLLDWNDSI 1470 PESVHLKAGE 1480 RISQKSAENG 1490 RGGRVLKPVR 1500 PLLLPRAAGE 1510 PLPTQRGAQE 1520 KMGTPAEQAQ 1530 GERNVPPPKS 1540 PLRLIANAIR 1550 RSLEPLLSNS 1560 EGGKKAWAKQ 1570 ESKTLPAQAC 1580 TRSFSLRKTN 1590 SNKDGDQHSP 1600 GRNQSSAFSP 1610 PDPALRTHSL 1620 PNRPSKVFPA 1630 LRSPPCSKIE 1640 DVPTLLEKVS 1650 LQENFPDASK 1660 PPKKRISLFS 1670 SLRLKDKSFE 1680 SFLQESRQRK 1690 DIRDLFGSPK 1700 RKVLPEDSAQ 1710 ALEKLLQPFK 1720 STSLRQAAPP 1730 PPPPPPPPPP 1740 PPTAGGADSK 1750 NFPLRAQVTE 1760 ASSSASSTSS 1770 SSADEEFDPQ 1780 LSLQLKEKKT 1790 LRRRKKLEKA 1800 MKQLVKQEEL 1810 KRLYKAQAIQ 1820 RQLEEVEERQ 1830 RASEIQGVRL 1840 EKALRGEADS 1850 GTQDEAQLLQ 1860 EWFKLVLEKN 1870 KLMRYESELL 1880 IMAQELELED 1890 HQSRLEQKLR 1900 EKMLKEESQK 1910 DEKDLNEEQE 1920 VFTELMQVIE 1930 QRDKLVDSLE 1940 EQRIREKAED 1950 QHFESFVFSR GCQLSRT

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
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:0051019	mitogen-activated protein kinase binding
Molecular Function	GO:0016174	NAD(P)H oxidase H2O2-forming activity
Molecular Function	GO:0016491	oxidoreductase 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:0007010	cytoskeleton organization
Biological Process	GO:0007507	heart development
Biological Process	GO:0001947	heart looping
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0019417	sulfur oxidation

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.