CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001476
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein-methionine sulfoxide oxidase MICAL2 
Protein Synonyms/Alias
 Molecule interacting with CasL protein 2; MICAL-2 
Gene Name
 MICAL2 
Gene Synonyms/Alias
 KIAA0750; MICAL2PV1; MICAL2PV2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
458TTPENINKNFEQYTLubiquitination[1]
634RPVDSWRKNYGENADubiquitination[1]
646NADLSLAKSSISNNYubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (By similarity). 
Sequence Annotation
 DOMAIN 516 619 CH.
 DOMAIN 1000 1062 LIM zinc-binding.
 NP_BIND 97 125 FAD (By similarity).
 REGION 2 494 Monooxygenase domain (By similarity).
 BINDING 97 97 FAD (By similarity).
 BINDING 116 116 FAD (By similarity).
 BINDING 118 118 FAD (By similarity).
 BINDING 123 123 FAD (By similarity).
 BINDING 125 125 FAD (By similarity).
 BINDING 398 398 FAD (By similarity).  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1124 AA 
Protein Sequence
MGENEDEKQA QAGQVFENFV QASTCKGTLQ AFNILTRHLD LDPLDHRNFY SKLKSKVTTW 60
KAKALWYKLD KRGSHKEYKR GKSCTNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDS 120
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEIHVN 180
VEFVKVLEPP EDQENQKIGW RAEFLPTDHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK 240
LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDCTHYFV 300
MTAKKQSLLD KGVIINDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ LPSLDFAMNH 360
YGQPDVAMFD FTCMYASENA ALVRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD 420
TAWMVKSWNQ GTPPLELLAE RESLYRLLPQ TTPENINKNF EQYTLDPGTR YPNLNSHCVR 480
PHQVKHLYIT KELEHYPLER LGSVRRSVNL SRKESDIRPS KLLTWCQQQT EGYQHVNVTD 540
LTTSWRSGLA LCAIIHRFRP ELINFDSLNE DDAVENNQLA FDVAEREFGI PPVTTGKEMA 600
SAQEPDKLSM VMYLSKFYEL FRGTPLRPVD SWRKNYGENA DLSLAKSSIS NNYLNLTFPR 660
KRTPRVDGQT GENDMNKRRR KGFTNLDEPS NFSSRSLGSN QECGSSKEGG NQNKVKSMAN 720
QLLAKFEEST RNPSLMKQER RVSGIGKPVL CSSSGPPVHS CCPKPEEATP SPSPPLKRQF 780
PSVVVTGHVL RELKQVSAGS ECLSRPWRAR AKSDLQLGGT ENFATLPSTR PRAQALSGVL 840
WRLQQVEEKI LQKRAQNLAN REFHTKNIKE KAAHLASMFG HGDFPQNKLL SKGLSHTHPP 900
SPPSRLPSPD PAASSSPSTV DSASPARKEK KSPSGFHFHP SHLRTVHPQL TVGKVSSGIG 960
AAAEVLVNLY MNDHRPKAQA TSPDLESMRK SFPLNLGGSD TCYFCKKRVY VMERLSAEGH 1020
FFHRECFRCS ICATTLRLAA YTFDCDEGKF YCKPHFIHCK TNSKQRKRRA ELKQQREEEA 1080
TWQEQEAPRR DTPTESSCAV AAIGTLEGSP PVHFSLPVLH PLLG 1124 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; ISS:UniProtKB.
 GO:0071949; F:FAD binding; ISS:UniProtKB.
 GO:0016709; F: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; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030042; P:actin filament depolymerization; ISS:UniProtKB. 
Interpro
 IPR001715; CH-domain.
 IPR002938; mOase_FAD-bd.
 IPR003042; Rng_hydrolase-like.
 IPR001781; Znf_LIM. 
Pfam
 PF00307; CH
 PF01494; FAD_binding_3
 PF00412; LIM 
SMART
 SM00033; CH
 SM00132; LIM 
PROSITE
 PS50021; CH
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS
 PR00420; RNGMNOXGNASE.