CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024720
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein-methionine sulfoxide oxidase MICAL1 
Protein Synonyms/Alias
 Molecule interacting with CasL protein 1; MICAL-1 
Gene Name
 Mical1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
115ARVVLVEKRTKFSRHacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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. Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4 (By similarity). 
Sequence Annotation
 DOMAIN 507 608 CH.
 DOMAIN 679 741 LIM zinc-binding.
 NP_BIND 95 123 FAD (By similarity).
 REGION 1 489 Monooxygenase domain (By similarity).
 BINDING 95 95 FAD (By similarity).
 BINDING 114 114 FAD (By similarity).
 BINDING 116 116 FAD (By similarity).
 BINDING 121 121 FAD (By similarity).
 BINDING 123 123 FAD (By similarity).
 BINDING 393 393 FAD (By similarity).
 MOD_RES 616 616 Phosphoserine (By similarity).  
Keyword
 Actin-binding; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1047 AA 
Protein Sequence
MASPTSTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLPQYHK IKAQLNYWSA 60
KSLWAKLDKR ASQPAYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRTKFS 120
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGFT 180
FTGLQPPPKK GSGWRARIQP SPPAQLASYE FDVLISAGGG KFVPEGFTIR EMRGKLAIGI 240
TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDD THYFVMTAKK 300
QCLLRLGVLR QDLPETDQLL GKANVVPEAL QQFARAAADF ATQGKLGKLE FAQDARGRPD 360
VAAFDFTSMM RSESSARIQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 420
KRWAEGTGPL ELLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ 480
DLYDIMDKEH ARKKSDETDA RKTTTGSAGT EELLHWCQEQ TAGFPGVSVT DFSSSWADGR 540
ALCALVHRLQ PGLLEPSELQ GMSALEATAW ALRVAEYELG IIPVLSAQAV VAGSDPLGLI 600
AYLSHFHSAF KNTPHSSGLV SQPHGTPSAI LFLGKLQRSL QRTRTKVEEE TPCTEEPPVS 660
EPSVPPALPS EHEEAGAEDV CELCGKRLYI LERFCVDGHF FHRGCFCCRT CEATLRPGGY 720
GQYPGDGYFY CLQHLPQEDQ KEADNNGSPE NQELPTPGDS TTQSGPSSPV PPVTEASPVP 780
SPSQPARRLI RLSSVERLRL SSLNIIPDSG VEPPPKPPRS CLDLAQESLK SSFMGWGVLR 840
APQVPEAIEK GEEEEEEEEE EEEEEEELPP PLALEVEQSL LTLAKNSGDM TKYPTWRRTL 900
MRRAKEEEMK RFCKAQAIQR RLNEIEAAMR ELETEGMKLE VALRKESSSP EKQKKLWLEQ 960
LLQLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHEFRG INREETLKTQ ADRLSEDRVL 1020
RKLLDVVNQR DALIQFQEER RLREMPV 1047 
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.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0001933; P:negative regulation of protein phosphorylation; IEA:Compara. 
Interpro
 IPR001715; CH-domain.
 IPR022735; DUF3585.
 IPR002938; mOase_FAD-bd.
 IPR001781; Znf_LIM. 
Pfam
 PF00307; CH
 PF12130; DUF3585
 PF01494; FAD_binding_3
 PF00412; LIM 
SMART
 SM00033; CH
 SM00132; LIM 
PROSITE
 PS50021; CH
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS