| Tag | Content |
|---|
| CPLM ID | CPLM-016911 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein-methionine sulfoxide oxidase MICAL3 |
Protein Synonyms/Alias | Molecule interacting with CasL protein 3; MICAL-3 |
Gene Name | Mical3 |
Gene Synonyms/Alias | Kiaa0819; Kiaa1364 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1946 | GELSEEKKILNEMLE | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process (By similarity). |
Sequence Annotation | DOMAIN 518 621 CH.
DOMAIN 762 824 LIM zinc-binding.
NP_BIND 88 117 FAD (Potential).
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).
MOD_RES 649 649 Phosphoserine (By similarity).
MOD_RES 887 887 Phosphothreonine (By similarity).
MOD_RES 977 977 Phosphoserine.
MOD_RES 1153 1153 Phosphoserine.
MOD_RES 1187 1187 Phosphoserine.
MOD_RES 1216 1216 Phosphoserine.
MOD_RES 1307 1307 Phosphoserine.
MOD_RES 1335 1335 Phosphoserine (By similarity).
MOD_RES 1339 1339 Phosphothreonine (By similarity).
MOD_RES 1369 1369 Phosphoserine (By similarity).
MOD_RES 1382 1382 Phosphoserine (By similarity).
MOD_RES 1452 1452 Phosphothreonine (By similarity). |
Keyword | Actin-binding; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Exocytosis; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1993 AA |
Protein Sequence | MEERKQETTN QAHVLFDRFV QATTCKGTLR AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 60
KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 120
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 180
VEFQGLVQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 240
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 300
MTAKKQSLLD KGVILHDYTD TELLLSRENV DQEALLNYAR EAADFSTQQQ LPSLDFAINH 360
YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 420
SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNININFLR 480
PSQVRHLYDS GETKDIHLEM ENMVNPRTTP KLTRNESVAR SSKLLGWCQR QTEGYSGVNV 540
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 600
MASVGEPDKL SMVMYLTQFY EMFKDSLSSS DTLDLNAEEK AVLIASTKSP ISFLSKLGQT 660
ISRKRSPKDK KEKDSDGAGK RRKTSQSEEE EPPRSYKGER PTLVSTLTDR RMDAAVGNQN 720
KVKYMATQLL AKFEENAPAQ STGVRRQGSI KKEFPQNLGG SDTCYFCQKR VYVMERLSAE 780
GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE 840
VKGALQDGPT ADANGLASVA ASSAERSPGT SMNGLEEPSI AKRLRGTPER IELENYRRSV 900
RQVEELEEVP EETQAEHNLS SVLDKGTEED VASSSSESEM EEEEEEDDED DHLPTSDLGG 960
VPWKEAVRIH ALLKGRSEEE LEASKNFEPE EEEEEEEYEE EDEEYEEEEE EESSEAGNKR 1020
LQQIITAADP LAIQADVHWT HIREREAEER MLPTSESSTS RAPLDEDDLE EDADSEPAET 1080
EGEAAEDGDP GDTGAELDDQ HWSDDIPSDA EAEHRLQSQA KVKAELELRV SENEEEKPSD 1140
APKQEERGTS QVSSPSQPPE KQVGVFSPAR SPGTEEAKSP LATKVKSPEE PLFPTPLLLR 1200
EKPKAEVPEE QKAVLSPIRS QPVALPEARS PTSPTSLQPE SLLAPPTPPT PPPTQLPICS 1260
QPQPSSDASI PSPTKSPIRF QPVPAKTSTP LTPLPVKSQG DPKDRLSGPL AVEEVLKRSD 1320
LVEEFWMKSA EIRRSLGLTP VDRSKGSEPS LPSPASKPIS LKSYSVDKSP QDEGLCLLKP 1380
PSVPKRLGLP KSAGDQPPLL TPKSPSDKEL RSSQEERRDL SSSSGLGLHD SSSNMKTLGS 1440
QSFNTSDSTM LTPPSSPPPP PPPNEEPATL RRKPHQTFER REASIIPPPT PASFMRPPRE 1500
PAQPPREEVR KSFVESVDEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW SRSEKLQAKE 1560
NGRLPPLEQD VPPQKRGLPL VSAEAKELAE ERMRAREKSV KSQALRDAMA KQLSRMQAME 1620
MVSSRSHTAQ SQGKELGSES TRHPSLRGTQ EPTLKHEATS EEILSPPSDS GGPDGSVTSS 1680
EGSSGKSKKR SSLFSPRRNK KEKKTKGEAR PPEKPSPGLP EDVVAKPKSL WKSVFSGYKK 1740
DKKKKSDEKS CSSTPSSGAT VDSGQRRASP MVRAELQLRR QLSFSEDSDL SSDDILERSS 1800
QKSKREPRTY TEEELSAKLT RRVQKAARRQ AKQEELKRLH RAQIIQRQLE QVEEKQRQLE 1860
ERGVAVEKAL RGEAGMGKKD DPKLMQEWFK LVQEKNAMVR YESELMIFAR ELELEDRQSR 1920
LQQELRERMA VEDHLKTEGE LSEEKKILNE MLEVVEQRDS LVALLEEQRL REKEEDKDLE 1980
AAMLCKGFSL DWS 1993 |
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:0006887; P:exocytosis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |