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Protein

[F-actin]-methionine sulfoxide oxidase MICAL1

Gene

Mical1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of sectrory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels. May act as Rab effector protein and play a role in vesicle trafficking.By similarity3 Publications

Catalytic activityi

[F-actin]-L-methionine + NADPH + O2 + H+ = [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O.1 Publication

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei95FAD1 Publication1
Binding sitei114FAD1 Publication1
Binding sitei116FAD1 Publication1
Binding sitei121FAD1 Publication1
Binding sitei123FAD1 Publication1
Binding sitei393FAD1 Publication1
Metal bindingi683Zinc 1By similarity1
Metal bindingi686Zinc 1By similarity1
Metal bindingi704Zinc 1; via pros nitrogenBy similarity1
Metal bindingi707Zinc 1By similarity1
Metal bindingi710Zinc 2By similarity1
Metal bindingi713Zinc 2By similarity1
Metal bindingi733Zinc 2By similarity1
Metal bindingi736Zinc 2; via pros nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi95 – 123FAD1 PublicationAdd BLAST29

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • FAD binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • monooxygenase activity Source: MGI
  • 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 Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

GO - Biological processi

  • actin filament depolymerization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • regulation of regulated secretory pathway Source: UniProtKB
  • sulfur oxidation Source: UniProtKB

Keywordsi

Molecular functionActin-binding, Monooxygenase, Oxidoreductase
LigandFAD, Flavoprotein, Metal-binding, NADP, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
[F-actin]-methionine sulfoxide oxidase MICAL1 (EC:1.14.13.2251 Publication)
Alternative name(s):
Molecule interacting with CasL protein 1
Short name:
MICAL-1
Short name:
mMical1
NEDD9-interacting protein with calponin homology and LIM domains
Gene namesi
Name:Mical1
Synonyms:Mical, Nical
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2385847. Mical1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000758431 – 1048[F-actin]-methionine sulfoxide oxidase MICAL1Add BLAST1048

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei475PhosphothreonineBy similarity1
Modified residuei616PhosphoserineBy similarity1
Modified residuei777PhosphoserineCombined sources1
Modified residuei781PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8VDP3.
PeptideAtlasiQ8VDP3.
PRIDEiQ8VDP3.

PTM databases

iPTMnetiQ8VDP3.
PhosphoSitePlusiQ8VDP3.

Expressioni

Tissue specificityi

Expressed in the postnatal and adult hippocampus; found in dentate gyrus, the polymorphic layer, cornu ammonis (CA) 1-3 and in mossy fibers of the striatum lucidum. In adult hippocampus strongly expressed in CA3 pyramidial neurons.1 Publication

Gene expression databases

BgeeiENSMUSG00000019823.
ExpressionAtlasiQ8VDP3. baseline and differential.
GenevisibleiQ8VDP3. MM.

Interactioni

Subunit structurei

Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB1B is of low affinity compared to other Rab proteins; at least in case of RAB8A and RAB10 can bind 2 molecules of the Rab proteins simultaneously (By similarity). Interacts with STK38 and STK38L.By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ8VDP3. 4 interactors.
STRINGi10090.ENSMUSP00000019967.

Structurei

Secondary structure

11048
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 19Combined sources11
Helixi23 – 37Combined sources15
Helixi44 – 53Combined sources10
Turni58 – 60Combined sources3
Helixi61 – 71Combined sources11
Helixi74 – 79Combined sources6
Turni80 – 84Combined sources5
Beta strandi86 – 90Combined sources5
Helixi94 – 105Combined sources12
Beta strandi109 – 115Combined sources7
Beta strandi124 – 126Combined sources3
Helixi129 – 136Combined sources8
Turni137 – 139Combined sources3
Helixi140 – 143Combined sources4
Turni145 – 148Combined sources4
Beta strandi154 – 156Combined sources3
Helixi157 – 170Combined sources14
Beta strandi174 – 178Combined sources5
Beta strandi180 – 185Combined sources6
Beta strandi194 – 200Combined sources7
Helixi204 – 207Combined sources4
Beta strandi211 – 216Combined sources6
Beta strandi228 – 233Combined sources6
Beta strandi238 – 245Combined sources8
Helixi250 – 253Combined sources4
Beta strandi258 – 262Combined sources5
Turni263 – 266Combined sources4
Helixi269 – 277Combined sources9
Beta strandi281 – 298Combined sources18
Helixi300 – 305Combined sources6
Beta strandi308 – 311Combined sources4
Helixi316 – 319Combined sources4
Turni322 – 324Combined sources3
Helixi327 – 341Combined sources15
Turni342 – 346Combined sources5
Beta strandi357 – 359Combined sources3
Beta strandi361 – 365Combined sources5
Beta strandi367 – 373Combined sources7
Beta strandi375 – 381Combined sources7
Beta strandi384 – 390Combined sources7
Helixi392 – 394Combined sources3
Helixi400 – 402Combined sources3
Helixi405 – 424Combined sources20
Helixi429 – 440Combined sources12
Helixi441 – 445Combined sources5
Turni448 – 450Combined sources3
Helixi455 – 457Combined sources3
Helixi462 – 464Combined sources3
Beta strandi466 – 468Combined sources3
Helixi476 – 482Combined sources7
Beta strandi483 – 485Combined sources3
Helixi508 – 520Combined sources13
Turni521 – 523Combined sources3
Beta strandi531 – 533Combined sources3
Helixi534 – 536Combined sources3
Helixi540 – 549Combined sources10
Helixi564 – 579Combined sources16
Helixi587 – 592Combined sources6
Helixi596 – 610Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BRAX-ray2.00A/B1-484[»]
2BRYX-ray1.45A/B1-489[»]
2C4CX-ray2.90A/B1-489[»]
4TXIX-ray2.31A2-615[»]
4TXKX-ray2.88A2-615[»]
ProteinModelPortaliQ8VDP3.
SMRiQ8VDP3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VDP3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini507 – 608Calponin-homology (CH)PROSITE-ProRule annotationAdd BLAST102
Domaini681 – 743LIM zinc-bindingPROSITE-ProRule annotationAdd BLAST63

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 489Monooxygenase domainAdd BLAST489
Regioni906 – 1048RAB-binding domain (RBD)By similarityAdd BLAST143

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili847 – 867Sequence analysisAdd BLAST21
Coiled coili906 – 949Sequence analysisAdd BLAST44
Coiled coili974 – 1031Sequence analysisAdd BLAST58

Domaini

The C-terminal coiled coil part contains the plexin-interacting region.
The C-terminal RAB-binding domain (RBD), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound forms).By similarity

Sequence similaritiesi

Belongs to the Mical family.Curated

Keywords - Domaini

Coiled coil, LIM domain

Phylogenomic databases

eggNOGiKOG1700. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000047263.
HOVERGENiHBG052474.
InParanoidiQ8VDP3.
KOiK19947.
OMAiFYCLQHL.
OrthoDBiEOG091G009H.
TreeFamiTF324129.

Family and domain databases

CDDicd00014. CH. 1 hit.
Gene3Di1.10.418.10. 1 hit.
3.50.50.60. 1 hit.
InterProiView protein in InterPro
IPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR029937. MICAL1.
IPR001781. Znf_LIM.
PANTHERiPTHR11915:SF387. PTHR11915:SF387. 1 hit.
PfamiView protein in Pfam
PF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
SMARTiView protein in SMART
SM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF51905. SSF51905. 2 hits.
PROSITEiView protein in PROSITE
PS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VDP3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK
60 70 80 90 100
IKAQLNYWSA KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA
110 120 130 140 150
VELALLGARV VLVEKRIKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG
160 170 180 190 200
TLDHISIRQL QLLLLKVALL LGVEIHWGVK FTGLQPPPRK GSGWRAQLQP
210 220 230 240 250
NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI TANFVNGRTV
260 270 280 290 300
EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK
310 320 330 340 350
QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE
360 370 380 390 400
FAQDARGRPD VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW
410 420 430 440 450
PLGTGVARGF LAAFDAAWMV KRWAEGAGPL EVLAERESLY QLLSQTSPEN
460 470 480 490 500
MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ DLYDMMDKEH AQRKSDEPDS
510 520 530 540 550
RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL ALCALVHHLQ
560 570 580 590 600
PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI
610 620 630 640 650
AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE
660 670 680 690 700
TPSTEEPPVS EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG
710 720 730 740 750
HFFHRSCFCC HTCEATLWPG GYGQHPGDGH FYCLQHLPQE DQKEADNNGS
760 770 780 790 800
LESQELPTPG DSNMQPDPSS PPVTRVSPVP SPSQPARRLI RLSSLERLRL
810 820 830 840 850
SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV QAPQVPEAIE
860 870 880 890 900
KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL
910 920 930 940 950
MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP
960 970 980 990 1000
EQQKKLWLDQ LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG
1010 1020 1030 1040
YMNREETMKT EADLQSENQV LRKLLEVVNQ RDALIQFQEE RRLREMPA
Length:1,048
Mass (Da):116,785
Last modified:March 1, 2002 - v1
Checksum:iC31A392A4AE222FC
GO
Isoform 2 (identifier: Q8VDP3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-159: Missing.

Show »
Length:975
Mass (Da):108,692
Checksum:iB2D2BF964B034CBC
GO
Isoform 3 (identifier: Q8VDP3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: S → D

Show »
Length:1,048
Mass (Da):116,813
Checksum:iAF50CC8B1FBBBAE2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti871P → H in BAE35027 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04259187 – 159Missing in isoform 2. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_042592192S → D in isoform 3. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK159369 mRNA. Translation: BAE35027.1.
AK170881 mRNA. Translation: BAE42090.1.
AK171234 mRNA. Translation: BAE42330.1.
AK171411 mRNA. Translation: BAE42437.1.
AK171429 mRNA. Translation: BAE42447.1.
AK171479 mRNA. Translation: BAE42481.1.
AC153360 Genomic DNA. No translation available.
BC021477 mRNA. Translation: AAH21477.1.
BC034682 mRNA. Translation: AAH34682.1.
CCDSiCCDS35888.1. [Q8VDP3-1]
CCDS48547.1. [Q8VDP3-2]
RefSeqiNP_001157905.1. NM_001164433.1. [Q8VDP3-2]
NP_612188.1. NM_138315.2. [Q8VDP3-1]
XP_011241439.1. XM_011243137.2. [Q8VDP3-1]
UniGeneiMm.290431.

Genome annotation databases

EnsembliENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823. [Q8VDP3-1]
ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823. [Q8VDP3-2]
ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823. [Q8VDP3-3]
GeneIDi171580.
KEGGimmu:171580.
UCSCiuc007exn.2. mouse. [Q8VDP3-1]
uc007exp.2. mouse. [Q8VDP3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiMICA1_MOUSE
AccessioniPrimary (citable) accession number: Q8VDP3
Secondary accession number(s): D3Z4C6
, E9PXR1, Q3TB77, Q3TBH9, Q3TX89
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2002
Last modified: September 27, 2017
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families