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Q8VDP3 (MICA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-methionine sulfoxide oxidase MICAL1

EC=1.14.13.-
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 names
Name:Mical1
Synonyms:Mical, Nical
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1048 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Catalytic activity

[protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O. Ref.6

Cofactor

FAD.

Subunit structure

Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B By similarity. Interacts with STK38 and STK38L. Interacts with RAB8A. Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity.

Domain

The C-terminal coiled coil part contains the plexin-interacting region.

Sequence similarities

Belongs to the Mical family.

Contains 1 CH (calponin-homology) domain.

Contains 1 LIM zinc-binding domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
LIM domain
   LigandActin-binding
FAD
Flavoprotein
Metal-binding
NADP
Zinc
   Molecular functionMonooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament depolymerization

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

oxidation-reduction process

Inferred from sequence or structural similarity. Source: UniProtKB

sulfur oxidation

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionFAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

Rab GTPase binding

Inferred from physical interaction Ref.4. Source: UniProtKB

SH3 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

actin binding

Inferred from direct assay Ref.6. Source: UniProtKB

monooxygenase activity

Inferred from mutant phenotype PubMed 16275926. 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

Inferred from direct assay Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Stk38Q91VJ49EBI-4394891,EBI-2527046
Stk38lA4GW502EBI-4394891,EBI-4404035From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VDP3-1)

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.
Isoform 2 (identifier: Q8VDP3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-159: Missing.
Isoform 3 (identifier: Q8VDP3-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10481048Protein-methionine sulfoxide oxidase MICAL1
PRO_0000075843

Regions

Domain507 – 608102CH
Domain681 – 74363LIM zinc-binding
Nucleotide binding95 – 12329FAD
Region1 – 489489Monooxygenase domain
Coiled coil847 – 86721 Potential
Coiled coil906 – 94944 Potential
Coiled coil974 – 103158 Potential

Sites

Binding site951FAD
Binding site1141FAD
Binding site1161FAD
Binding site1211FAD
Binding site1231FAD
Binding site3931FAD

Amino acid modifications

Modified residue6161Phosphoserine By similarity

Natural variations

Alternative sequence87 – 15973Missing in isoform 2.
VSP_042591
Alternative sequence1921S → D in isoform 3.
VSP_042592

Experimental info

Sequence conflict8711P → H in BAE35027. Ref.1

Secondary structure

............................................................................................. 1048
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C31A392A4AE222FC

FASTA1,048116,785
        10         20         30         40         50         60 
MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA 

        70         80         90        100        110        120 
KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS 

       130        140        150        160        170        180 
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK 

       190        200        210        220        230        240 
FTGLQPPPRK GSGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI 

       250        260        270        280        290        300 
TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK 

       310        320        330        340        350        360 
QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD 

       370        380        390        400        410        420 
VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 

       430        440        450        460        470        480 
KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ 

       490        500        510        520        530        540 
DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL 

       550        560        570        580        590        600 
ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI 

       610        620        630        640        650        660 
AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS 

       670        680        690        700        710        720 
EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG 

       730        740        750        760        770        780 
GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP 

       790        800        810        820        830        840 
SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV 

       850        860        870        880        890        900 
QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL 

       910        920        930        940        950        960 
MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ 

       970        980        990       1000       1010       1020 
LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV 

      1030       1040 
LRKLLEVVNQ RDALIQFQEE RRLREMPA 

« Hide

Isoform 2 [UniParc].

Checksum: B2D2BF964B034CBC
Show »

FASTA975108,692
Isoform 3 [UniParc].

Checksum: AF50CC8B1FBBBAE2
Show »

FASTA1,048116,813

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Mammary tumor.
[4]"The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions."
Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.
Mol. Biol. Cell 19:971-983(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB8A.
[5]"MICAL-1 is a negative regulator of MST-NDR kinase signaling and apoptosis."
Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C., Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J.
Mol. Cell. Biol. 31:3603-3615(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STK38 AND STK38L.
[6]"MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[7]"High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule."
Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., Stuart D.I., Terman J.R., Kolodkin A.L., Pasterkamp R.J., Jones E.Y.
Proc. Natl. Acad. Sci. U.S.A. 102:16836-16841(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-489 IN COMPLEX WITH FAD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS35888.1. [Q8VDP3-1]
CCDS48547.1. [Q8VDP3-2]
RefSeqNP_001157905.1. NM_001164433.1. [Q8VDP3-2]
NP_612188.1. NM_138315.2. [Q8VDP3-1]
UniGeneMm.290431.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRAX-ray2.00A/B1-484[»]
2BRYX-ray1.45A/B1-489[»]
2C4CX-ray2.90A/B1-489[»]
ProteinModelPortalQ8VDP3.
SMRQ8VDP3. Positions 7-489, 506-612, 673-741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8VDP3. 4 interactions.
STRING10090.ENSMUSP00000019967.

PTM databases

PhosphoSiteQ8VDP3.

Proteomic databases

MaxQBQ8VDP3.
PaxDbQ8VDP3.
PRIDEQ8VDP3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823. [Q8VDP3-1]
ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823. [Q8VDP3-2]
ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823. [Q8VDP3-3]
GeneID171580.
KEGGmmu:171580.
UCSCuc007exn.2. mouse. [Q8VDP3-1]
uc007exp.2. mouse. [Q8VDP3-2]

Organism-specific databases

CTD64780.
MGIMGI:2385847. Mical1.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00640000091174.
HOGENOMHOG000047263.
HOVERGENHBG052474.
OMAKQCLLRL.
OrthoDBEOG769ZHM.
TreeFamTF324129.

Gene expression databases

ArrayExpressQ8VDP3.
BgeeQ8VDP3.
GenevestigatorQ8VDP3.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProIPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. mOase_FAD-bd.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMICAL1. mouse.
EvolutionaryTraceQ8VDP3.
NextBio371076.
PROQ8VDP3.
SOURCESearch...

Entry information

Entry nameMICA1_MOUSE
AccessionPrimary (citable) accession number: Q8VDP3
Secondary accession number(s): D3Z4C6 expand/collapse secondary AC list , E9PXR1, Q3TB77, Q3TBH9, Q3TX89
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot