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Q8VDP3

- MICA1_MOUSE

UniProt

Q8VDP3 - MICA1_MOUSE

Protein

Protein-methionine sulfoxide oxidase MICAL1

Gene

Mical1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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/STK4.2 Publications

    Catalytic activityi

    [protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.1 Publication

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951FAD1 Publication
    Binding sitei114 – 1141FAD1 Publication
    Binding sitei116 – 1161FAD1 Publication
    Binding sitei121 – 1211FAD1 Publication
    Binding sitei123 – 1231FAD1 Publication
    Binding sitei393 – 3931FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 12329FAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. FAD binding Source: UniProtKB
    3. monooxygenase activity Source: MGI
    4. 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
    5. protein binding Source: IntAct
    6. Rab GTPase binding Source: UniProtKB
    7. SH3 domain binding Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament depolymerization Source: UniProtKB
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    4. negative regulation of protein phosphorylation Source: UniProtKB
    5. oxidation-reduction process Source: UniProtKB
    6. sulfur oxidation Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Actin-binding, FAD, Flavoprotein, Metal-binding, NADP, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Mical1
    Synonyms:Mical, Nical
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:2385847. Mical1.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10481048Protein-methionine sulfoxide oxidase MICAL1PRO_0000075843Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei616 – 6161PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8VDP3.
    PaxDbiQ8VDP3.
    PRIDEiQ8VDP3.

    PTM databases

    PhosphoSiteiQ8VDP3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VDP3.
    BgeeiQ8VDP3.
    GenevestigatoriQ8VDP3.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Stk38Q91VJ49EBI-4394891,EBI-2527046
    Stk38lA4GW502EBI-4394891,EBI-4404035From a different organism.

    Protein-protein interaction databases

    IntActiQ8VDP3. 4 interactions.
    STRINGi10090.ENSMUSP00000019967.

    Structurei

    Secondary structure

    1
    1048
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1911
    Helixi23 – 3715
    Helixi44 – 5310
    Turni58 – 603
    Helixi61 – 7111
    Helixi74 – 796
    Turni80 – 845
    Beta strandi86 – 905
    Helixi94 – 10512
    Beta strandi109 – 1157
    Beta strandi124 – 1263
    Helixi129 – 1368
    Turni137 – 1393
    Helixi140 – 1434
    Turni145 – 1484
    Beta strandi154 – 1563
    Helixi157 – 17014
    Beta strandi174 – 1785
    Beta strandi180 – 1856
    Beta strandi194 – 2007
    Helixi204 – 2074
    Beta strandi211 – 2166
    Beta strandi228 – 2336
    Beta strandi238 – 2458
    Helixi250 – 2534
    Turni263 – 2664
    Helixi269 – 2779
    Beta strandi281 – 29818
    Helixi300 – 3056
    Beta strandi308 – 3114
    Helixi316 – 3194
    Turni322 – 3243
    Helixi327 – 34115
    Turni342 – 3465
    Beta strandi357 – 3593
    Beta strandi361 – 3655
    Beta strandi367 – 3737
    Beta strandi375 – 3817
    Beta strandi384 – 3907
    Helixi392 – 3943
    Helixi400 – 4023
    Helixi405 – 42420
    Helixi429 – 44012
    Helixi441 – 4455
    Turni448 – 4503
    Helixi455 – 4573
    Helixi462 – 4643
    Beta strandi466 – 4683
    Helixi476 – 4827
    Beta strandi483 – 4853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BRAX-ray2.00A/B1-484[»]
    2BRYX-ray1.45A/B1-489[»]
    2C4CX-ray2.90A/B1-489[»]
    ProteinModelPortaliQ8VDP3.
    SMRiQ8VDP3. Positions 7-489, 506-612, 673-741.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8VDP3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini507 – 608102CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini681 – 74363LIM zinc-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 489489Monooxygenase domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili847 – 86721Sequence AnalysisAdd
    BLAST
    Coiled coili906 – 94944Sequence AnalysisAdd
    BLAST
    Coiled coili974 – 103158Sequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the Mical family.Curated
    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, LIM domain

    Phylogenomic databases

    eggNOGiCOG5069.
    GeneTreeiENSGT00640000091174.
    HOGENOMiHOG000047263.
    HOVERGENiHBG052474.
    OMAiKQCLLRL.
    OrthoDBiEOG769ZHM.
    TreeFamiTF324129.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProiIPR001715. CH-domain.
    IPR022735. DUF3585.
    IPR002938. mOase_FAD-bd.
    IPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00307. CH. 1 hit.
    PF12130. DUF3585. 1 hit.
    PF01494. FAD_binding_3. 1 hit.
    PF00412. LIM. 1 hit.
    [Graphical view]
    SMARTiSM00033. CH. 1 hit.
    SM00132. LIM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS50021. CH. 1 hit.
    PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK     50
    IKAQLNYWSA KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA 100
    VELALLGARV VLVEKRIKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG 150
    TLDHISIRQL QLLLLKVALL LGVEIHWGVK FTGLQPPPRK GSGWRAQLQP 200
    NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI TANFVNGRTV 250
    EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK 300
    QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE 350
    FAQDARGRPD VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW 400
    PLGTGVARGF LAAFDAAWMV KRWAEGAGPL EVLAERESLY QLLSQTSPEN 450
    MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ DLYDMMDKEH AQRKSDEPDS 500
    RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL ALCALVHHLQ 550
    PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI 600
    AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE 650
    TPSTEEPPVS EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG 700
    HFFHRSCFCC HTCEATLWPG GYGQHPGDGH FYCLQHLPQE DQKEADNNGS 750
    LESQELPTPG DSNMQPDPSS PPVTRVSPVP SPSQPARRLI RLSSLERLRL 800
    SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV QAPQVPEAIE 850
    KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL 900
    MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP 950
    EQQKKLWLDQ LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG 1000
    YMNREETMKT EADLQSENQV LRKLLEVVNQ RDALIQFQEE RRLREMPA 1048
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti871 – 8711P → H in BAE35027. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei87 – 15973Missing in isoform 2. 1 PublicationVSP_042591Add
    BLAST
    Alternative sequencei192 – 1921S → D in isoform 3. CuratedVSP_042592

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS35888.1. [Q8VDP3-1 ]
    CCDS48547.1. [Q8VDP3-2 ]
    RefSeqi NP_001157905.1. NM_001164433.1. [Q8VDP3-2 ]
    NP_612188.1. NM_138315.2. [Q8VDP3-1 ]
    UniGenei Mm.290431.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BRA X-ray 2.00 A/B 1-484 [» ]
    2BRY X-ray 1.45 A/B 1-489 [» ]
    2C4C X-ray 2.90 A/B 1-489 [» ]
    ProteinModelPortali Q8VDP3.
    SMRi Q8VDP3. Positions 7-489, 506-612, 673-741.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8VDP3. 4 interactions.
    STRINGi 10090.ENSMUSP00000019967.

    PTM databases

    PhosphoSitei Q8VDP3.

    Proteomic databases

    MaxQBi Q8VDP3.
    PaxDbi Q8VDP3.
    PRIDEi Q8VDP3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019967 ; ENSMUSP00000019967 ; ENSMUSG00000019823 . [Q8VDP3-1 ]
    ENSMUST00000099934 ; ENSMUSP00000097519 ; ENSMUSG00000019823 . [Q8VDP3-2 ]
    ENSMUST00000119962 ; ENSMUSP00000113783 ; ENSMUSG00000019823 . [Q8VDP3-3 ]
    GeneIDi 171580.
    KEGGi mmu:171580.
    UCSCi uc007exn.2. mouse. [Q8VDP3-1 ]
    uc007exp.2. mouse. [Q8VDP3-2 ]

    Organism-specific databases

    CTDi 64780.
    MGIi MGI:2385847. Mical1.

    Phylogenomic databases

    eggNOGi COG5069.
    GeneTreei ENSGT00640000091174.
    HOGENOMi HOG000047263.
    HOVERGENi HBG052474.
    OMAi KQCLLRL.
    OrthoDBi EOG769ZHM.
    TreeFami TF324129.

    Miscellaneous databases

    ChiTaRSi MICAL1. mouse.
    EvolutionaryTracei Q8VDP3.
    NextBioi 371076.
    PROi Q8VDP3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VDP3.
    Bgeei Q8VDP3.
    Genevestigatori Q8VDP3.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    2.10.110.10. 1 hit.
    InterProi IPR001715. CH-domain.
    IPR022735. DUF3585.
    IPR002938. mOase_FAD-bd.
    IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00307. CH. 1 hit.
    PF12130. DUF3585. 1 hit.
    PF01494. FAD_binding_3. 1 hit.
    PF00412. LIM. 1 hit.
    [Graphical view ]
    SMARTi SM00033. CH. 1 hit.
    SM00132. LIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS50021. CH. 1 hit.
    PS00478. LIM_DOMAIN_1. 1 hit.
    PS50023. LIM_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiMICA1_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDP3
    Secondary accession number(s): D3Z4C6
    , E9PXR1, Q3TB77, Q3TBH9, Q3TX89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [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

    External Data

    Dasty 3