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Protein

Protein-methionine sulfoxide oxidase MICAL1

Gene

Mical1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 12329FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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
Gene namesi
Name:Mical1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi1309386. Mical1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10471047Protein-methionine sulfoxide oxidase MICAL1PRO_0000416299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei475 – 4751PhosphothreonineCombined sources
Modified residuei616 – 6161PhosphoserineBy similarity
Modified residuei777 – 7771PhosphoserineBy similarity
Modified residuei781 – 7811PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiD3ZBP4.
PRIDEiD3ZBP4.

PTM databases

iPTMnetiD3ZBP4.

Expressioni

Gene expression databases

GenevisibleiD3ZBP4. RN.

Interactioni

Subunit structurei

Interacts with STK38 and STK38L. Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B. Interacts with RAB8A (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000337.

Structurei

3D structure databases

ProteinModelPortaliD3ZBP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini507 – 608102CHPROSITE-ProRule annotationAdd
BLAST
Domaini679 – 74163LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili912 – 99685Sequence analysisAdd
BLAST

Domaini

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

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

eggNOGiKOG1700. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
InParanoidiD3ZBP4.
KOiK19947.
OMAiAYLSHFH.
OrthoDBiEOG769ZHM.
TreeFamiTF324129.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
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.
SSF51905. SSF51905. 2 hits.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: D3ZBP4-1) [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
MASPTSTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLPQYHK
60 70 80 90 100
IKAQLNYWSA KSLWAKLDKR ASQPAYQQGQ ACTNTKCLVV GAGPCGLRAA
110 120 130 140 150
VELALLGARV VLVEKRTKFS RHNVLHLWPF TIHDLRALGA KKFYGRFCTG
160 170 180 190 200
TLDHISIRQL QLLLLKVALL LGVEIHWGFT FTGLQPPPKK GSGWRARIQP
210 220 230 240 250
SPPAQLASYE FDVLISAGGG KFVPEGFTIR EMRGKLAIGI TANFVNGRTV
260 270 280 290 300
EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDD THYFVMTAKK
310 320 330 340 350
QCLLRLGVLR QDLPETDQLL GKANVVPEAL QQFARAAADF ATQGKLGKLE
360 370 380 390 400
FAQDARGRPD VAAFDFTSMM RSESSARIQE KHGARLLLGL VGDCLVEPFW
410 420 430 440 450
PLGTGVARGF LAAFDAAWMV KRWAEGTGPL ELLAERESLY QLLSQTSPEN
460 470 480 490 500
MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ DLYDIMDKEH ARKKSDETDA
510 520 530 540 550
RKTTTGSAGT EELLHWCQEQ TAGFPGVSVT DFSSSWADGR ALCALVHRLQ
560 570 580 590 600
PGLLEPSELQ GMSALEATAW ALRVAEYELG IIPVLSAQAV VAGSDPLGLI
610 620 630 640 650
AYLSHFHSAF KNTPHSSGLV SQPHGTPSAI LFLGKLQRSL QRTRTKVEEE
660 670 680 690 700
TPCTEEPPVS EPSVPPALPS EHEEAGAEDV CELCGKRLYI LERFCVDGHF
710 720 730 740 750
FHRGCFCCRT CEATLRPGGY GQYPGDGYFY CLQHLPQEDQ KEADNNGSPE
760 770 780 790 800
NQELPTPGDS TTQSGPSSPV PPVTEASPVP SPSQPARRLI RLSSVERLRL
810 820 830 840 850
SSLNIIPDSG VEPPPKPPRS CLDLAQESLK SSFMGWGVLR APQVPEAIEK
860 870 880 890 900
GEEEEEEEEE EEEEEEELPP PLALEVEQSL LTLAKNSGDM TKYPTWRRTL
910 920 930 940 950
MRRAKEEEMK RFCKAQAIQR RLNEIEAAMR ELETEGMKLE VALRKESSSP
960 970 980 990 1000
EKQKKLWLEQ LLQLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHEFRG
1010 1020 1030 1040
INREETLKTQ ADRLSEDRVL RKLLDVVNQR DALIQFQEER RLREMPV
Length:1,047
Mass (Da):116,672
Last modified:April 20, 2010 - v1
Checksum:iB74E4A60CBB65A5B
GO
Isoform 2 (identifier: D3ZBP4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-159: Missing.
     192-192: S → N

Show »
Length:974
Mass (Da):108,618
Checksum:iE57042E0598E7B29
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei87 – 15973Missing in isoform 2. CuratedVSP_042607Add
BLAST
Alternative sequencei192 – 1921S → N in isoform 2. CuratedVSP_042608

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474025 Genomic DNA. Translation: EDL99736.1.
RefSeqiNP_001099867.1. NM_001106397.1. [D3ZBP4-1]
UniGeneiRn.106944.

Genome annotation databases

EnsembliENSRNOT00000000337; ENSRNOP00000000337; ENSRNOG00000000307. [D3ZBP4-1]
GeneIDi294520.
KEGGirno:294520.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474025 Genomic DNA. Translation: EDL99736.1.
RefSeqiNP_001099867.1. NM_001106397.1. [D3ZBP4-1]
UniGeneiRn.106944.

3D structure databases

ProteinModelPortaliD3ZBP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000337.

PTM databases

iPTMnetiD3ZBP4.

Proteomic databases

PaxDbiD3ZBP4.
PRIDEiD3ZBP4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000337; ENSRNOP00000000337; ENSRNOG00000000307. [D3ZBP4-1]
GeneIDi294520.
KEGGirno:294520.

Organism-specific databases

CTDi64780.
RGDi1309386. Mical1.

Phylogenomic databases

eggNOGiKOG1700. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
InParanoidiD3ZBP4.
KOiK19947.
OMAiAYLSHFH.
OrthoDBiEOG769ZHM.
TreeFamiTF324129.

Miscellaneous databases

PROiD3ZBP4.

Gene expression databases

GenevisibleiD3ZBP4. RN.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
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.
SSF51905. SSF51905. 2 hits.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMICA1_RAT
AccessioniPrimary (citable) accession number: D3ZBP4
Secondary accession number(s): D3ZJD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 53 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.