MICA2_MOUSE
ID MICA2_MOUSE Reviewed; 1951 AA.
AC Q8BML1; B1B545; F6ZD54; F8WJF1; Q14DP1; Q3TR48; Q3UPU6; Q5DU17; Q8CID1;
AC Q9D5U9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=[F-actin]-monooxygenase MICAL2 {ECO:0000305};
DE EC=1.14.13.225 {ECO:0000269|PubMed:23911929, ECO:0000269|PubMed:23927065};
DE AltName: Full=ERK2-binding testicular protein 1 {ECO:0000303|PubMed:18241670};
DE AltName: Full=MICAL C-terminal-like protein;
DE Short=Mical-cL;
DE AltName: Full=Molecule interacting with CasL protein 2;
DE Short=MICAL-2;
DE Short=mMical2;
GN Name=Mical2 {ECO:0000312|MGI:MGI:2444947};
GN Synonyms=Kiaa0750 {ECO:0000303|Ref.1}, Micalcl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1361-1951 (ISOFORM 7).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Eye, Pituitary, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1173-1951 (ISOFORM 5), INTERACTION WITH
RP MAPK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP REGION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=18241670; DOI=10.1016/j.bbrc.2008.01.078;
RA Miura K., Imaki J.;
RT "Molecular cloning of Ebitein1: a novel extracellular signal-regulated
RT kinase 2-binding protein in testis.";
RL Biochem. Biophys. Res. Commun. 368:336-342(2008).
RN [6]
RP INTERACTION WITH PLXNA4.
RX PubMed=12110185; DOI=10.1016/s0092-8674(02)00794-8;
RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.;
RT "MICALs, a family of conserved flavoprotein oxidoreductases, function in
RT plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [7]
RP INTERACTION WITH MAPK1, AND MUTAGENESIS OF 1319-ARG--ARG-1322.
RX PubMed=18590835; DOI=10.1016/j.bbapap.2008.05.015;
RA Miura K., Imaki J.;
RT "Identification of ERK2-binding domain of EBITEIN1, a novel ERK2-binding
RT protein.";
RL Biochim. Biophys. Acta 1784:1319-1325(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ENZYME KINETICS.
RX PubMed=23927065; DOI=10.1021/bi4008462;
RA McDonald C.A., Liu Y.Y., Palfey B.A.;
RT "Actin stimulates reduction of the MICAL-2 monooxygenase domain.";
RL Biochemistry 52:6076-6084(2013).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA Gladyshev V.N.;
RT "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT reversible stereoselective methionine oxidation.";
RL Mol. Cell 51:397-404(2013).
CC -!- FUNCTION: Methionine monooxygenase that promotes depolymerization of F-
CC actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin
CC to form methionine-sulfoxide, resulting in actin filament disassembly
CC and preventing repolymerization (PubMed:23911929, PubMed:23927065).
CC Regulates the disassembly of branched actin networks also by oxidizing
CC ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from
CC the network. Acts as a key regulator of the SRF signaling pathway
CC elicited by nerve growth factor and serum: mediates oxidation and
CC subsequent depolymerization of nuclear actin, leading to increase
CC MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-
CC dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through
CC RhoA (By similarity). {ECO:0000250|UniProtKB:O94851,
CC ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:23911929,
CC ECO:0000269|PubMed:23927065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.225; Evidence={ECO:0000269|PubMed:23911929,
CC ECO:0000269|PubMed:23927065};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8TDZ2};
CC -!- SUBUNIT: Interacts with PLXNA4 (PubMed:12110185). Interacts with RAB1B
CC (By similarity). Interacts with MAPK1/ERK2 (PubMed:18241670,
CC PubMed:18590835). Interacts with RAB1B, RAB35, RAB8A, RAB10, RAB13 and
CC RAB15 (in their GTP-bound forms); binding to RAB1B and RAB35 is of low
CC affinity compared to other Rab proteins; binding to RAB1B and RAB35 is
CC of low affinity compared to other Rab proteins; at least in case of
CC RAB8A may bind 2 molecules of RAB8A simultaneously through a high and a
CC low affinity binding site, respectively (By similarity).
CC {ECO:0000250|UniProtKB:O94851, ECO:0000269|PubMed:12110185,
CC ECO:0000269|PubMed:18241670, ECO:0000269|PubMed:18590835}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18241670}. Nucleus
CC {ECO:0000250|UniProtKB:O94851}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=4;
CC IsoId=Q8BML1-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8BML1-1; Sequence=VSP_061301, VSP_061305, VSP_061309;
CC Name=2;
CC IsoId=Q8BML1-2; Sequence=VSP_061302, VSP_061306, VSP_061307;
CC Name=3;
CC IsoId=Q8BML1-3; Sequence=VSP_061301, VSP_061303, VSP_061304;
CC Name=5; Synonyms=Ebitein1 {ECO:0000303|PubMed:18241670};
CC IsoId=Q8BML1-5; Sequence=VSP_061310, VSP_061311, VSP_061314;
CC Name=6;
CC IsoId=Q8BML1-6; Sequence=VSP_061300, VSP_061308, VSP_061310,
CC VSP_061311, VSP_061312, VSP_061313;
CC Name=7;
CC IsoId=Q8BML1-7; Sequence=VSP_061311;
CC -!- TISSUE SPECIFICITY: Expressed only in testis (at protein level).
CC {ECO:0000269|PubMed:18241670}.
CC -!- DEVELOPMENTAL STAGE: During spermatogenesis, first expressed after
CC meiosis, gradually increases to a maximum at Oakberg's stage 9 and then
CC decreases until it is undetectable when spermatozoa begin to generate
CC flagella (at protein level). {ECO:0000269|PubMed:18241670}.
CC -!- DOMAIN: The C-terminal RAB-binding domain (RBD)(1796-1945), also
CC described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their
CC GTP-bound forms). {ECO:0000250|UniProtKB:O94851}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90416.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG12802.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220353; BAD90416.1; ALT_INIT; mRNA.
DR EMBL; AK014911; BAB29617.1; ALT_INIT; mRNA.
DR EMBL; AK030608; BAC27044.1; -; mRNA.
DR EMBL; AK138935; BAE23824.1; -; mRNA.
DR EMBL; AK143191; BAE25298.1; -; mRNA.
DR EMBL; AK163078; BAE37182.1; -; mRNA.
DR EMBL; AC100153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031386; AAH31386.1; -; mRNA.
DR EMBL; BC111895; AAI11896.1; -; mRNA.
DR EMBL; BC112415; AAI12416.1; -; mRNA.
DR EMBL; AB359922; BAG12802.1; ALT_INIT; mRNA.
DR CCDS; CCDS21753.1; -. [Q8BML1-1]
DR CCDS; CCDS57581.1; -. [Q8BML1-2]
DR RefSeq; NP_001180234.1; NM_001193305.1. [Q8BML1-2]
DR RefSeq; NP_796256.1; NM_177282.5. [Q8BML1-1]
DR RefSeq; XP_006508017.1; XM_006507954.1. [Q8BML1-2]
DR AlphaFoldDB; Q8BML1; -.
DR BioGRID; 236364; 4.
DR STRING; 10090.ENSMUSP00000051163; -.
DR iPTMnet; Q8BML1; -.
DR PhosphoSitePlus; Q8BML1; -.
DR jPOST; Q8BML1; -.
DR MaxQB; Q8BML1; -.
DR PaxDb; Q8BML1; -.
DR PeptideAtlas; Q8BML1; -.
DR PRIDE; Q8BML1; -.
DR ProteomicsDB; 252555; -. [Q8BML1-1]
DR ProteomicsDB; 252556; -. [Q8BML1-2]
DR ProteomicsDB; 252557; -. [Q8BML1-3]
DR ProteomicsDB; 252558; -.
DR ProteomicsDB; 252559; -.
DR Antibodypedia; 24509; 162 antibodies from 24 providers.
DR DNASU; 320878; -.
DR Ensembl; ENSMUST00000033033; ENSMUSP00000033033; ENSMUSG00000038244. [Q8BML1-6]
DR Ensembl; ENSMUST00000037991; ENSMUSP00000047639; ENSMUSG00000038244. [Q8BML1-2]
DR Ensembl; ENSMUST00000050149; ENSMUSP00000051163; ENSMUSG00000038244. [Q8BML1-1]
DR GeneID; 320878; -.
DR KEGG; mmu:320878; -.
DR UCSC; uc009jgm.2; mouse. [Q8BML1-3]
DR UCSC; uc009jgn.2; mouse. [Q8BML1-4]
DR UCSC; uc009jgo.2; mouse. [Q8BML1-2]
DR CTD; 9645; -.
DR MGI; MGI:2444947; Mical2.
DR VEuPathDB; HostDB:ENSMUSG00000038244; -.
DR eggNOG; ENOG502QWDX; Eukaryota.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158780; -.
DR HOGENOM; CLU_000329_0_1_1; -.
DR InParanoid; Q8BML1; -.
DR OMA; HVRDNAY; -.
DR OrthoDB; 1029138at2759; -.
DR TreeFam; TF324129; -.
DR TreeFam; TF336446; -.
DR BRENDA; 1.14.13.225; 3474.
DR BioGRID-ORCS; 100504195; 2 hits in 75 CRISPR screens.
DR BioGRID-ORCS; 320878; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mical2; mouse.
DR ChiTaRS; Micalcl; mouse.
DR PRO; PR:Q9D5U9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BML1; protein.
DR Bgee; ENSMUSG00000038244; Expressed in dentate gyrus of hippocampal formation granule cell and 195 other tissues.
DR ExpressionAtlas; Q8BML1; baseline and differential.
DR Genevisible; Q8BML1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IDA:UniProtKB.
DR GO; GO:0043914; F:NADPH:sulfur oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; 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; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; ISS:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR029939; MICAL2.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF39; PTHR23167:SF39; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW LIM domain; Metal-binding; Monooxygenase; NADP; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1951
FT /note="[F-actin]-monooxygenase MICAL2"
FT /id="PRO_0000075845"
FT DOMAIN 516..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 991..1053
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 2..494
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 663..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1353
FT /note="Interaction with MAPK1"
FT /evidence="ECO:0000269|PubMed:18241670"
FT REGION 1348..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1747..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..681
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 664..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 116..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 123..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 993
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1014
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1023
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1046
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94851"
FT MOD_RES 1683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A1F2"
FT VAR_SEQ 1..1185
FT /note="Missing (in isoform 6)"
FT /id="VSP_061300"
FT VAR_SEQ 737..976
FT /note="Missing (in isoform 1 and isoform 3)"
FT /id="VSP_061301"
FT VAR_SEQ 928..940
FT /note="Missing (in isoform 2)"
FT /id="VSP_061302"
FT VAR_SEQ 1040..1055
FT /note="KFYCKPHFVHCKTSSK -> NPRGQESTSLWPWSQM (in isoform 3)"
FT /id="VSP_061303"
FT VAR_SEQ 1056..1951
FT /note="Missing (in isoform 3)"
FT /id="VSP_061304"
FT VAR_SEQ 1103..1200
FT /note="DEPISPKKPKSVPEPNPRDVEAEATSPRPSEWTSVRISPGEDTVRQDVLAVR
FT VLVTSEDSSSDTESDYGSITAPCAGAYEERPQLPESPPLSKPLTRH -> GTSTSFFRK
FT ALSWPLRLTRGLLNLPQSLLRWMQGLQEAAGHHVRDNAHNYCFMFELLSLGLLLLWAFS
FT KVLAAMYRESEESLENIRSWLLRFIPVKLQ (in isoform 1)"
FT /id="VSP_061305"
FT VAR_SEQ 1103..1115
FT /note="DEPISPKKPKSVP -> VRFSLPVLHPLLG (in isoform 2)"
FT /id="VSP_061306"
FT VAR_SEQ 1116..1951
FT /note="Missing (in isoform 2)"
FT /id="VSP_061307"
FT VAR_SEQ 1186..1222
FT /note="QLPESPPLSKPLTRHISLRENLTQPVSLLHEEPQALP -> MARRPDSRRQA
FT AVAARARSWELTSPIANTKQKVNGKK (in isoform 6)"
FT /id="VSP_061308"
FT VAR_SEQ 1201..1951
FT /note="Missing (in isoform 1)"
FT /id="VSP_061309"
FT VAR_SEQ 1298
FT /note="T -> PA (in isoform 5 and isoform 6)"
FT /id="VSP_061310"
FT VAR_SEQ 1723..1743
FT /note="RKLEGGEGGSSLVSSLVLVSD -> H (in isoform 5, isoform 7
FT and isoform 6)"
FT /id="VSP_061311"
FT VAR_SEQ 1801..1816
FT /note="AIQRQLEEVEERQRTL -> VCILQSEASAWPWPSS (in isoform 6)"
FT /id="VSP_061312"
FT VAR_SEQ 1817..1951
FT /note="Missing (in isoform 6)"
FT /id="VSP_061313"
FT VAR_SEQ 1832
FT /note="Missing (in isoform 5)"
FT /id="VSP_061314"
FT MUTAGEN 1319..1322
FT /note="RRAR->AAAA,AAAR,ARAR,RAAR: Abolishes interaction
FT with MAPK1."
FT /evidence="ECO:0000269|PubMed:18590835"
FT CONFLICT 1362
FT /note="S -> C (in Ref. 2; BAB29617)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8BML1-2:1052
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1951 AA; 218042 MW; 7AD3496E499D6FED CRC64;
MGENEDEKQA QASQVFENFV QATTCKGTLQ AFNILTCLLD LDPLDHRNFY SQLKSKVNTW
KAKALWHKLD KRGSHKEYKR GKACSNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDT
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEVHVN
VEFVRVLEPP EDQENQKVGW RAEFLPADHA LSDFEFDVII GADGHRNTLE GFRRKEFRGK
LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDSTHYFV
MTAKKQSLLD KGVILNDYID TEMLLCSENV NQDNLLSYAR EAADFATNYQ LPSLDFAINH
NGQPDVAMFD FTSMYASENA ALMRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVKSWDQ GTPPLEVLAE RESLYRLLPQ TTPENINKNF EQYTLDPATR YPNLNLHCVR
PHQVKHLYIT KEMDRFPLER WGSVRRSVSL SRRESDIRPN KLLTWCQQQT KGYQHVRVTD
LTTSWRSGLA LCAIIHSFRP ELINFDSLNE DDAVENNQLA FDVAKREFGI LPVTTGKEMA
STQEPDKLSM VMYLSKFYEL FRGTPLRPMD SWRKNYGENA DFGLGKTFIQ NNYLNLTLPR
KRTPRVDTQT EENDMNKRRR QGFNHLEELP SFSSRSLGSS QEYAKESGSQ NKVKHMANQL
LAKFEENTRN PSVVKQDCRR VSGIGKPVLC SASRPPGTSC CPKLEESTPR LPPPLKRQFS
STVATGQVLR ELNQVPASGE CPSRPWRARA KSDLQLGGVE NLATLPRTCQ GALALSGVLR
RLQQVEEKVL QKRAQNLANR EFHTKNIKEK AAHLASMFGH GDLPQDKLLS KRVPHAHPPS
PPSCLPSPHP AAASSPPAAD SVSPARKVVA LNHRLPPPLH LTVGKVSSGI GAAAEVLVNL
YLNDHRPKTQ ATSPDLESPR KAFPLSLGGR DTCYFCKKRV YMIERLSAEG HFFHQECFRC
SVCSATLRLA AYAFDCDEGK FYCKPHFVHC KTSSKQRKRR AELNQQREEE GTWQEQEAPR
RDVPTESSCA VAAISTPEGS PPDEPISPKK PKSVPEPNPR DVEAEATSPR PSEWTSVRIS
PGEDTVRQDV LAVRVLVTSE DSSSDTESDY GSITAPCAGA YEERPQLPES PPLSKPLTRH
ISLRENLTQP VSLLHEEPQA LPALQRAHSL QSPTPSKYQN WRRRFQSNST PMNQRAPSPP
KEPPPPPSLS SSSSLPSSFS SASVPGHTAD DSSSPQVTYN LHSPQISRGD VSPTPIYLRR
ARAQGIVKEI PLYLPHSPML ESTEDCLVEP GRESLRSPEE ISSSEGCQEA RALGNTRSIQ
HPILGKDQYL PNQNLALGAA GNPGDPREES RMGQPGGPEL SKERKLGLKK LVLTEEQKNK
LLDWSDCTQE HKTGEQLSQE SAENIRGGSL KPTCSSTLSQ AVKEKLLSQK KALGGMRTPA
VKAPQEREVP PPKSPLKLIA NAILRSLLHN SEAGKKTSPK PESKTLPRGQ PHARSFSLRK
LGSSKDGDQQ SPGRHMAKKA SAFFSLASPT SKVAQASDLS LPNSILRSRS LPSRPSKMFF
STTPHSKVED VPTLLEKVSL QDATHSPKTG ASHISSLGLK DKSFESFLQE CKQRKDIGDF
FNSPKEEGPP GNRVPSLEKL VQPVGSTSMG QVAHPSSTGQ DARKLEGGEG GSSLVSSLVL
VSDPVAPVTE ATSSPTSSSA EEEADSQLSL RIKEKILRRR RKLEKQSAKQ EELKRLHKAQ
AIQRQLEEVE ERQRTLAIQG VKLEKVLRGE AADSGTQDEA QLLQEWFKLV LEKNKLMRYE
SELLIMAQEL ELEDHQSRLE QKLRQKMLKD EGQKDENDLK EEQEIFEEMM QVIEQRNKLV
DSLEEQRVKE RTQDQHFENF VLSRGCQLSR T
