ID MICA2_MOUSE Reviewed; 960 AA.
AC Q8BML1; F6ZD54; F8WJF1; Q14DP1; Q3TR48; Q3UPU6; Q5DU17;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 81.
DE RecName: Full=Protein-methionine sulfoxide oxidase MICAL2;
DE EC=1.14.13.-;
DE AltName: Full=Molecule interacting with CasL protein 2;
DE Short=MICAL-2;
GN Name=Mical2; Synonyms=Kiaa0750;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.
RT The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
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
RT in plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin
CC by mediating oxidation of specific methionine residues on actin.
CC Acts by modifying actin subunits through the addition of oxygen to
CC form methionine-sulfoxide, leading to promote actin filament
CC severing and prevent repolymerization (By similarity).
CC -!- CATALYTIC ACTIVITY: [protein]-methionine + NADPH + O(2) =
CC [protein]-methionine-sulfoxide + NADP(+) + H(2)O.
CC -!- COFACTOR: FAD (By similarity).
CC -!- SUBUNIT: Interacts with RAB1B (By similarity). Interacts with VIM
CC and PLXNA4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC cytoskeleton (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BML1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BML1-2; Sequence=VSP_042597, VSP_042599;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8BML1-3; Sequence=VSP_042598;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the Mical family.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90416.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AK220353; BAD90416.1; 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; BC111895; AAI11896.1; -; mRNA.
DR EMBL; BC112415; AAI12416.1; -; mRNA.
DR IPI; IPI00223052; -.
DR RefSeq; NP_001180234.1; NM_001193305.1.
DR RefSeq; NP_796256.1; NM_177282.5.
DR UniGene; Mm.488195; -.
DR UniGene; Mm.52312; -.
DR ProteinModelPortal; Q8BML1; -.
DR SMR; Q8BML1; 16-488, 511-629, 749-807.
DR STRING; 10090.ENSMUSP00000102260; -.
DR PhosphoSite; Q8BML1; -.
DR PaxDb; Q8BML1; -.
DR PRIDE; Q8BML1; -.
DR Ensembl; ENSMUST00000037991; ENSMUSP00000047639; ENSMUSG00000038244.
DR Ensembl; ENSMUST00000050149; ENSMUSP00000051163; ENSMUSG00000038244.
DR Ensembl; ENSMUST00000106648; ENSMUSP00000102259; ENSMUSG00000038244.
DR GeneID; 320878; -.
DR KEGG; mmu:320878; -.
DR UCSC; uc009jgn.2; mouse.
DR CTD; 9645; -.
DR MGI; MGI:2444947; Mical2.
DR eggNOG; COG5069; -.
DR GeneTree; ENSGT00640000091174; -.
DR HOGENOM; HOG000047263; -.
DR HOVERGEN; HBG052474; -.
DR OMA; ACQGALA; -.
DR OrthoDB; EOG43BMN4; -.
DR ChiTaRS; MICAL2; mouse.
DR NextBio; 397627; -.
DR ArrayExpress; Q8BML1; -.
DR Bgee; Q8BML1; -.
DR Genevestigator; Q8BML1; -.
DR GermOnline; ENSMUSG00000038244; Mus musculus.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; 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; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 2.10.110.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR002938; mOase_FAD-bd.
DR InterPro; IPR003042; Rng_hydrolase-like.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; Calponin-homology; 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; Complete proteome; Cytoplasm;
KW Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1 960 Protein-methionine sulfoxide oxidase
FT MICAL2.
FT /FTId=PRO_0000075845.
FT DOMAIN 516 619 CH.
FT DOMAIN 751 813 LIM zinc-binding.
FT NP_BIND 97 125 FAD (By similarity).
FT REGION 2 494 Monooxygenase domain (By similarity).
FT BINDING 97 97 FAD (By similarity).
FT BINDING 116 116 FAD (By similarity).
FT BINDING 118 118 FAD (By similarity).
FT BINDING 123 123 FAD (By similarity).
FT BINDING 125 125 FAD (By similarity).
FT BINDING 398 398 FAD (By similarity).
FT VAR_SEQ 736 736 Q -> QDCRRVSGIGKPVLCSASRPPGTSCCPKLEESTPRL
FT PPPLKRQFSSTVATGQVLRELNQVPASGECPSRPWRARAKS
FT DLQLGGVENLATLPRTCQGALALSGVLRRLQQVEEKVLQKR
FT AQNLANREFHTKNIKEKAAHLASMFGHGDLPQDKLLSKRVP
FT HAHPPSPPSCLPSPHPAAASSPPAADSVSPARKLTVGKVSS
FT GIGAAAEVLVNLYLNDHRPKTQATSPDL (in isoform
FT 2).
FT /FTId=VSP_042597.
FT VAR_SEQ 799 960 GKFYCKPHFVHCKTSSKQRKRRAELNQQREEEGTWQEQEAP
FT RRDVPTESSCAVAAISTPEGSPPGTSTSFFRKALSWPLRLT
FT RGLLNLPQSLLRWMQGLQEAAGHHVRDNAHNYCFMFELLSL
FT GLLLLWAFSKVLAAMYRESEESLENIRSWLLRFIPVKLQ
FT -> GNPRGQESTSLWPWSQM (in isoform 3).
FT /FTId=VSP_042598.
FT VAR_SEQ 863 960 GTSTSFFRKALSWPLRLTRGLLNLPQSLLRWMQGLQEAAGH
FT HVRDNAHNYCFMFELLSLGLLLLWAFSKVLAAMYRESEESL
FT ENIRSWLLRFIPVKLQ -> VRFSLPVLHPLLG (in
FT isoform 2).
FT /FTId=VSP_042599.
SQ SEQUENCE 960 AA; 110072 MW; 0D70BBA2144730E2 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 PSVVKQESPR KAFPLSLGGR DTCYFCKKRV YMIERLSAEG HFFHQECFRC
SVCSATLRLA AYAFDCDEGK FYCKPHFVHC KTSSKQRKRR AELNQQREEE GTWQEQEAPR
RDVPTESSCA VAAISTPEGS PPGTSTSFFR KALSWPLRLT RGLLNLPQSL LRWMQGLQEA
AGHHVRDNAH NYCFMFELLS LGLLLLWAFS KVLAAMYRES EESLENIRSW LLRFIPVKLQ
//
