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Database: UniProt
Entry: A0A096NZ47_PAPAN
LinkDB: A0A096NZ47_PAPAN
Original site: A0A096NZ47_PAPAN 
ID   A0A096NZ47_PAPAN        Unreviewed;      1192 AA.
AC   A0A096NZ47;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Molecule interacting with CasL protein 1 {ECO:0000256|ARBA:ARBA00044245};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN   Name=MICAL1 {ECO:0000313|Ensembl:ENSPANP00000018365.3};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000018365.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000018365.3, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000018365.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001591};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000547};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004608}. Midbody
CC       {ECO:0000256|ARBA:ARBA00004214}.
CC   -!- SIMILARITY: Belongs to the Mical family.
CC       {ECO:0000256|ARBA:ARBA00008223}.
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DR   AlphaFoldDB; A0A096NZ47; -.
DR   STRING; 9555.ENSPANP00000018365; -.
DR   Ensembl; ENSPANT00000011001.3; ENSPANP00000018365.3; ENSPANG00000014435.3.
DR   eggNOG; KOG1700; Eukaryota.
DR   GeneTree; ENSGT00940000159117; -.
DR   HOGENOM; CLU_000329_0_0_1; -.
DR   Proteomes; UP000028761; Chromosome 6.
DR   Bgee; ENSPANG00000014435; Expressed in aorta and 65 other cell types or tissues.
DR   ExpressionAtlas; A0A096NZ47; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:UniProt.
DR   CDD; cd21196; CH_MICAL1; 1.
DR   CDD; cd09358; LIM_Mical_like; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR022735; bMERB_dom.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR23167:SF35; [F-ACTIN]-MONOOXYGENASE MICAL1; 1.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   Pfam; PF12130; bMERB_dom; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM01203; DUF3585; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS51848; BMERB; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          679..783
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          866..928
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1088..1192
FT                   /note="BMERB"
FT                   /evidence="ECO:0000259|PROSITE:PS51848"
FT   REGION          816..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1098..1125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        816..836
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1056
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  131012 MW;  CF7B076103955CC7 CRC64;
     MEGDGAGYVR SSWGPGYQIC PCVAYKGSSV LSTSKKSPHA LIPRPKEGRL RIPTQRLGDP
     RTGRLSWRLP WCPICPLCPR LMFFTSKFGK FHLGVDGIAA VSGADAGRGV GWEEQSQSLV
     NPEFPGDTSL LSSPPLLFYF FCSPASSPSS STSPATCLCP AAALPGSPRE ASMASPTSTN
     PAHAHFESFL QAQLCQDVLS SFQELCGALG LEPGGGLPQY HKIKDQLNYW SAKSLWTKLD
     KRAGQAVYQQ GRACTSTKCL VVGAGPCGLR VAVELALLGA RVVLVEKRTK FSRHNVLHLW
     PFTIHDLRAL GAKKFYGRFC TGTLDHISIR QLQLLLLKVV LLLGVEIHWG VTFTGLQPPP
     RKGSGWRAQL QPNPPAQLAN YEFDVLISAA GGKFVPEGFK VREMRGKLAI GITANFVNGR
     TVEETQVPEI SGVARIYNQS FFQSLLKATG IDLENIVYYK DDTHYFVMTA KKQCLLRLGV
     LRQDWPDTDR LLGSANVVPE ALQRFARAAA DFATHGKLGK LEFAQDAHRQ PDVCAFDFTS
     MMRAESSARV QEKHGARLLL ALVGDCLVEP FWPLGTGVAR GFLAAFDAAW MVKRWAEGAE
     PLEVLAERES LYQLLSQTSP ENMHRNVAQY GLDPATRYPN LNLRAVTPNQ VRDLYDVLTK
     EPVQRNDKTD ARMPTTGSAG TQEELLRWCQ EQTAGYPGVH VSDLSSSWTD GLALCALVHR
     LQPGLLEPSE LQGLGALEAT AWALKVAEHE LGITPVVSAQ AVVAGSDPLG LIAYLSHFHS
     AFKSTAHSPG PVSQASPGTS SAVLFLGKLQ RTLQRSRAKE NAEDAGGKKL RLEMDAETPS
     TEVPPDPEPG VPLTPPSQHQ EAGAGDLCAL CGEHLYVLER LCVDGHFFHR SCFRCHTCEA
     TLWPGGYEQH PGDGRFYCLQ HLPQPDHKEE GSDGGPESPE LPTPSENSMP PDLSTPTASQ
     EGVGPVPDPS QPTRRRIHLS SLERQRLSSL NLTPDPEMEP PPKPPRSCSA LARHALESSF
     VGWGLPAQSP QALAAMEKEE EESSSSSEEE EDVPLDSDVE QALQTFAKTS GTMNDYPTWR
     RTLLRRAKEE EMKRFRKAQT IQRRLNEIEG ALRELEAEGV KLELALRRQS SSPEQQKKLW
     VGQLLQLVDK KNSLVAEEAE LMIMVQELNL EEKQWQLDQE LRGYMNREGT QK
//
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