ID L9JHU1_TUPCH Unreviewed; 1116 AA.
AC L9JHU1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=TREES_T100016209 {ECO:0000313|EMBL:ELW50095.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW50095.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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 EMBL; KB320987; ELW50095.1; -; Genomic_DNA.
DR AlphaFoldDB; L9JHU1; -.
DR STRING; 246437.L9JHU1; -.
DR InParanoid; L9JHU1; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
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; 2.
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 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:UP000011518};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 552..656
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 697..759
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 967..1116
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 783..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 977..1004
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 786..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 123293 MW; 079BFBD92BC96CBE CRC64;
MASPTSTNPA HAHFESFLQA QQCQDVLSSF QGLCEALGLE PGGGLPQYHK IKAQLNYWSA
KSLWAKLDKR ASQPVYKQGQ ACTSTKCLVV GAGPCGLRAA VELALLGARV VLVEKRSKFS
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWRVA
FTGLQPPPRK GSGWRAQLQP SPPVQLANYE FDVLISAAGG KFVPEGFTVR EMRGKLAIGI
TANLLPPSPP VQLANYEFDV LISAAGGKFV PEGFTVREMR GKLAIGITAN FVNGRTVEET
QVPEISGVAK IYNQSFFQSL LKTTGIDLEN IVYYKDDTHY FVMTAKKQCL LRLGVLRQDW
PETDRLLDSA NVVPEALQRF ARAAADFATH GKLGKLEFAQ DARGQPDVSA FDFTSMMRAE
SSARVQEKHG ARLLLGLVGD CLVEPFWPLG TGVARGFLAA FDAAWMVKRW AEGAGPLEVL
AERESLYQLL SQTSPENMHR NVAQYALDPA TRYPNLNLRA VTPNQVRDLY DVVAKEPVRR
KIDETDSGKP ATGAQEELLR WCQEQTTGYP GVHVTDLSSS WADGLALCAL VPRLQPSLLE
PSELQGVGAL EATARALKMA EHELGITPVL SAQAVVAGSD PLGLIAYLSH FHSAFKSASH
SPDPASQTSP GTSSAILFLG KLQRTLQRTR SKADSGDLCA LCGGHLYVLE RLCADGHFFH
RSCFRCHICE ATLWPAGYGR HPGDGHYYCL QHLPQPGHKE DGSDKGPETP VTTVEVCVRE
LPLPGENCMP PNPSTPTAPQ EGASPVPVPS QPTRRLIRLS SPERQRLSSL NLSPDPEMEP
PPKPPRSCSA LARHALEGSF MGWGIPSQRP QDLVVIEKEE EGLSSSEEEE EEEDVALDSD
MEQNFPYFQA RFFAALSNSL SYSCPPEGQA LLLTNLIFPQ ALLILAKNSP TTNKYPTWHR
TLLRRAKEEE MKRFCKAQSI QRRLNEIEAA LRELEAEGVK LELAMRRQSS SPEQQKKLWL
EQLLQLVQKK NSLVAEEAEL MITVQELNLE EKQGQLDREL RGYINREETL KTAADRQAEA
QVLQKLVDVV NQRDALIRFQ EERRLSELAL GTGAQG
//
