ID T0MGX6_CAMFR Unreviewed; 1060 AA.
AC T0MGX6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=CB1_000993026 {ECO:0000313|EMBL:EQB78441.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EQB78441.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EQB78441.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB017228; EQB78441.1; -; Genomic_DNA.
DR AlphaFoldDB; T0MGX6; -.
DR Proteomes; UP000030684; 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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000030684};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 586..690
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 760..822
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 911..1060
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 570..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 921..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 860..878
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1060 AA; 117277 MW; 43F0680C354D9B35 CRC64;
MSYSCARPCA SRKLFLSSVY FSAFGSCVVN VSSRLNDAEE SESLIDAYIK VFINWSNNNI
CHILSLYYGP GAKPGAVSMA APTATNPAHA HFESFLQAQL CQDVLSSFQG LCGALGLEPG
GGLPQYHKIK AQLNYWSAKS LWAKLDKRAS QPVYQQGRAC TSTKCLVVGA GPCGLRAAVE
LAMLGAHVVV VEKRTKFSRH NVLHLWPFTI HDLRGLGAKK FYGRFCTGSL DHISIRQLQL
LLLKVTLLLG VEIHWGVTFT GLQPPPKKGS GWRAQLQPNP PAQLTNYEFD VLISAAGGKF
VPEGFTVREM RGKLAIGITA NFVNGRTVEE TQVPEISGVA RIYNQSFFQS LLKATGIDLE
NIVYYKDDTH YFVMTAKKQC LLRLGVLRQD WPDTDRLLGS ANVVPEALQR FARAAANFAT
HGKLGKLEFA QDAHGRPDVS AFDFTSMMRA ESSARVQEKH GARLLLGLVG DCLVEPFWPL
GTGVARGFLA AFDAAWMVKR WAEGVGPLEV LAERESLYQL LSQTSPENMH HNVAQYGLDP
TTRYPNLNLR AVTPNQVRDL YNVEAKEPVR RISDKTDSGE PATGSAGTQE ELLRWCQEQT
AGYPGVHVTD LSSSWADGLA LCALVHRLRP SLLEPSELQG VGALEATSWA LRMAEHELGI
TPVLSAQAVV AGSDPLGLIA YLSHFHSAFK NTPHNPGDLE GPVSPGSPGI AGAVLLLGKL
QRTLQRTRAQ VEAETPSTEE RPVPEPVTPP SEHQEAGAED LCALCGEHLY ILERLCADGR
FFHRSCFRCH ICEATLWPGG YGQHPEDEHF YCLQHLPQPG HKEDGSDTGP ESQALEGSFV
GWGVPAQRSQ VLAAMENEEE SPSSSEEEAE EEEDMPLDPD TTQQVLWNLA KNSGTMNNYP
TWRRTLLRRA KEEEMKRFCK AQAIQRRLNE IEVALRELEA KGTKLELALR SQSSSPKKQK
ALWLEQLLQL VQEKNSLVAE EAELMITVQE LNLEEKQWQL DQKLRTYINR EEILKTAADR
QAEDQVLRQL VDVVNQRDAL IRFREERRLS ELATGSGAQG
//
