ID M7B5E2_CHEMY Unreviewed; 2283 AA.
AC M7B5E2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=UY3_10541 {ECO:0000313|EMBL:EMP32329.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP32329.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(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; KB540908; EMP32329.1; -; Genomic_DNA.
DR STRING; 8469.M7B5E2; -.
DR eggNOG; ENOG502QQV6; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd22198; CH_MICAL_EHBP-like; 1.
DR CDD; cd07439; FANCE_c-term; 1.
DR CDD; cd09439; LIM_Mical; 1.
DR Gene3D; 1.25.40.480; -; 1.
DR Gene3D; 3.40.50.790; -; 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; IPR021025; Fanconi_anaemia_gr_E_prot_C.
DR InterPro; IPR008677; MRVI1.
DR InterPro; IPR023674; Ribosomal_uL1-like.
DR InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
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; PF11510; FA_FANCE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF05781; MRVI1; 1.
DR Pfam; PF00687; Ribosomal_L1; 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 SUPFAM; SSF56808; Ribosomal protein L1; 1.
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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000031443};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 1542..1648
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1777..1839
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2042..2191
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 215..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1838..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2052..2079
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 989..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1914..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1988..2013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2283 AA; 255273 MW; 10D261F15EE97EEE CRC64;
MFSAITEASR SHRADAMEAP PAPWLQRFDK PSRLLLHTLT SRPCGALAAF RALQRSRACD
EPGQAFHWQI FTETLCAEEP VLRGPEQTLT LRPILLLLPV MCQRNLLSLL HMVQGSMPKD
CLSQLLQATR KDPSPDLWVR ALRDLLQRGL REERSCWTPL PLTDTCQQQL KTLCQKFVGG
TGSKPDLERK RSWFTQEHPG PELWLAGDAT DSASRLRKRK QVAEESLDPE GERQRKRSRL
EEEELDLEPL AGCAFVKGAG AGEEEIGIEA SGRGSIRSQT RGANENAQPD AVMETREASK
RSQQDAAAKV PDFMQVHVPR LKMLLEMESN QTDGTAPPEL QILNECTPGQ LEGLCSLLQL
SECPERSLVQ FCTWLLALVP EVSYTHAAIL TEQLFLQRVL SLTQPASRHL MAALTSFCSK
YARPVCCALI APALRASGAG PEGTKLVCEL IEDSLEPEYV RLVLSQVLEM PWSEELITVV
QTLLGRQVEL PPELFNLLVL KLCRLAQEFA KSMNYTKLMM AVLTIYSSNI TPAHRRHLSG
ALDLNHTALR KSLQAALEQM APRLKSFLCR EFSVCVLGVQ QHYDEAKAVN IPHMNIEPLK
KLKNKLVKKL ESLIKQIPLT LGQGLNKAGK FPSLFTHNEK IVAKVDEVKS TIEFQMKKVL
FLAVAVGHVK MTGDELVYKV HLAINFLVFL LKNCQNLSMQ MSDPAKVVYS GNEFHRFHDT
GHRRKNPDPP KDPLLNSLPE LSVLERLGLH RVALTEQDVE AAFTHLALAF RCDIFTLRRR
VQAAFTHLAL AFRCDIFTLR RRVQRLGLSC VDPKCKELVR QLQLSLTVLA GSVERATSAA
EKLGAVHQEA RMSRAAEVMV QHVENLKRHH LREHTELEEM KRLIQQNSRN RQLAENRDDG
EQRLKLPLMR TFQQASARRR VSIAVIPKQL TPLPSPESGR APEGEAAKAA WESSPSTERR
TCCLQEDSAD GYFILRSDSS SSLHQSQPEA DRLEYEGDRG RYAEGSQPEL RRRGSTGKPM
KEEPDGASDS SGLTEELEQL SLTHHHQATE ALLKGDAVAE GHPASLCHCQ EVLDSFQALC
GQLGLEHKGQ LQFYRKLKSC LNDWSAKDLW GKLDKKAGHK DYDQGRACAN TKCLIIGAGP
CGLRTAIELA FLGARVVLVE KRDSFSRNNV LHLWPFTIHD LRVLGAKKFY GRFCTGTLDH
ISIRQLQLIL LKVALLLGVE VHVNVQFEGL IPPAEKGSGR GGAWRAALQP SSSPVGQYEF
DVLISAGGGK FVPKGFKRKE MRGKLAIGIT TNFVNRHSRA EVEVAEISGV ARIYNQQFFQ
NLYNKTGIDL ENIVYYKDDT HYFVMTAKKQ SLLRKGVIVQ DKADIESLLS AENISQEALL
SYAKEAANFS TNYQLPDLEF ALNHRNCPDV DMFDFTCMNR SENAALVREC HGARLLIGLP
FWPLGTGVAR GFLAAFDTAW MVKRWAAGTS PLDLLAERES IYQQLSQTSP DNTNKNTSQY
SIDPTTRYRN INLQAIKPNQ VRDMYVVGMI EIDHKKRNSH VGRAYEELLS WCQTHTAGYR
GVTVTDFTHS WKSGLALCAL IHRFRPNLLD FNSLDQHSPI KNNQMALDIA EQELGIQPVL
SSTEMASVAE PNQLGLITYL SQFYEAFKSS AKPEEKVGKL RAPPSTRGAV LFLSKLQKSL
SLSRKRNQDS AQQDAETKRT RREAGALKSV SINLLAFSGA IAPVPEGHVG ICFSVWGCGK
PGVEPESKLT NREPSTVRAS QAAGAQSSLT SPTESSDACY FCGKRVYILE RVSAEGHFFH
RGCFQCHQCG TTLRLGDFAF DEDDGRFYCM LHYSSPRSMD VPDSGSQAAP HERMWGGPSP
PDTAGRAQPQ DPGAGRGDGV NGWSQREEWS LGAAPGHPTP GPPEKGPAPP GFRQAEEEGE
DTRKRKKIQL SLSEKLKLST LSLDSETESQ EGPGTHRAGS EPLRSAVPAK DQGAPERGQV
CWAEPGFSEE AEDIEETDSD GEEEEEEEES QDLGYLTENS LLSLGEKEKY FTWNRTLTRR
AKEAEMKRFC KAQSIQRRLE EIEVTFRKLE EKGIKLERSL RGEGGTQSEL RTKWMNQLLS
LVQKKNSLVS EESDLMIEVQ GLKLEEKQCQ LDQELRRYMN MEETLKMPQD RLAEKEILAQ
LLEVVNQRNA LIHVLDEKRL SEAFPGPDKG AYPGPENRSN GYRLQYLANS YFHGAQRLLL
VPLLTDSCNF SSSLSYAVLL WPCRSQGTRE TRELLTGGSL FAMKLHGAIP EGAWSPAHRC
WER
//
