MICA3_HUMAN
ID MICA3_HUMAN Reviewed; 2002 AA.
AC Q7RTP6; B2RXJ5; E9PEF0; O94909; Q5U4P4; Q6ICK4; Q96DF2; Q9P2I3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=[F-actin]-monooxygenase MICAL3;
DE EC=1.14.13.225 {ECO:0000305|PubMed:24440334};
DE AltName: Full=Molecule interacting with CasL protein 3;
DE Short=MICAL-3;
GN Name=MICAL3; Synonyms=KIAA0819, KIAA1364;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1626-2002 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 682-966 (ISOFORM 4).
RC TISSUE=Lymph, and Pancreas;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-2002 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1014-2002 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP IDENTIFICATION (ISOFORM 3 AND PARTIAL ISOFORM 1).
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 in
RT plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [7]
RP INTERACTION WITH RAB1B, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=15694364; DOI=10.1016/j.bbrc.2004.12.182;
RA Fischer J., Weide T., Barnekow A.;
RT "The MICAL proteins and rab1: a possible link to the cytoskeleton?";
RL Biochem. Biophys. Res. Commun. 328:415-423(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; THR-887; SER-1371 AND
RP SER-1384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310 AND THR-1454, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-1337 AND THR-1341,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION, INTERACTION WITH ERC1 AND RAB8A, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 93-GLY--GLY-98.
RX PubMed=21596566; DOI=10.1016/j.cub.2011.04.030;
RA Grigoriev I., Yu K.L., Martinez-Sanchez E., Serra-Marques A., Smal I.,
RA Meijering E., Demmers J., Peranen J., Pasterkamp R.J., van der Sluijs P.,
RA Hoogenraad C.C., Akhmanova A.;
RT "Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of
RT exocytotic carriers.";
RL Curr. Biol. 21:967-974(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; THR-887; SER-1143;
RP SER-1310; SER-1337; SER-1433; SER-1649; SER-1701 AND SER-1704, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION
RP SIGNAL, AND MUTAGENESIS OF 680-LYS--LYS-683.
RX PubMed=24440334; DOI=10.1016/j.cell.2013.12.035;
RA Lundquist M.R., Storaska A.J., Liu T.C., Larsen S.D., Evans T.,
RA Neubig R.R., Jaffrey S.R.;
RT "Redox modification of nuclear actin by MICAL-2 regulates SRF signaling.";
RL Cell 156:563-576(2014).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134; SER-1160; SER-1274;
RP THR-1276; SER-1278; SER-1649 AND THR-1651, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INTERACTION WITH NINL, AND SUBCELLULAR LOCATION.
RX PubMed=26485645; DOI=10.1371/journal.pgen.1005575;
RA Bachmann-Gagescu R., Dona M., Hetterschijt L., Tonnaer E., Peters T.,
RA de Vrieze E., Mans D.A., van Beersum S.E., Phelps I.G., Arts H.H.,
RA Keunen J.E., Ueffing M., Roepman R., Boldt K., Doherty D., Moens C.B.,
RA Neuhauss S.C., Kremer H., van Wijk E.;
RT "The ciliopathy protein CC2D2A associates with NINL and functions in RAB8-
RT MICAL3-regulated vesicle trafficking.";
RL PLoS Genet. 11:E1005575-E1005575(2015).
RN [18]
RP FUNCTION, INTERACTION WITH KIF23, AND SUBCELLULAR LOCATION.
RX PubMed=27528609; DOI=10.1074/jbc.m116.748186;
RA Liu Q., Liu F., Yu K.L., Tas R., Grigoriev I., Remmelzwaal S.,
RA Serra-Marques A., Kapitein L.C., Heck A.J., Akhmanova A.;
RT "MICAL3 flavoprotein monooxygenase forms a complex with centralspindlin and
RT regulates cytokinesis.";
RL J. Biol. Chem. 291:20617-20629(2016).
RN [19]
RP STRUCTURE BY NMR OF 515-630.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from human MICAL-3 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1841-1990, INTERACTION WITH
RP RAB1B; RAB8A; RAB10; RAB13 AND RAB15, AND DOMAIN.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin by
CC mediating oxidation of specific methionine residues on actin to form
CC methionine-sulfoxide, resulting in actin filament disassembly and
CC preventing repolymerization. In the absence of actin, it also functions
CC as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector
CC protein and plays a role in vesicle trafficking. Involved in exocytic
CC vesicles tethering and fusion: the monooxygenase activity is required
CC for this process and implicates RAB8A associated with exocytotic
CC vesicles. Required for cytokinesis. Contributes to stabilization and/or
CC maturation of the intercellular bridge independently of its
CC monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the
CC intercellular bridge, and together these proteins are proposed to
CC function in timely abscission. {ECO:0000269|PubMed:21596566,
CC ECO:0000269|PubMed:24440334}.
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:0000305|PubMed:24440334};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their
CC GTP-bound forms); binding to RAB1B is of low affinity compared to other
CC Rab proteins; at least in case of RAB8A can bind 2 molecules of RAB8A
CC simultaneously through a high and a low affinity binding site,
CC respectively. Interacts with ERC1 and RAB8A; may bridge ERC1 with
CC RAB8A. Interacts with KIF23 and ERC1; enhances the interaction between
CC KIF23 and ERC1. Interacts with NINL isoform 2.
CC {ECO:0000269|PubMed:15694364, ECO:0000269|PubMed:21596566,
CC ECO:0000269|PubMed:26485645, ECO:0000269|PubMed:27528609,
CC ECO:0000269|PubMed:27552051}.
CC -!- INTERACTION:
CC Q7RTP6-1; Q02241: KIF23; NbExp=8; IntAct=EBI-13945605, EBI-306852;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15694364}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:21596566}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:15694364}. Nucleus
CC {ECO:0000269|PubMed:24440334}. Midbody {ECO:0000269|PubMed:27528609}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27528609}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000305|PubMed:26485645}. Note=Mainly localizes in the nucleus.
CC {ECO:0000269|PubMed:24440334}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q7RTP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7RTP6-2; Sequence=VSP_039487, VSP_039488;
CC Name=3;
CC IsoId=Q7RTP6-3; Sequence=VSP_039485, VSP_039487, VSP_039488;
CC Name=4;
CC IsoId=Q7RTP6-4; Sequence=VSP_039486, VSP_039489;
CC Name=5;
CC IsoId=Q7RTP6-5; Sequence=VSP_042600, VSP_042601, VSP_042602;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15694364}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their
CC GTP-bound forms). {ECO:0000269|PubMed:27552051}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
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DR EMBL; CR456364; CAG30250.1; -; mRNA.
DR EMBL; BX647382; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006562; AAH06562.2; -; mRNA.
DR EMBL; BC085009; AAH85009.1; -; mRNA.
DR EMBL; BC157876; AAI57877.1; -; mRNA.
DR EMBL; BC171887; AAI71887.1; -; mRNA.
DR EMBL; AB020626; BAA74842.1; -; mRNA.
DR EMBL; AB037785; BAA92602.1; -; mRNA.
DR EMBL; BK000464; DAA01343.1; -; mRNA.
DR EMBL; BK000465; DAA01344.1; -; mRNA.
DR CCDS; CCDS46659.1; -. [Q7RTP6-1]
DR CCDS; CCDS46660.1; -. [Q7RTP6-4]
DR CCDS; CCDS46661.1; -. [Q7RTP6-5]
DR RefSeq; NP_001116203.1; NM_001122731.2. [Q7RTP6-4]
DR RefSeq; NP_001129476.1; NM_001136004.3. [Q7RTP6-5]
DR RefSeq; NP_056056.2; NM_015241.2. [Q7RTP6-1]
DR RefSeq; XP_005261319.1; XM_005261262.3.
DR PDB; 2D88; NMR; -; A=518-625.
DR PDB; 5SZG; X-ray; 2.70 A; A/B=1841-1990.
DR PDB; 6ICI; X-ray; 2.30 A; A=1-700.
DR PDBsum; 2D88; -.
DR PDBsum; 5SZG; -.
DR PDBsum; 6ICI; -.
DR AlphaFoldDB; Q7RTP6; -.
DR BMRB; Q7RTP6; -.
DR SMR; Q7RTP6; -.
DR BioGRID; 121609; 64.
DR IntAct; Q7RTP6; 47.
DR MINT; Q7RTP6; -.
DR STRING; 9606.ENSP00000416015; -.
DR GlyGen; Q7RTP6; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q7RTP6; -.
DR PhosphoSitePlus; Q7RTP6; -.
DR BioMuta; MICAL3; -.
DR DMDM; 300669653; -.
DR EPD; Q7RTP6; -.
DR jPOST; Q7RTP6; -.
DR MassIVE; Q7RTP6; -.
DR MaxQB; Q7RTP6; -.
DR PaxDb; Q7RTP6; -.
DR PeptideAtlas; Q7RTP6; -.
DR PRIDE; Q7RTP6; -.
DR ProteomicsDB; 68879; -. [Q7RTP6-1]
DR ProteomicsDB; 68880; -. [Q7RTP6-2]
DR ProteomicsDB; 68881; -. [Q7RTP6-3]
DR ProteomicsDB; 68882; -. [Q7RTP6-4]
DR ProteomicsDB; 68883; -. [Q7RTP6-5]
DR Antibodypedia; 34804; 26 antibodies from 10 providers.
DR DNASU; 57553; -.
DR Ensembl; ENST00000383094.7; ENSP00000372574.3; ENSG00000243156.9. [Q7RTP6-2]
DR Ensembl; ENST00000400561.6; ENSP00000383406.2; ENSG00000243156.9. [Q7RTP6-4]
DR Ensembl; ENST00000414725.6; ENSP00000391827.2; ENSG00000243156.9. [Q7RTP6-3]
DR Ensembl; ENST00000441493.7; ENSP00000416015.2; ENSG00000243156.9. [Q7RTP6-1]
DR Ensembl; ENST00000585038.1; ENSP00000462033.1; ENSG00000243156.9. [Q7RTP6-5]
DR GeneID; 57553; -.
DR KEGG; hsa:57553; -.
DR MANE-Select; ENST00000441493.7; ENSP00000416015.2; NM_015241.3; NP_056056.2.
DR UCSC; uc002zng.5; human. [Q7RTP6-1]
DR CTD; 57553; -.
DR DisGeNET; 57553; -.
DR GeneCards; MICAL3; -.
DR HGNC; HGNC:24694; MICAL3.
DR HPA; ENSG00000243156; Tissue enhanced (brain).
DR MIM; 608882; gene.
DR neXtProt; NX_Q7RTP6; -.
DR OpenTargets; ENSG00000243156; -.
DR PharmGKB; PA142671454; -.
DR VEuPathDB; HostDB:ENSG00000243156; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000155580; -.
DR HOGENOM; CLU_000329_1_1_1; -.
DR InParanoid; Q7RTP6; -.
DR OMA; CWPRSEK; -.
DR OrthoDB; 430978at2759; -.
DR PhylomeDB; Q7RTP6; -.
DR TreeFam; TF324129; -.
DR PathwayCommons; Q7RTP6; -.
DR SABIO-RK; Q7RTP6; -.
DR SignaLink; Q7RTP6; -.
DR BioGRID-ORCS; 57553; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; MICAL3; human.
DR EvolutionaryTrace; Q7RTP6; -.
DR GeneWiki; MICAL3; -.
DR GenomeRNAi; 57553; -.
DR Pharos; Q7RTP6; Tbio.
DR PRO; PR:Q7RTP6; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q7RTP6; protein.
DR Bgee; ENSG00000243156; Expressed in sural nerve and 122 other tissues.
DR ExpressionAtlas; Q7RTP6; baseline and differential.
DR Genevisible; Q7RTP6; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 1.
DR DisProt; DP02396; -.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045268; LIMA-like.
DR InterPro; IPR029941; MICAL3.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 1.
DR PANTHER; PTHR24206:SF66; PTHR24206:SF66; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51905; SSF51905; 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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell cycle;
KW Cell division; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Exocytosis; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase;
KW NADP; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..2002
FT /note="[F-actin]-monooxygenase MICAL3"
FT /id="PRO_0000075846"
FT DOMAIN 518..624
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 762..824
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1841..1990
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 2..494
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 658..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1791..1821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1821..1992
FT /evidence="ECO:0000255"
FT MOTIF 663..684
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24440334"
FT COMPBIAS 662..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..952
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1017
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1097
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 116..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 123..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1276
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1454
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1651
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT VAR_SEQ 746
FT /note="R -> RQLTQERGASQPSCCLPGQVRPAPTPRWK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_039485"
FT VAR_SEQ 747
FT /note="Q -> QQREKECSRTCPKKVITLSPPPTPPPCRAHGGQQTYRDLDADNRGKQ
FT SPHHERPEPEPPRRFFVDQWELSLSLRSSARPASPSSDSLRQKYIKMYTGGVSSLAEQI
FT ANQLQRKEQPKALLDKKEL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042600"
FT VAR_SEQ 871..949
FT /note="GVNGLEEPSIAKRLRGTPERIELENYRLSLRQAEALQEVPEETQAEHNLSSV
FT LDTGAEEDVASSSSESEMEEEGEEEEE -> LTSLFGWVARHSLGLCDKAKGMSQHLQS
FT NISSFGQQVAQNPLDSFFMCQLLAFGVPFLYGLSEVLVQIRGEFHWQAVAQ (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042601"
FT VAR_SEQ 934..966
FT /note="SSSESEMEEEGEEEEEEPRLPPSDLGGVPWKEA -> RDWVSPWLPRMVSNS
FT WAQMIHPPQPPTVLGSQM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_039486"
FT VAR_SEQ 934..948
FT /note="SSSESEMEEEGEEEE -> RSARRAAGRPPATRP (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:15461802"
FT /id="VSP_039487"
FT VAR_SEQ 949..2002
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10718198,
FT ECO:0000303|PubMed:15461802"
FT /id="VSP_039488"
FT VAR_SEQ 950..2002
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042602"
FT VAR_SEQ 967..2002
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_039489"
FT VARIANT 11
FT /note="P -> A (in dbSNP:rs11913706)"
FT /id="VAR_059451"
FT VARIANT 745
FT /note="R -> Q (in dbSNP:rs2289719)"
FT /id="VAR_059452"
FT VARIANT 750
FT /note="M -> L (in dbSNP:rs5992128)"
FT /id="VAR_018263"
FT MUTAGEN 93..98
FT /note="GAGPCG->WAWPCW: Abolishes Monooxygenase activity and
FT impairs ability to control docking and fusion of exocytic
FT carriers."
FT /evidence="ECO:0000269|PubMed:21596566"
FT MUTAGEN 680..683
FT /note="KRRK->AAAA: In MICAL-3NLSMut; abolishes nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:24440334"
FT CONFLICT 414
FT /note="G -> D (in Ref. 2; BX647382)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="Q -> R (in Ref. 5; BAA74842)"
FT /evidence="ECO:0000305"
FT CONFLICT 1717
FT /note="E -> V (in Ref. 4; AAH06562)"
FT /evidence="ECO:0000305"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 286..303
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 410..429
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:2D88"
FT HELIX 522..532
FT /evidence="ECO:0007829|PDB:6ICI"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:2D88"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 551..560
FT /evidence="ECO:0007829|PDB:6ICI"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:2D88"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:2D88"
FT HELIX 575..590
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 598..602
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:6ICI"
FT HELIX 1842..1877
FT /evidence="ECO:0007829|PDB:5SZG"
FT HELIX 1887..1889
FT /evidence="ECO:0007829|PDB:5SZG"
FT HELIX 1892..1938
FT /evidence="ECO:0007829|PDB:5SZG"
FT HELIX 1942..1944
FT /evidence="ECO:0007829|PDB:5SZG"
FT HELIX 1947..1980
FT /evidence="ECO:0007829|PDB:5SZG"
FT CONFLICT Q7RTP6-4:957
FT /note="Q -> R (in Ref. 2; BX647382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2002 AA; 224295 MW; F85C97FD4D647B80 CRC64;
MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW
KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH
YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR
PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE
MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT
ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN
KVKYMATQLL AKFEENAPAQ SIGIRRQGSM KKEFPQNLGG SDTCYFCQKR VYVMERLSAE
GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE
AKGPLQDGAT TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL
RQAEALQEVP EETQAEHNLS SVLDTGAEED VASSSSESEM EEEGEEEEEE PRLPPSDLGG
VPWKEAVRIH ALLKGKSEEE LEASKSFGPG NEEEEEEEEE YEEEEEEDYD EEEEESSEAG
NQRLQQVMHA ADPLEIQADV HWTHIREREE EERMAPASES SASGAPLDEN DLEEDVDSEP
AEIEGEAAED GDPGDTGAEL DDDQHWSDSP SDADRELRLP CPAEGEAELE LRVSEDEEKL
PASPKHQERG PSQATSPIRS PQESALLFIP VHSPSTEGPQ LPPVPAATQE KSPEERLFPE
PLLPKEKPKA DAPSDLKAVH SPIRSQPVTL PEARTPVSPG SPQPQPPVAA STPPPSPLPI
CSQPQPSTEA TVPSPTQSPI RFQPAPAKTS TPLAPLPVQS QSDTKDRLGS PLAVDEALRR
SDLVEEFWMK SAEIRRSLGL TPVDRSKGPE PSFPTPAFRP VSLKSYSVEK SPQDEGLHLL
KPLSIPKRLG LPKPEGEPLS LPTPRSPSDR ELRSAQEERR ELSSSSGLGL HGSSSNMKTL
GSQSFNTSDS AMLTPPSSPP PPPPPGEEPA TLRRKLREAE PNASVVPPPL PATWMRPPRE
PAQPPREEVR KSFVESVEEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW PRPEKPRHPP
LAKENGRLPA LEGTLQPQKR GLPLVSAEAK ELAEERMRAR EKSVKSQALR DAMARQLSRM
QQMELASGAP RPRKASSAPS QGKERRPDSP TRPTLRGSEE PTLKHEATSE EVLSPPSDSG
GPDGSFTSSE GSSGKSKKRS SLFSPRRNKK EKKSKGEGRP PEKPSSNLLE EAAAKPKSLW
KSVFSGYKKD KKKKADDKSC PSTPSSGATV DSGKHRVLPV VRAELQLRRQ LSFSEDSDLS
SDDVLEKSSQ KSRREPRTYT EEELNAKLTR RVQKAARRQA KQEELKRLHR AQIIQRQLQQ
VEERQRRLEE RGVAVEKALR GEAGMGKKDD PKLMQEWFKL VQEKNAMVRY ESELMIFARE
LELEDRQSRL QQELRERMAV EDHLKTEEEL SEEKQILNEM LEVVEQRDSL VALLEEQRLR
EREEDKDLEA AMLSKGFSLN WS
