MICA3_MOUSE
ID MICA3_MOUSE Reviewed; 1993 AA.
AC Q8CJ19; B2RR77; Q3UGQ8; Q3V160; Q69ZY5; Q80TE8; Q8BXB1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=[F-actin]-monooxygenase MICAL3;
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q7RTP6};
DE AltName: Full=Molecule interacting with CasL protein 3;
DE Short=MICAL-3;
GN Name=Mical3; Synonyms=Kiaa0819, Kiaa1364;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RA Korenbaum E., Hust H., Munck M., Noegel A.A.;
RT "Flavoprotein oxidoreductase MICAL-3 is associated with spermatid
RT development.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1526-1993 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 1-695 (ISOFORMS 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1740 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685; SER-687; SER-977;
RP SER-1187; SER-1369; THR-1452 AND SER-1903, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 play 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:0000250|UniProtKB:Q7RTP6}.
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:0000250|UniProtKB:Q7RTP6};
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. {ECO:0000250|UniProtKB:Q7RTP6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q7RTP6}. Nucleus
CC {ECO:0000250|UniProtKB:Q7RTP6}. Midbody {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q7RTP6}. Note=Mainly localizes in the nucleus.
CC {ECO:0000250|UniProtKB:Q7RTP6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CJ19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CJ19-2; Sequence=VSP_039491, VSP_039492;
CC Name=3;
CC IsoId=Q8CJ19-3; Sequence=VSP_039493, VSP_039494;
CC Name=4;
CC IsoId=Q8CJ19-4; Sequence=VSP_039490, VSP_039495;
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:0000250|UniProtKB:Q7RTP6}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65779.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF536756; AAN06715.1; -; mRNA.
DR EMBL; AK173033; BAD32311.1; -; mRNA.
DR EMBL; AK122497; BAC65779.1; ALT_INIT; mRNA.
DR EMBL; AC079443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC138257; AAI38258.1; -; mRNA.
DR EMBL; AK132669; BAE21292.1; -; mRNA.
DR EMBL; AK147803; BAE28149.1; -; mRNA.
DR EMBL; AK048201; BAC33271.1; -; mRNA.
DR CCDS; CCDS20487.1; -. [Q8CJ19-3]
DR CCDS; CCDS85152.1; -. [Q8CJ19-1]
DR RefSeq; NP_001257404.1; NM_001270475.1. [Q8CJ19-1]
DR RefSeq; NP_700445.2; NM_153396.3. [Q8CJ19-3]
DR RefSeq; XP_006505863.1; XM_006505800.2. [Q8CJ19-1]
DR AlphaFoldDB; Q8CJ19; -.
DR SMR; Q8CJ19; -.
DR BioGRID; 228787; 15.
DR IntAct; Q8CJ19; 5.
DR STRING; 10090.ENSMUSP00000096056; -.
DR iPTMnet; Q8CJ19; -.
DR PhosphoSitePlus; Q8CJ19; -.
DR SwissPalm; Q8CJ19; -.
DR EPD; Q8CJ19; -.
DR MaxQB; Q8CJ19; -.
DR PaxDb; Q8CJ19; -.
DR PeptideAtlas; Q8CJ19; -.
DR PRIDE; Q8CJ19; -.
DR ProteomicsDB; 292319; -. [Q8CJ19-1]
DR ProteomicsDB; 292320; -. [Q8CJ19-2]
DR ProteomicsDB; 292321; -. [Q8CJ19-3]
DR ProteomicsDB; 292322; -. [Q8CJ19-4]
DR Antibodypedia; 34804; 26 antibodies from 10 providers.
DR DNASU; 194401; -.
DR Ensembl; ENSMUST00000077159; ENSMUSP00000076402; ENSMUSG00000051586. [Q8CJ19-3]
DR Ensembl; ENSMUST00000207889; ENSMUSP00000146544; ENSMUSG00000051586. [Q8CJ19-1]
DR GeneID; 194401; -.
DR KEGG; mmu:194401; -.
DR UCSC; uc009dnw.2; mouse. [Q8CJ19-1]
DR UCSC; uc009dnx.1; mouse. [Q8CJ19-4]
DR UCSC; uc009dnz.3; mouse. [Q8CJ19-3]
DR UCSC; uc009doa.1; mouse. [Q8CJ19-2]
DR CTD; 57553; -.
DR MGI; MGI:2442733; Mical3.
DR VEuPathDB; HostDB:ENSMUSG00000051586; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000155580; -.
DR HOGENOM; CLU_000329_0_1_1; -.
DR InParanoid; Q8CJ19; -.
DR OMA; CWPRSEK; -.
DR OrthoDB; 430978at2759; -.
DR PhylomeDB; Q8CJ19; -.
DR TreeFam; TF324129; -.
DR BioGRID-ORCS; 194401; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mical3; mouse.
DR PRO; PR:Q8CJ19; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8CJ19; protein.
DR Bgee; ENSMUSG00000051586; Expressed in embryonic brain and 221 other tissues.
DR ExpressionAtlas; Q8CJ19; baseline and differential.
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; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 1.
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 Actin-binding; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Exocytosis; FAD;
KW Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1993
FT /note="[F-actin]-monooxygenase MICAL3"
FT /id="PRO_0000075847"
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 1832..1981
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..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1817..1983
FT /evidence="ECO:0000255"
FT COMPBIAS 662..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1093
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1467
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 1585..1604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1837
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:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..871
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039490"
FT VAR_SEQ 748..774
FT /note="GSIKKEFPQNLGGSDTCYFCQKRVYVM -> VSPKLSSRMTTWYRKEGLHAA
FT ISQALV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_039491"
FT VAR_SEQ 775..1993
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_039492"
FT VAR_SEQ 810..864
FT /note="GKFYCKPHYCYRLSGYAQRKRPAVAPLSGKEVKGALQDGPTADANGLASVAA
FT SSA -> EFSPNFWTSASYHVPVALPATVMPMCLLYHPSQVLVCLEGGPAFMSPVLFND
FT TNS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_039493"
FT VAR_SEQ 865..1993
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_039494"
FT VAR_SEQ 1016..1061
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039495"
FT CONFLICT 281
FT /note="A -> T (in Ref. 1; AAN06715)"
FT /evidence="ECO:0000305"
FT CONFLICT 1249
FT /note="P -> H (in Ref. 5; BAE28149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1993 AA; 223721 MW; 5059DCB5EF4DB091 CRC64;
MEERKQETTN QAHVLFDRFV QATTCKGTLR AFQELCDHLE LKPKDYRSFY HKLKSKLNYW
KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
VEFQGLVQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
MTAKKQSLLD KGVILHDYTD TELLLSRENV DQEALLNYAR EAADFSTQQQ LPSLDFAINH
YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNININFLR
PSQVRHLYDS GETKDIHLEM ENMVNPRTTP KLTRNESVAR SSKLLGWCQR QTEGYSGVNV
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE
MASVGEPDKL SMVMYLTQFY EMFKDSLSSS DTLDLNAEEK AVLIASTKSP ISFLSKLGQT
ISRKRSPKDK KEKDSDGAGK RRKTSQSEEE EPPRSYKGER PTLVSTLTDR RMDAAVGNQN
KVKYMATQLL AKFEENAPAQ STGVRRQGSI KKEFPQNLGG SDTCYFCQKR VYVMERLSAE
GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE
VKGALQDGPT ADANGLASVA ASSAERSPGT SMNGLEEPSI AKRLRGTPER IELENYRRSV
RQVEELEEVP EETQAEHNLS SVLDKGTEED VASSSSESEM EEEEEEDDED DHLPTSDLGG
VPWKEAVRIH ALLKGRSEEE LEASKNFEPE EEEEEEEYEE EDEEYEEEEE EESSEAGNKR
LQQIITAADP LAIQADVHWT HIREREAEER MLPTSESSTS RAPLDEDDLE EDADSEPAET
EGEAAEDGDP GDTGAELDDQ HWSDDIPSDA EAEHRLQSQA KVKAELELRV SENEEEKPSD
APKQEERGTS QVSSPSQPPE KQVGVFSPAR SPGTEEAKSP LATKVKSPEE PLFPTPLLLR
EKPKAEVPEE QKAVLSPIRS QPVALPEARS PTSPTSLQPE SLLAPPTPPT PPPTQLPICS
QPQPSSDASI PSPTKSPIRF QPVPAKTSTP LTPLPVKSQG DPKDRLSGPL AVEEVLKRSD
LVEEFWMKSA EIRRSLGLTP VDRSKGSEPS LPSPASKPIS LKSYSVDKSP QDEGLCLLKP
PSVPKRLGLP KSAGDQPPLL TPKSPSDKEL RSSQEERRDL SSSSGLGLHD SSSNMKTLGS
QSFNTSDSTM LTPPSSPPPP PPPNEEPATL RRKPHQTFER REASIIPPPT PASFMRPPRE
PAQPPREEVR KSFVESVDEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW SRSEKLQAKE
NGRLPPLEQD VPPQKRGLPL VSAEAKELAE ERMRAREKSV KSQALRDAMA KQLSRMQAME
MVSSRSHTAQ SQGKELGSES TRHPSLRGTQ EPTLKHEATS EEILSPPSDS GGPDGSVTSS
EGSSGKSKKR SSLFSPRRNK KEKKTKGEAR PPEKPSPGLP EDVVAKPKSL WKSVFSGYKK
DKKKKSDEKS CSSTPSSGAT VDSGQRRASP MVRAELQLRR QLSFSEDSDL SSDDILERSS
QKSKREPRTY TEEELSAKLT RRVQKAARRQ AKQEELKRLH RAQIIQRQLE QVEEKQRQLE
ERGVAVEKAL RGEAGMGKKD DPKLMQEWFK LVQEKNAMVR YESELMIFAR ELELEDRQSR
LQQELRERMA VEDHLKTEGE LSEEKKILNE MLEVVEQRDS LVALLEEQRL REKEEDKDLE
AAMLCKGFSL DWS
