CSI1_ARATH
ID CSI1_ARATH Reviewed; 2150 AA.
AC F4IIM1; Q0WUD1; Q6NPD6; Q8RUY6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Protein CELLULOSE SYNTHASE INTERACTIVE 1 {ECO:0000303|PubMed:20616083};
DE AltName: Full=Protein POM-POM 2 {ECO:0000303|PubMed:7743935};
GN Name=CSI1 {ECO:0000303|PubMed:20616083};
GN Synonyms=POM2 {ECO:0000303|PubMed:7743935};
GN OrderedLocusNames=At2g22125 {ECO:0000312|Araport:AT2G22125};
GN ORFNames=T16B14.2 {ECO:0000312|EMBL:AAM15466.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 993-2150.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1829-2150.
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=7743935; DOI=10.1242/dev.121.4.1237;
RA Hauser M.-T., Morikami A., Benfey P.N.;
RT "Conditional root expansion mutants of Arabidopsis.";
RL Development 121:1237-1252(1995).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REVIEW.
RC STRAIN=cv. Columbia;
RX PubMed=21150290; DOI=10.4161/psb.5.12.13621;
RA Gu Y., Somerville C.;
RT "Cellulose synthase interacting protein: a new factor in cellulose
RT synthesis.";
RL Plant Signal. Behav. 5:1571-1574(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, INTERACTION WITH CESA1; CESA3 AND
RP CESA6, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=20616083; DOI=10.1073/pnas.1007092107;
RA Gu Y., Kaplinsky N., Bringmann M., Cobb A., Carroll A., Sampathkumar A.,
RA Baskin T.I., Persson S., Somerville C.R.;
RT "Identification of a cellulose synthase-associated protein required for
RT cellulose biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12866-12871(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22294619; DOI=10.1105/tpc.111.093575;
RA Bringmann M., Li E., Sampathkumar A., Kocabek T., Hauser M.-T., Persson S.;
RT "POM-POM2/cellulose synthase interacting1 is essential for the functional
RT association of cellulose synthase and microtubules in Arabidopsis.";
RL Plant Cell 24:163-177(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MICROTUBULES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22190487; DOI=10.1073/pnas.1118560109;
RA Li S., Lei L., Somerville C.R., Gu Y.;
RT "Cellulose synthase interactive protein 1 (CSI1) links microtubules and
RT cellulose synthase complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:185-190(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH
RP MICROTUBULES, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22427339; DOI=10.1105/tpc.111.095059;
RA Mei Y., Gao H.-B., Yuan M., Xue H.-W.;
RT "The Arabidopsis ARCP protein, CSI1, which is required for microtubule
RT stability, is necessary for root and anther development.";
RL Plant Cell 24:1066-1080(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=22751327; DOI=10.4161/psb.20338;
RA Lei L., Li S., Gu Y.;
RT "Cellulose synthase interactive protein 1 (CSI1) mediates the intimate
RT relationship between cellulose microfibrils and cortical microtubules.";
RL Plant Signal. Behav. 7:714-718(2012).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23623553; DOI=10.1016/j.cub.2013.04.013;
RA Landrein B., Lathe R., Bringmann M., Vouillot C., Ivakov A., Boudaoud A.,
RA Persson S., Hamant O.;
RT "Impaired cellulose synthase guidance leads to stem torsion and twists
RT phyllotactic patterns in Arabidopsis.";
RL Curr. Biol. 23:895-900(2013).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CESA3 AND CESA6.
RX PubMed=24368796; DOI=10.1105/tpc.113.116715;
RA Lei L., Li S., Du J., Bashline L., Gu Y.;
RT "Cellulose synthase INTERACTIVE3 regulates cellulose biosynthesis in both a
RT microtubule-dependent and microtubule-independent manner in Arabidopsis.";
RL Plant Cell 25:4912-4923(2013).
RN [14]
RP REVIEW.
RX PubMed=25262237; DOI=10.1016/b978-0-12-800178-3.00001-4;
RA Hamada T.;
RT "Microtubule organization and microtubule-associated proteins in plant
RT cells.";
RL Int. Rev. Cell Mol. Biol. 312:1-52(2014).
RN [15]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=25535279; DOI=10.1104/pp.114.249003;
RA Worden N., Wilkop T.E., Esteve V.E., Jeannotte R., Lathe R., Vernhettes S.,
RA Weimer B., Hicks G., Alonso J., Labavitch J., Persson S., Ehrhardt D.,
RA Drakakaki G.;
RT "CESA TRAFFICKING INHIBITOR inhibits cellulose deposition and interferes
RT with the trafficking of cellulose synthase complexes and their associated
RT proteins KORRIGAN1 and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1.";
RL Plant Physiol. 167:381-393(2015).
CC -!- FUNCTION: Regulator of the microtubular cytoskeleton (PubMed:22427339).
CC Microtubule-associated protein essential for the functional association
CC of cellulase synthase (CESA) complexes (CSCs) and cortical microtubules
CC (PubMed:22294619, PubMed:22190487, PubMed:22751327, PubMed:23623553,
CC PubMed:24368796). Promotes dynamics of CSCs in the plasma membrane
CC (PubMed:21150290, PubMed:20616083, PubMed:22294619, PubMed:22190487,
CC PubMed:22751327, PubMed:23623553, PubMed:24368796). Regulates primary
CC cell wall biosynthesis and cellulose microfibrils organization
CC (PubMed:21150290, PubMed:20616083, PubMed:23623553). Required for the
CC regulation of root cell elongation/expansion (PubMed:7743935,
CC PubMed:21150290, PubMed:20616083, PubMed:22294619, PubMed:22427339).
CC Necessary for the formation of ovules, pollen cell wall morphogenesis
CC and pollen tube development (PubMed:22294619). Involved in anther
CC dehiscence, via dehydration-induced microtubule depolymerization and
CC reorganization. May play a role in early gynoecial development
CC (PubMed:22427339). {ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:21150290, ECO:0000269|PubMed:22190487,
CC ECO:0000269|PubMed:22294619, ECO:0000269|PubMed:22427339,
CC ECO:0000269|PubMed:22751327, ECO:0000269|PubMed:23623553,
CC ECO:0000269|PubMed:24368796, ECO:0000269|PubMed:7743935}.
CC -!- FUNCTION: Target of the cellulase synthase (CESA) complexes (CSCs)
CC trafficking inhibitor CESTRIN, which reduces cellulose content and
CC alters anisotropic growth of hypocotyls; CESTRIN treatment inhibits the
CC dynamics of CSCs. {ECO:0000269|PubMed:25535279}.
CC -!- SUBUNIT: Associates with cellulase synthase (CESA) complexes
CC (PubMed:20616083, PubMed:22751327). Interacts with CESA1, CESA3 and
CC CESA6 (PubMed:20616083, PubMed:24368796). Binds to cortical
CC microtubules (PubMed:22190487, PubMed:22427339, PubMed:22751327).
CC {ECO:0000269|PubMed:20616083, ECO:0000269|PubMed:22190487,
CC ECO:0000269|PubMed:22427339, ECO:0000269|PubMed:22751327,
CC ECO:0000269|PubMed:24368796}.
CC -!- INTERACTION:
CC F4IIM1; Q94JQ6: CESA6; NbExp=2; IntAct=EBI-4430539, EBI-15659159;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:22190487, ECO:0000269|PubMed:22294619,
CC ECO:0000269|PubMed:22751327, ECO:0000269|PubMed:24368796}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi
CC apparatus {ECO:0000269|PubMed:22294619}. Endomembrane system
CC {ECO:0000269|PubMed:22294619}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22190487, ECO:0000269|PubMed:22294619,
CC ECO:0000269|PubMed:22427339}. Note=Undergoes dynamic changes in
CC response to dehydration (PubMed:22427339). Colocalizes with cellulase
CC synthase (CESA) complexes (CSCs) in a dynamic way, both at the plasma
CC membrane and in post-Golgi compartments (PubMed:24368796,
CC PubMed:20616083, PubMed:22294619, PubMed:22190487). Present in distinct
CC punctae at the cell cortex, called microtubule-associated cellulose
CC synthase compartments, that move with constant velocities of 200 to 300
CC nm/min (PubMed:22294619). Present with cortical microtubule
CC depolymerizing ends (PubMed:22294619, PubMed:22190487).
CC {ECO:0000269|PubMed:20616083, ECO:0000269|PubMed:22190487,
CC ECO:0000269|PubMed:22294619, ECO:0000269|PubMed:22427339,
CC ECO:0000269|PubMed:24368796}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC flowers and pollen (PubMed:20616083, PubMed:22427339). Highly expressed
CC in floral tissues (PubMed:22427339). {ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:22427339}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the stigma and pollen
CC grains. Present at lower levels in sepals, filaments, and anther wall.
CC Absent from the ovary. {ECO:0000269|PubMed:22427339}.
CC -!- DISRUPTION PHENOTYPE: Altered microtubule-dependent dynamics of
CC cellulase synthase (CESA) complexes (CSCs) (PubMed:22190487,
CC PubMed:21150290, PubMed:20616083, PubMed:22294619, PubMed:22751327,
CC PubMed:23623553, PubMed:24368796). Reduced cellulose content, with
CC abnormal organization of cellulose microfibrils (PubMed:20616083,
CC PubMed:23623553). Anisotropic growth defect; abnormal cell expansion,
CC such as reduced cell elongation but increased cell volume, leading to
CC radially swollen epidermal cells in both primary root and dark-grown
CC hypocotyls, as well as dwarfism (PubMed:7743935, PubMed:21150290,
CC PubMed:20616083, PubMed:22294619, PubMed:22190487, PubMed:22427339,
CC PubMed:24368796). Organ and cell twisting leading to alterated
CC phyllotaxis, such as subtle right-handed torsion of the inflorescence
CC stems and hypocotyls, and associated with altered microtubule
CC organization and uncoupled cellulose deposition from cortical
CC microtubules (PubMed:22294619, PubMed:23623553). Reduced fertility due
CC to smaller gynoecia with fewer ovules, heterostyly, the inability of
CC anthers to release pollen, and pollen defects displaying irregular or
CC collapsed cell wall morphologies as well as altered pollen tube
CC development (PubMed:22427339, PubMed:21150290, PubMed:20616083,
CC PubMed:22294619). Defective anther dehiscence. Decreased number of
CC ovules per gynoecium. Hypersensitive to the microtubule-disrupting drug
CC oryzalin. Altered depolymerization of cortical microtubules in response
CC to dehydration. Enhanced sensitivity to exogenous calcium leading to
CC root growth inhibition (PubMed:22427339). The csi1 csi3 double mutants
CC shows an enhanced cell expansion defect compared to csi1 as well as an
CC additive reduction of cellulase synthase (CESA) complexes (CSCs)
CC velocities (PubMed:24368796). {ECO:0000269|PubMed:20616083,
CC ECO:0000269|PubMed:21150290, ECO:0000269|PubMed:22190487,
CC ECO:0000269|PubMed:22294619, ECO:0000269|PubMed:22427339,
CC ECO:0000269|PubMed:22751327, ECO:0000269|PubMed:23623553,
CC ECO:0000269|PubMed:24368796, ECO:0000269|PubMed:7743935}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15466.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAR20777.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007168; AAM15432.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007232; AAM15466.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07269.1; -; Genomic_DNA.
DR EMBL; AK227230; BAE99267.1; -; mRNA.
DR EMBL; BT010720; AAR20777.1; ALT_INIT; mRNA.
DR EMBL; BT010988; AAR24766.1; -; mRNA.
DR RefSeq; NP_179803.4; NM_127781.5.
DR AlphaFoldDB; F4IIM1; -.
DR SMR; F4IIM1; -.
DR IntAct; F4IIM1; 4.
DR STRING; 3702.AT2G22125.1; -.
DR iPTMnet; F4IIM1; -.
DR PaxDb; F4IIM1; -.
DR PRIDE; F4IIM1; -.
DR ProMEX; F4IIM1; -.
DR ProteomicsDB; 224421; -.
DR DNASU; 816747; -.
DR EnsemblPlants; AT2G22125.1; AT2G22125.1; AT2G22125.
DR GeneID; 816747; -.
DR Gramene; AT2G22125.1; AT2G22125.1; AT2G22125.
DR KEGG; ath:AT2G22125; -.
DR Araport; AT2G22125; -.
DR TAIR; locus:2827868; AT2G22125.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_233004_0_0_1; -.
DR InParanoid; F4IIM1; -.
DR OMA; IIFPITH; -.
DR OrthoDB; 14104at2759; -.
DR PRO; PR:F4IIM1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IIM1; baseline and differential.
DR GO; GO:0010330; C:cellulose synthase complex; IDA:UniProtKB.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:UniProtKB.
DR GO; GO:0009901; P:anther dehiscence; IMP:UniProtKB.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0048467; P:gynoecium development; IMP:UniProtKB.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0048868; P:pollen tube development; IMP:UniProtKB.
DR GO; GO:0010208; P:pollen wall assembly; IMP:UniProtKB.
DR GO; GO:0072699; P:protein localization to cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 7.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR044297; CSI1/2/3.
DR PANTHER; PTHR46369; PTHR46369; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00185; ARM; 19.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF48371; SSF48371; 4.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Golgi apparatus; Growth regulation;
KW Membrane; Reference proteome; Repeat.
FT CHAIN 1..2150
FT /note="Protein CELLULOSE SYNTHASE INTERACTIVE 1"
FT /id="PRO_0000438333"
FT REPEAT 66..95
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 96..135
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 137..176
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 182..223
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REPEAT 226..265
FT /note="ARM 5"
FT /evidence="ECO:0000255"
FT REPEAT 268..308
FT /note="ARM 6"
FT /evidence="ECO:0000255"
FT REPEAT 311..359
FT /note="ARM 7"
FT /evidence="ECO:0000255"
FT REPEAT 416..441
FT /note="ARM 8"
FT /evidence="ECO:0000255"
FT REPEAT 442..480
FT /note="ARM 9"
FT /evidence="ECO:0000255"
FT REPEAT 483..522
FT /note="ARM 10"
FT /evidence="ECO:0000255"
FT REPEAT 525..564
FT /note="ARM 11"
FT /evidence="ECO:0000255"
FT REPEAT 567..606
FT /note="ARM 12"
FT /evidence="ECO:0000255"
FT REPEAT 608..638
FT /note="ARM 13"
FT /evidence="ECO:0000255"
FT REPEAT 646..685
FT /note="ARM 14"
FT /evidence="ECO:0000255"
FT REPEAT 688..727
FT /note="ARM 15"
FT /evidence="ECO:0000255"
FT REPEAT 731..770
FT /note="ARM 16"
FT /evidence="ECO:0000255"
FT REPEAT 817..858
FT /note="ARM 17"
FT /evidence="ECO:0000255"
FT REPEAT 866..907
FT /note="ARM 18"
FT /evidence="ECO:0000255"
FT REPEAT 912..952
FT /note="ARM 19"
FT /evidence="ECO:0000255"
FT REPEAT 960..1002
FT /note="ARM 20"
FT /evidence="ECO:0000255"
FT REPEAT 1017..1058
FT /note="ARM 21"
FT /evidence="ECO:0000255"
FT REPEAT 1089..1128
FT /note="ARM 22"
FT /evidence="ECO:0000255"
FT REPEAT 1132..1173
FT /note="ARM 23"
FT /evidence="ECO:0000255"
FT REPEAT 1186..1227
FT /note="ARM 24"
FT /evidence="ECO:0000255"
FT REPEAT 1230..1270
FT /note="ARM 25"
FT /evidence="ECO:0000255"
FT REPEAT 1272..1311
FT /note="ARM 26"
FT /evidence="ECO:0000255"
FT REPEAT 1313..1352
FT /note="ARM 27"
FT /evidence="ECO:0000255"
FT REPEAT 1357..1397
FT /note="ARM 28"
FT /evidence="ECO:0000255"
FT REPEAT 1399..1438
FT /note="ARM 29"
FT /evidence="ECO:0000255"
FT REPEAT 1440..1479
FT /note="ARM 30"
FT /evidence="ECO:0000255"
FT REPEAT 1482..1521
FT /note="ARM 31"
FT /evidence="ECO:0000255"
FT REPEAT 1540..1568
FT /note="ARM 32"
FT /evidence="ECO:0000255"
FT REPEAT 1569..1607
FT /note="ARM 33"
FT /evidence="ECO:0000255"
FT REPEAT 1609..1648
FT /note="ARM 34"
FT /evidence="ECO:0000255"
FT REPEAT 1650..1687
FT /note="ARM 35"
FT /evidence="ECO:0000255"
FT REPEAT 1690..1729
FT /note="ARM 36"
FT /evidence="ECO:0000255"
FT REPEAT 1732..1769
FT /note="ARM 37"
FT /evidence="ECO:0000255"
FT REPEAT 1815..1855
FT /note="ARM 38"
FT /evidence="ECO:0000255"
FT REPEAT 1858..1897
FT /note="ARM 39"
FT /evidence="ECO:0000255"
FT REPEAT 1943..1982
FT /note="ARM 40"
FT /evidence="ECO:0000255"
FT REPEAT 1991..2030
FT /note="ARM 41"
FT /evidence="ECO:0000255"
FT DOMAIN 2011..2128
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1963
FT /note="K -> E (in Ref. 4; AAR20777/AAR24766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2150 AA; 230706 MW; 9A5F129A7FD8D222 CRC64;
MTSALGWRFP STNGNGLAPS DTERNGDMKM HDSEPPTPHS TTKMSLRDRT TSMEDPDGTL
ASVAQCIEQL RQGSSSAQER EYCLKQLLDL IEMRENAFSA VGSHSQAVPV LVSLLRSGSV
GVKIQAATVL GSLCKENELR VKVLLGGCIP PLLGLLKSSS VEGQIAAAKT IYAVSEGGVK
DHVGSKIFST EGVVPVLWDQ LRSGNKKGEV DGLLTGALKN LSSTTEGFWS ETIRAGGVDV
LVKLLTSGQS STLSNVCFLL ACMMMEDASV CSSVLTADIT KQLLKLLGSG NEAPVRAEAA
AALKSLSAQS KEAKREIANS NGIPVLINAT IAPSKEFMQG EYAQALQENA MCALANISGG
LSYVISSLGQ SLESCSSPAQ TADTLGALAS ALMIYDGKAE TTRASDPLVV EQTLLKQFKP
RLPFLVQERT IEALASLYGN SILSVKLSNS DAKRLLVGLI TMAVNEVQDE LVKALLMLCN
HEGSLWQALQ GREGIQLLIS LLGLSSEQQQ ECAVALLCLL SNENDESKWA ITAAGGIPPL
VQILETGSAK AREDSATILR NLCNHSEDIR ACVESADAVP ALLWLLKNGS PNGKEIAAKT
LNHLIHKSDT ATISQLTALL TSDLPESKIY VLDALKSMLS VVPFNDMLRE GSASNDAIET
MIKLMSSGKE ETQANSASAL AAIFQSRKDL RESALALKTL LSAIKLLNVD SERILVESCR
CLAAILLSIK ENRDVAISAR EALPTIVSLA NSSVLEVAEQ GMCALANLIL DSEVSEKVIV
EDIILSATRI LREGTVSGKT LAAAAIARLL SRRRIDSALT DSVNRAGTVL TLVSLLESAD
GRSDAISEAL DALAIFSRSG ANGNVKPAWA VLAESPNSMA PIVSSIVSVA NPSLQDKAIE
VLSRLCRDQP IVLGNMVNNA RDCVSSIAKR VINTRDPKIK IGGAAIIICA AKVDDQKMIE
NLNETQLCAK FVQALVGILD SVQDQEKDEK DKICICIHPK EKEEDEEEEA TENREGSTGA
TVISGDNLAI WLLSVLSCHD EKSRAVILES EGIELITDRI GNRFLQADNG EDANIWVCAL
LLAILFQDRE ITRAHATMKA VPVLSNLVKS EEYADRYFAA QALASLVCNG SRGTLLSVAN
SGAAAGFISL LGCSDDDIKE LLQLSQEFTL VRYPDQVALE RLFRVEDIRV GATSRKAIPL
LVELLKPIPD RPGAPLLSLN LLTQLAGDCP QNMIVMVESG ALEGLSKYLS LGPQDEQEEA
ATGLLGILFS SAEIRRHESA FGAVSQLVAV LRLGGRGARY SAAKALDSLF TADHIRNAES
SRQAVQPLVE ILNTGSEREQ HAAIAALVRL LSDNPSRALA VADVEMNAVD VLCRILSSNY
TMELKGDAAE LCYVLFANTR IRSTVAAARC VEPLVSLLVT EFSPAQHSVV RALDKLVDDE
QLAELVAAHG AVVPLVGLLY GKNYVLHEAI SRALVKLGKD RPACKLEMVK AGVIDCVLDI
LHEAPDFLCA AFSELLRILT NNATIAKGQS AAKVVEPLFH LLTRLEFGAD GQHSALQVLV
NILEHPQCRA DYTLTPHQVI EPLIPLLESP SPAVQQLAAE LLSHLLYEEH LQKDPLTQLA
IGPLIHVLGS GIHLLQQRAV KALVSIALTW PNEIAKEGGV SELSKVILQA DPSLSNVLWE
SAASILVIIL QFSSEFYLEV PVAVLVRLLR SASENTVVGA LNALLVLESD DGTSAESMAE
SGAIEALLDL LRSHQCEDTA ARLLEVLLNN VKIRDSKATK TAILPLSQYL LDPQTQAQQA
RLLATLALGD LFQNEALARS TDAASACRAL VNVLEEQPTE EMKVVAICAL QNLVMYSRSN
KRAVAEAGGV QVVLDLISSS DPETSVQAAM FVKLLFSNHT VQEYASSETV RAITAAIEKD
LWATGTVNDE YLKALNSLFN NFPRLRATEP ATLSIPHLVT SLKTGSEATQ EAALDALFLL
RQAWSACPAE VSRAQSVAAA DAIPLLQYLI QSGPPRFQEK AEFLLQCLPG TLVVTIKRGN
NMKQSVGNPS VFCKITLGNN PPRQTKVIST GPNPEWDESF SWSFESPPKG QKLHISCKNK
SKMGKSSFGK VTIQIDRVVM LGAVAGEYSL LPESKSGPRN LEIEFQWSNK
