SHRM_DROME
ID SHRM_DROME Reviewed; 1576 AA.
AC A1Z9P3; A1Z9P2; Q3KN39; Q7K1B1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein Shroom {ECO:0000303|PubMed:20549743, ECO:0000312|FlyBase:FBgn0085408};
GN Name=Shrm {ECO:0000303|PubMed:20549743, ECO:0000312|FlyBase:FBgn0085408};
GN Synonyms=Shroom {ECO:0000312|FlyBase:FBgn0085408};
GN ORFNames=CG34379 {ECO:0000312|FlyBase:FBgn0085408};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16684770; DOI=10.1074/jbc.m512463200;
RA Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.;
RT "Differential actin-dependent localization modulates the evolutionarily
RT conserved activity of Shroom family proteins.";
RL J. Biol. Chem. 281:20542-20554(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-667 AND SER-668, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, INTERACTION WITH F-ACTIN (ISOFORM D), SUBCELLULAR LOCATION
RP (ISOFORMS D AND F), DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=20549743; DOI=10.1002/dvdy.22326;
RA Bolinger C., Zasadil L., Rizaldy R., Hildebrand J.D.;
RT "Specific isoforms of drosophila shroom define spatial requirements for the
RT induction of apical constriction.";
RL Dev. Dyn. 239:2078-2093(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM D), DEVELOPMENTAL STAGE (ISOFORM
RP D), AND DISRUPTION PHENOTYPE (ISOFORM D).
RX PubMed=24535826; DOI=10.1083/jcb.201307070;
RA Simoes S., Mainieri A., Zallen J.A.;
RT "Rho GTPase and Shroom direct planar polarized actomyosin contractility
RT during convergent extension.";
RL J. Cell Biol. 204:575-589(2014).
RN [10] {ECO:0007744|PDB:3THF}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1393-1576, FUNCTION, SUBUNIT,
RP INTERACTION WITH ROK, SUBCELLULAR LOCATION (ISOFORM D), DOMAIN, AND
RP MUTAGENESIS OF 1402-LYS--LEU-1406; 1468-LEU--LEU-1471; 1470-SER--ALA-1476;
RP 1509-LEU--ARG-1516 AND 1546-LEU--LEU-1553.
RX PubMed=22493320; DOI=10.1091/mbc.e11-11-0937;
RA Mohan S., Rizaldy R., Das D., Bauer R.J., Heroux A., Trakselis M.A.,
RA Hildebrand J.D., VanDemark A.P.;
RT "Structure of Shroom domain 2 reveals a three-segmented coiled-coil
RT required for dimerization, Rock binding, and apical constriction.";
RL Mol. Biol. Cell 23:2131-2142(2012).
CC -!- FUNCTION: Binds to Rho-kinase Rok and targets it to the apical cell
CC cortex where it mediates apical constriction (PubMed:20549743,
CC PubMed:22493320). During embryogenic axis elongation, required for the
CC localization to adherens junctions and the establishment of planar
CC polarization of both Rho-kinase Rok and myosin regulatory light chain
CC sqh (PubMed:24535826). May be involved in the assembly of microtubule
CC arrays during cell elongation (By similarity).
CC {ECO:0000250|UniProtKB:Q27IV2, ECO:0000269|PubMed:20549743,
CC ECO:0000269|PubMed:22493320, ECO:0000269|PubMed:24535826}.
CC -!- SUBUNIT: Monomer or homodimer (PubMed:22493320). Interacts with Rok
CC (PubMed:22493320). {ECO:0000269|PubMed:22493320}.
CC -!- SUBUNIT: [Isoform D]: Binds (via N-terminus) to F-actin
CC (PubMed:20549743). {ECO:0000269|PubMed:20549743}.
CC -!- SUBCELLULAR LOCATION: [Isoform D]: Cell junction, adherens junction
CC {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320,
CC ECO:0000269|PubMed:24535826}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:20549743}. Note=In
CC adherens junctions, enriched in discrete spots and in tricellular
CC junctions (PubMed:20549743, PubMed:22493320). In adherens junctions,
CC localization requires Rho1 GTPase activity and interaction with the F-
CC actin cytoskeleton (PubMed:20549743, PubMed:24535826).
CC {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320,
CC ECO:0000269|PubMed:24535826}.
CC -!- SUBCELLULAR LOCATION: [Isoform F]: Apical cell membrane
CC {ECO:0000269|PubMed:20549743}; Peripheral membrane protein.
CC Note=Localization to the apical cell membrane depends on N-terminal
CC region (PubMed:20549743). Excluded from the lateral membrane
CC (PubMed:20549743). {ECO:0000269|PubMed:20549743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=D {ECO:0000312|FlyBase:FBgn0085408}; Synonyms=dShrmA
CC {ECO:0000303|PubMed:20549743, ECO:0000303|PubMed:22493320};
CC IsoId=A1Z9P3-3; Sequence=Displayed;
CC Name=F {ECO:0000312|FlyBase:FBgn0085408}; Synonyms=dShrmB
CC {ECO:0000303|PubMed:20549743};
CC IsoId=A1Z9P3-2; Sequence=VSP_024971, VSP_037000;
CC Name=G {ECO:0000312|FlyBase:FBgn0085408}; Synonyms=dShrmC
CC {ECO:0000303|PubMed:20549743};
CC IsoId=A1Z9P3-1; Sequence=VSP_036999, VSP_037000;
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo (at protein level)
CC (PubMed:20549743). Expressed in the dorsal trunk of the trachea (at
CC protein level) (PubMed:20549743). Isoform D: Expressed in the
CC invaginating foregut (at protein level) (PubMed:20549743). Planar
CC polarized during axis elongation from stage 7 (at protein level)
CC (PubMed:24535826). {ECO:0000269|PubMed:20549743,
CC ECO:0000269|PubMed:24535826}.
CC -!- DOMAIN: The ASD2 domain mediates the interaction with Rok and is
CC required for apical constriction induction.
CC {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320}.
CC -!- DISRUPTION PHENOTYPE: During axis elongation in the embryo decreases
CC localization to adherens junctions and planar polarization for both
CC Rho-kinase Rok and myosin regulatory light chain sqh (PubMed:24535826).
CC The mislocalization of sqh impairs the generation of sustained
CC actomyosin contractility during cell rearrangement and can account for
CC the reduction in the formation of multicellular rosette and convergent
CC extension (PubMed:24535826). RNAi-mediated knockdown in the embryo
CC decreases Rho-kinase Rok localization to adherens junctions and planar
CC polarization during axis elongation (PubMed:24535826). Has no effect on
CC Rho1 localization or activity (PubMed:24535826). Isoform D: RNAi-
CC mediated knockdown in the embryo, ecreases localization to adherens
CC junctions and planar polarization for both Rho-kinase Rok and myosin
CC regulatory light chain sqh (PubMed:24535826).
CC {ECO:0000269|PubMed:24535826}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58259.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM70999.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF58260.2; -; Genomic_DNA.
DR EMBL; AY069213; AAL39358.1; -; mRNA.
DR EMBL; BT023900; ABA81834.1; -; mRNA.
DR RefSeq; NP_001097307.1; NM_001103837.2. [A1Z9P3-3]
DR RefSeq; NP_001286417.1; NM_001299488.1. [A1Z9P3-3]
DR RefSeq; NP_610952.1; NM_137108.3. [A1Z9P3-2]
DR RefSeq; NP_725378.2; NM_166047.2. [A1Z9P3-1]
DR PDB; 3THF; X-ray; 2.70 A; A/B=1393-1576.
DR PDBsum; 3THF; -.
DR AlphaFoldDB; A1Z9P3; -.
DR SMR; A1Z9P3; -.
DR BioGRID; 62342; 13.
DR IntAct; A1Z9P3; 1.
DR STRING; 7227.FBpp0111526; -.
DR iPTMnet; A1Z9P3; -.
DR PaxDb; A1Z9P3; -.
DR DNASU; 36592; -.
DR EnsemblMetazoa; FBtr0112614; FBpp0111526; FBgn0085408. [A1Z9P3-3]
DR EnsemblMetazoa; FBtr0112616; FBpp0111528; FBgn0085408. [A1Z9P3-2]
DR EnsemblMetazoa; FBtr0290253; FBpp0288692; FBgn0085408. [A1Z9P3-1]
DR EnsemblMetazoa; FBtr0339991; FBpp0309010; FBgn0085408. [A1Z9P3-3]
DR GeneID; 36592; -.
DR KEGG; dme:Dmel_CG34379; -.
DR UCSC; CG34379-RD; d. melanogaster.
DR CTD; 36592; -.
DR FlyBase; FBgn0085408; Shrm.
DR VEuPathDB; VectorBase:FBgn0085408; -.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000167525; -.
DR HOGENOM; CLU_242240_0_0_1; -.
DR InParanoid; A1Z9P3; -.
DR OMA; PIPLMAR; -.
DR PhylomeDB; A1Z9P3; -.
DR BioGRID-ORCS; 36592; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36592; -.
DR PRO; PR:A1Z9P3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0085408; Expressed in spermathecum and 80 other tissues.
DR ExpressionAtlas; A1Z9P3; baseline and differential.
DR Genevisible; A1Z9P3; DM.
DR GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0003383; P:apical constriction; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IDA:FlyBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:FlyBase.
DR GO; GO:0032438; P:melanosome organization; ISS:UniProtKB.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:FlyBase.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR030493; Shroom.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF32; PTHR15012:SF32; 1.
DR Pfam; PF08687; ASD2; 1.
DR PROSITE; PS51307; ASD2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1576
FT /note="Protein Shroom"
FT /id="PRO_0000286069"
FT DOMAIN 1305..1572
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..920
FT /note="F-actin binding region required for planar polarity
FT and cortical localization"
FT /evidence="ECO:0000269|PubMed:20549743,
FT ECO:0000269|PubMed:24535826"
FT REGION 589..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1232..1296
FT /evidence="ECO:0000255"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..786
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2..10
FT /note="KMRNHKENG -> AQWFQWLNF (in isoform F)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_024971"
FT VAR_SEQ 2..10
FT /note="KMRNHKENG -> VFGGKFRIR (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_036999"
FT VAR_SEQ 11..917
FT /note="Missing (in isoform F and isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037000"
FT MUTAGEN 1402..1406
FT /note="KMDEL->AMDRA: Does not affect dimerization or
FT binding to Rok."
FT MUTAGEN 1468..1471
FT /note="LLSL->AASA: Loss of dimerization and binding to
FT Rok."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1470..1476
FT /note="SLSERLA->ALEEDLE: Reduces binding to Rok."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1509..1516
FT /note="LKSDIERR->AASDIEDA: Loss of binding to Rok."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1546..1553
FT /note="LIADARDL->AAADARDA: Loss of dimerization and binding
FT to Rok."
FT /evidence="ECO:0000269|PubMed:22493320"
FT HELIX 1398..1445
FT /evidence="ECO:0007829|PDB:3THF"
FT HELIX 1448..1527
FT /evidence="ECO:0007829|PDB:3THF"
FT HELIX 1530..1567
FT /evidence="ECO:0007829|PDB:3THF"
SQ SEQUENCE 1576 AA; 172713 MW; 52A7D124F9559D13 CRC64;
MKMRNHKENG NGSEMGESTK SLAKMEPENN NKISVVSVSK LLLKDSNGAN SRSSNSNASF
SSASVAGSVQ DDLPHHNSSS SQLGQQHGSS LDQCGLTQAG LEEYNNRSSS YYDQTAFHHQ
KQPSYAQSEG YHSYVSSSDS TSATPFLDKL RQESDLLSRQ SHHWSENDLS SVCSNSVAPS
PIPLLARQSH SHSHSHAHSH SNSHGHSHGH AHSASSSSSS NNNSNGSATN NNNNNSSEST
SSTETLKWLG SMSDISEASH ATGYSAISES VSSSQRIVHS SRVPTPKRHH SESVLYLHNN
EEQGDSSPTA SNSSQMMISE EANGEESPPS VQPLRIQHRH SPSYPPVHTS MVLHHFQQQQ
QQQQDYQHPS RHHTNQSTLS TQSSLLELAS PTEKPRSLMG QSHSMGDLQQ KNPHQNPMLG
RSAGQQHKSS ISVTISSSEA VVTIAPQPPA GKPSKLQLSL GKSEALSCST PNMGEQSPTN
SIDSYRSNHR LFPVSTYTEP VHSNTSQYVQ HPKPQFSSGL HKSAKLPVIT PAGATVQPTW
HSVAERINDF ERSQLGEPPK FAYLEPTKTH RLSNPALKAL QKNAVQSYVE RQQQQQKEEQ
QLLRPHSQSY QACHVERKSL PNNLSPIMVG LPTGSNSAST RDCSSPTPPP PPRRSGSLLP
NLLRRSSSAS DYAEFRELHQ AQGQVKGPSI RNISNAEKIS FNDCGMPPPP PPPRGRLAVP
TRRTSSATEY APMRDKLLLQ QAAALAHQQH HPQQHRHAQP PHVPPERPPK HPNLRVPSPE
LPPPPQSELD ISYTFDEPLP PPPPPEVLQP RPPPSPNRRN CFAGASTRRT TYEAPPPTAI
VAAKVPPLVP KKPTSLQHKH LANGGGGSRK RPHHATPQPI LENVASPVAP PPPLLPRARS
TAHDNVIASN LESNQQKRSN SKASYLPRQS LEKLNNTDPD HGIYKLTLTS NEDLVAHTKP
SYGVTGKLPN NLPDVLPLGV KLHQQPKLQP GSPNGDANVT LRYGSNNNLT GNSPTVAPPP
YYGGGQRYST PVLGQGYGKS SKPVTPQQYT RSQSYDVKHT SAVTMPTMSQ SHVDLKQAAH
DLETTLEEVL PTATPTPTPT PTPTPPRLSP ASSHSDCSLS TSSLECTINP IATPIPKPEA
HIFRAEVIST TLNTNPLTTP PKPAMNRQES LRENIEKITQ LQSVLMSAHL CDASLLGGYT
TPLITSPTAS FANEPLMTPP LPPSPPPPLE PEEEEEQEEN DVHDKQPEIE ELQLMQRSEL
VLMVNPKPST TDMACQTDEL EDRDTDLEAA REEHQTRTTL QPRQRQPIEL DYEQMSRELV
KLLPPGDKIA DILTPKICKP TSQYVSNLYN PDVPLRLAKR DVGTSTLMRM KSITSSAEIR
VVSVELQLAE PSEEPTNLIK QKMDELIKHL NQKIVSLKRE QQTISEECSA NDRLGQDLFA
KLAEKVRPSE ASKFRTHVDA VGNITSLLLS LSERLAQTES SLETRQQERG ALESKRDLLY
EQMEEAQRLK SDIERRGVSI AGLLAKNLSA DMCADYDYFI NMKAKLIADA RDLAVRIKGS
EEQLSSLSDA LVQSDC
