RUFY3_MOUSE
ID RUFY3_MOUSE Reviewed; 469 AA.
AC Q9D394; Q3U348; Q3UF96; Q6PE64; Q8VD10;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein RUFY3 {ECO:0000305};
DE AltName: Full=Rap2-interacting protein x {ECO:0000303|PubMed:16928684};
DE Short=RIPx {ECO:0000303|PubMed:16928684};
DE AltName: Full=Single axon-regulated protein 1 {ECO:0000250|UniProtKB:Q5FVJ0};
DE Short=Singar1 {ECO:0000250|UniProtKB:Q5FVJ0};
GN Name=Rufy3 {ECO:0000312|MGI:MGI:106484};
GN Synonyms=D5Bwg0860e, Ripx {ECO:0000303|PubMed:16928684};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 27-469 (ISOFORM 4).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Hippocampus, Medulla oblongata, and Sympathetic ganglion;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 (ISOFORMS 2 AND 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-49 AND THR-51,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-49 AND SER-53
RP (ISOFORMS 2 AND 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FSCN1 AND DBN1, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=24720729; DOI=10.1111/jnc.12740;
RA Wei Z., Sun M., Liu X., Zhang J., Jin Y.;
RT "Rufy3, a protein specifically expressed in neurons, interacts with actin-
RT bundling protein Fascin to control the growth of axons.";
RL J. Neurochem. 130:678-692(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-247.
RX PubMed=16928684; DOI=10.1074/jbc.m604960200;
RA Kukimoto-Niino M., Takagi T., Akasaka R., Murayama K., Uchikubo-Kamo T.,
RA Terada T., Inoue M., Watanabe S., Tanaka A., Hayashizaki Y., Kigawa T.,
RA Shirouzu M., Yokoyama S.;
RT "Crystal structure of the RUN domain of the RAP2-interacting protein x.";
RL J. Biol. Chem. 281:31843-31853(2006).
CC -!- FUNCTION: Plays a role in the generation of neuronal polarity formation
CC and axon growth (PubMed:24720729). Implicated in the formation of a
CC single axon by developing neurons (PubMed:24720729). May inhibit the
CC formation of additional axons by inhibition of PI3K in minor neuronal
CC processes (By similarity). Plays a role in the formation of F-actin-
CC enriched protrusive structures at the cell periphery (By similarity).
CC Plays a role in cytoskeletal organization by regulating the subcellular
CC localization of FSCN1 and DBN1 at axonal growth cones
CC (PubMed:24720729). Promotes gastric cancer cell migration and invasion
CC in a PAK1-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099,
CC ECO:0000269|PubMed:24720729}.
CC -!- SUBUNIT: Interacts (via N-terminus) with FSCN1; this interaction
CC induces neuron axon development (PubMed:24720729). Interacts with DBN1
CC (PubMed:24720729). Interacts with PAK1 (By similarity). Interacts (via
CC C-terminus) with Ras-related Rab-5 proteins (By similarity). Interacts
CC (via C-terminus) with Ras-related Rap-2 proteins (By similarity).
CC Interacts with PIK3CA and PIK3R1 (By similarity).
CC {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099,
CC ECO:0000269|PubMed:24720729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L099}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q7L099}. Cell projection,
CC invadopodium {ECO:0000250|UniProtKB:Q7L099}. Perikaryon
CC {ECO:0000269|PubMed:24720729}. Cell projection
CC {ECO:0000269|PubMed:24720729}. Cell projection, growth cone
CC {ECO:0000269|PubMed:24720729}. Cell projection, filopodium
CC {ECO:0000269|PubMed:24720729}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:24720729}. Note=Accumulates in axon growth cones in
CC a F-actin-dependent manner (PubMed:24720729). Colocalized with FSCN1
CC and F-actin at filipodia and lamellipodia of axonal growth cones
CC (PubMed:24720729). Colocalized with DBN1 and F-actin at transitional
CC domain of the axonal growth cone (PubMed:24720729). Colocalizes with
CC PAK1, F-actin, myosins and integrins in invadopodia at the cell
CC periphery (By similarity). Colocalized with Ras-related Rab-5 proteins
CC in cytoplasmic vesicles (By similarity). {ECO:0000250|UniProtKB:Q5FVJ0,
CC ECO:0000250|UniProtKB:Q7L099, ECO:0000269|PubMed:24720729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9D394-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D394-2; Sequence=VSP_019792, VSP_019794;
CC Name=3;
CC IsoId=Q9D394-3; Sequence=VSP_019793;
CC Name=4;
CC IsoId=Q9D394-4; Sequence=VSP_019792;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:24720729). {ECO:0000269|PubMed:24720729}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the embryonic brain development
CC from 11.5 dpc, onwards (PubMed:24720729). Expressed in the upper layers
CC of the cortex at 11.5 dpc (PubMed:24720729). Expressed in the
CC intermediate zone to the cortical plate of the cortex at 18.5 dpc
CC (PubMed:24720729). Expressed in neurons (at protein level)
CC (PubMed:24720729). {ECO:0000269|PubMed:24720729}.
CC -!- PTM: Phosphorylated by PAK1. Isoform 1 is partially phosphorylated.
CC {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK018184; BAB31113.1; -; mRNA.
DR EMBL; AK083242; BAC38826.1; -; mRNA.
DR EMBL; AK148795; BAE28665.1; -; mRNA.
DR EMBL; AK154941; BAE32941.1; -; mRNA.
DR EMBL; CT010404; CAJ18610.1; -; mRNA.
DR EMBL; BC017648; AAH17648.1; -; mRNA.
DR EMBL; BC049127; AAH49127.1; -; mRNA.
DR EMBL; BC058259; AAH58259.1; -; mRNA.
DR CCDS; CCDS19403.1; -. [Q9D394-1]
DR CCDS; CCDS80323.1; -. [Q9D394-4]
DR CCDS; CCDS80325.1; -. [Q9D394-3]
DR RefSeq; NP_001276704.1; NM_001289775.1. [Q9D394-4]
DR RefSeq; NP_001276705.1; NM_001289776.1. [Q9D394-3]
DR RefSeq; NP_001276706.1; NM_001289777.1. [Q9D394-3]
DR RefSeq; NP_081806.1; NM_027530.3. [Q9D394-1]
DR PDB; 2CXF; X-ray; 3.07 A; A=65-247.
DR PDB; 2CXL; X-ray; 3.20 A; A=65-247.
DR PDB; 2DWG; X-ray; 3.22 A; A/B=65-237.
DR PDB; 2DWK; X-ray; 2.00 A; A=65-237.
DR PDBsum; 2CXF; -.
DR PDBsum; 2CXL; -.
DR PDBsum; 2DWG; -.
DR PDBsum; 2DWK; -.
DR AlphaFoldDB; Q9D394; -.
DR SMR; Q9D394; -.
DR BioGRID; 206843; 12.
DR STRING; 10090.ENSMUSP00000031229; -.
DR iPTMnet; Q9D394; -.
DR PhosphoSitePlus; Q9D394; -.
DR EPD; Q9D394; -.
DR jPOST; Q9D394; -.
DR MaxQB; Q9D394; -.
DR PaxDb; Q9D394; -.
DR PeptideAtlas; Q9D394; -.
DR PRIDE; Q9D394; -.
DR ProteomicsDB; 256809; -. [Q9D394-1]
DR ProteomicsDB; 256810; -. [Q9D394-2]
DR ProteomicsDB; 256811; -. [Q9D394-3]
DR ProteomicsDB; 256812; -. [Q9D394-4]
DR ABCD; Q9D394; 3 sequenced antibodies.
DR Antibodypedia; 12878; 73 antibodies from 23 providers.
DR DNASU; 52822; -.
DR Ensembl; ENSMUST00000031229; ENSMUSP00000031229; ENSMUSG00000029291. [Q9D394-1]
DR Ensembl; ENSMUST00000196686; ENSMUSP00000143209; ENSMUSG00000029291. [Q9D394-3]
DR Ensembl; ENSMUST00000196894; ENSMUSP00000143770; ENSMUSG00000029291. [Q9D394-4]
DR Ensembl; ENSMUST00000199312; ENSMUSP00000143115; ENSMUSG00000029291. [Q9D394-3]
DR GeneID; 52822; -.
DR KEGG; mmu:52822; -.
DR UCSC; uc008xzw.2; mouse. [Q9D394-4]
DR UCSC; uc008xzx.2; mouse. [Q9D394-2]
DR UCSC; uc008xzy.2; mouse. [Q9D394-3]
DR UCSC; uc008xzz.2; mouse. [Q9D394-1]
DR CTD; 22902; -.
DR MGI; MGI:106484; Rufy3.
DR VEuPathDB; HostDB:ENSMUSG00000029291; -.
DR eggNOG; KOG4381; Eukaryota.
DR GeneTree; ENSGT00940000156035; -.
DR HOGENOM; CLU_014576_0_0_1; -.
DR InParanoid; Q9D394; -.
DR OrthoDB; 753155at2759; -.
DR PhylomeDB; Q9D394; -.
DR TreeFam; TF323904; -.
DR BioGRID-ORCS; 52822; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Rufy3; mouse.
DR EvolutionaryTrace; Q9D394; -.
DR PRO; PR:Q9D394; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D394; protein.
DR Bgee; ENSMUSG00000029291; Expressed in mammillary body and 272 other tissues.
DR ExpressionAtlas; Q9D394; baseline and differential.
DR Genevisible; Q9D394; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IDA:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IDA:UniProtKB.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50826; RUN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell projection;
KW Coiled coil; Cytoplasm; Developmental protein; Differentiation; Membrane;
KW Neurogenesis; Oncogene; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="Protein RUFY3"
FT /id="PRO_0000245834"
FT DOMAIN 95..227
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT REGION 321..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 267..464
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..60
FT /note="MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTP
FT DPEPTHED -> MAESPAPGAAAESCGEEQERGGERRPSEPLEPRGASARGADREDEAG
FT PSEPDSPVAAPFFLLYPGDGGAGFTARPPPQRAWRTPPSPGSPLPFLLLSYPSGGSGGG
FT GKHH (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019792"
FT VAR_SEQ 58
FT /note="H -> HEDSWEDLTDLVEQVRADP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019793"
FT VAR_SEQ 446..469
FT /note="SEKDLVKQAKTLNSAANKLIPKHH -> RLRQAERGRQSAELDNRLFKQDFG
FT DKINSLQLEVEALTRQRTQLELELKQEKERKSQNRGTPGKGAQKPELRMDGKHRIQEEN
FT VKLKKPLEESHRLLTHPAEEQGQPSLSEKPQVCQLCQEDDSLTKNTCRNCRGTFCNACT
FT TNELPLPSSIKPERVCNPCHEQLIKQYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019794"
FT CONFLICT 224
FT /note="M -> I (in Ref. 3; AAH17648)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> G (in Ref. 1; BAE32941)"
FT /evidence="ECO:0000305"
FT HELIX 66..90
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:2DWK"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2DWG"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2DWK"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:2DWK"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:2DWK"
FT MOD_RES Q9D394-2:27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9D394-2:49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9D394-2:53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT Q9D394-2:55
FT /note="V -> A (in Ref. 1; BAE32941)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9D394-4:27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9D394-4:49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9D394-4:53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 469 AA; 53007 MW; CFB8D2C3363D06BD CRC64;
MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL TPDPEPTHED
PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP LQQFFVVMEH CLKHGLKAKK
TFLGQNKSFW GPLELVEKLV PEAAEITASV KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM
KALINKKELL SEFYEVNALM MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM
YLKDGNSSKG SEGDGQITAI LDQKNYVEEL NRHLNATVNN LQTKVDLLEK SNTKLTEELA
VANNRIITLQ EEMERVKEES SYLLESNRKG PKQDRTAEGQ ALSEARKHLK EETQLRLDVE
KELELQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD LRALKHELAF KLQSSDLGVK
QKSELNSRLE EKTNQMAATI KQLEQSEKDL VKQAKTLNSA ANKLIPKHH
