TWF1_MOUSE
ID TWF1_MOUSE Reviewed; 350 AA.
AC Q91YR1; O09132; Q52L77; Q80X09;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Twinfilin-1;
DE AltName: Full=Protein A6;
GN Name=Twf1; Synonyms=Ptk9;
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 {ECO:0000312|EMBL:AAH15081.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9249064; DOI=10.1016/s0378-1119(97)00073-5;
RA Beeler J.F., Patel B.K.R., Chedid M., LaRochelle W.J.;
RT "Cloning and characterization of the mouse homolog of the human A6 gene.";
RL Gene 193:31-37(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TWF2 AND
RP PHOSPHOINOSITIDE, AND DEVELOPMENTAL STAGE.
RX PubMed=12807912; DOI=10.1074/jbc.m303642200;
RA Vartiainen M.K., Sarkkinen E.M., Matilainen T., Salminen M.,
RA Lappalainen P.;
RT "Mammals have two twinfilin isoforms whose subcellular localizations and
RT tissue distributions are differentially regulated.";
RL J. Biol. Chem. 278:34347-34355(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-51.
RC STRAIN=NMRI; TISSUE=Mammary gland, and Mammary tumor;
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH G-ACTIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10669753; DOI=10.1128/mcb.20.5.1772-1783.2000;
RA Vartiainen M., Ojala P.J., Auvinen P., Peranen J., Lappalainen P.;
RT "Mouse A6/twinfilin is an actin monomer-binding protein that localizes to
RT the regions of rapid actin dynamics.";
RL Mol. Cell. Biol. 20:1772-1783(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
RX PubMed=15282541; DOI=10.1038/sj.emboj.7600310;
RA Falck S., Paavilainen V.O., Wear M.A., Grossmann J.G., Cooper J.A.,
RA Lappalainen P.;
RT "Biological role and structural mechanism of twinfilin-capping protein
RT interaction.";
RL EMBO J. 23:3010-3019(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
RX PubMed=16511569; DOI=10.1038/sj.emboj.7601019;
RA Helfer E., Nevalainen E.M., Naumanen P., Romero S., Didry D., Pantaloni D.,
RA Lappalainen P., Carlier M.-F.;
RT "Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends:
RT implications in motility.";
RL EMBO J. 25:1184-1195(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [12]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-142.
RX PubMed=12207032; DOI=10.1074/jbc.m208225200;
RA Paavilainen V.O., Merckel M.C., Falck S., Ojala P.J., Pohl E., Wilmanns M.,
RA Lappalainen P.;
RT "Structural conservation between the actin monomer-binding sites of
RT twinfilin and actin-depolymerizing factor (ADF)/cofilin.";
RL J. Biol. Chem. 277:43089-43095(2002).
RN [13]
RP STRUCTURE BY NMR OF 161-313.
RX PubMed=19768801; DOI=10.1002/pro.248;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
RA Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
RT "NMR solution structures of actin depolymerizing factor homology domains.";
RL Protein Sci. 18:2384-2392(2009).
CC -!- FUNCTION: Actin-binding protein involved in motile and morphological
CC processes. Inhibits actin polymerization, likely by sequestering G-
CC actin. By capping the barbed ends of filaments, it also regulates
CC motility. Seems to play an important role in clathrin-mediated
CC endocytosis and distribution of endocytic organelles.
CC {ECO:0000269|PubMed:10669753, ECO:0000269|PubMed:15282541,
CC ECO:0000269|PubMed:16511569, ECO:0000269|PubMed:9249064}.
CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein
CC (CP) (PubMed:12807912, PubMed:15282541, PubMed:16511569). May also be
CC able to interact with TWF2 and phosphoinositides, PI(4,5)P2
CC (PubMed:12807912). When bound to PI(4,5)P2, it is down-regulated
CC (PubMed:12807912). Interacts with ACTG1 (By similarity).
CC {ECO:0000250|UniProtKB:Q12792, ECO:0000269|PubMed:10669753,
CC ECO:0000269|PubMed:12807912, ECO:0000269|PubMed:15282541,
CC ECO:0000269|PubMed:16511569}.
CC -!- INTERACTION:
CC Q91YR1; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-527441, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10669753}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10669753}. Note=Diffuse
CC cytoplasmic localization with perinuclear and G-actin-rich cortical
CC actin structures sublocalization. Also found at membrane ruffles and
CC cell-cell contacts.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC liver and kidney. Also expressed in heart, lung and testis. Not
CC detected in spleen or skeletal muscle. {ECO:0000269|PubMed:10669753,
CC ECO:0000269|PubMed:12807912, ECO:0000269|PubMed:9249064}.
CC -!- DEVELOPMENTAL STAGE: Expression was widespread throughout the embryonic
CC stages analyzed; 10.5 dpc, 12.5 dpc, 14.5 dpc and 18.5 dpc. At 14.5
CC dpc, strongest expression was observed in the developing central and
CC peripheral nervous system (CNS and PNS, respectively) and in the
CC olfactory sensory epithelium. In the CNS, the proliferating neuronal
CC precursors in the ventricular zone expressed it more than the
CC postmitotic neurons. At 18.5 dpc, highest expression levels were
CC detected in the mechanosensory hair cells of the inner ear and in the
CC differentiated keratinocytes of the skin.
CC {ECO:0000269|PubMed:12807912}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:Q12792}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace - Issue 73
CC of August 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/073";
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DR EMBL; U82324; AAB66592.1; -; mRNA.
DR EMBL; AY267188; AAP31404.1; -; mRNA.
DR EMBL; AK147990; BAE28272.1; -; mRNA.
DR EMBL; AK150852; BAE29908.1; -; mRNA.
DR EMBL; BC015081; AAH15081.1; -; mRNA.
DR EMBL; BC094034; AAH94034.1; -; mRNA.
DR CCDS; CCDS27773.1; -.
DR RefSeq; NP_032997.3; NM_008971.4.
DR PDB; 1M4J; X-ray; 1.60 A; A/B=1-142.
DR PDB; 2D8B; NMR; -; A=161-313.
DR PDB; 2HD7; NMR; -; A=176-316.
DR PDB; 3DAW; X-ray; 2.55 A; B=167-322.
DR PDB; 6RSW; X-ray; 1.95 A; B=176-316.
DR PDB; 6YP9; X-ray; 2.56 A; B=176-315.
DR PDB; 7DS2; X-ray; 1.95 A; C=315-350.
DR PDB; 7DS4; X-ray; 1.85 A; C=315-344.
DR PDB; 7DS6; X-ray; 1.69 A; C=315-327.
DR PDB; 7DS8; X-ray; 1.95 A; C=328-344.
DR PDB; 7DSB; X-ray; 2.44 A; D=315-344.
DR PDBsum; 1M4J; -.
DR PDBsum; 2D8B; -.
DR PDBsum; 2HD7; -.
DR PDBsum; 3DAW; -.
DR PDBsum; 6RSW; -.
DR PDBsum; 6YP9; -.
DR PDBsum; 7DS2; -.
DR PDBsum; 7DS4; -.
DR PDBsum; 7DS6; -.
DR PDBsum; 7DS8; -.
DR PDBsum; 7DSB; -.
DR AlphaFoldDB; Q91YR1; -.
DR SMR; Q91YR1; -.
DR BioGRID; 202468; 11.
DR DIP; DIP-33923N; -.
DR IntAct; Q91YR1; 6.
DR MINT; Q91YR1; -.
DR STRING; 10090.ENSMUSP00000023087; -.
DR iPTMnet; Q91YR1; -.
DR PhosphoSitePlus; Q91YR1; -.
DR SwissPalm; Q91YR1; -.
DR EPD; Q91YR1; -.
DR jPOST; Q91YR1; -.
DR MaxQB; Q91YR1; -.
DR PaxDb; Q91YR1; -.
DR PeptideAtlas; Q91YR1; -.
DR PRIDE; Q91YR1; -.
DR ProteomicsDB; 298037; -.
DR Antibodypedia; 13271; 377 antibodies from 30 providers.
DR DNASU; 19230; -.
DR Ensembl; ENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
DR GeneID; 19230; -.
DR KEGG; mmu:19230; -.
DR UCSC; uc007xjl.1; mouse.
DR CTD; 5756; -.
DR MGI; MGI:1100520; Twf1.
DR VEuPathDB; HostDB:ENSMUSG00000022451; -.
DR eggNOG; KOG1747; Eukaryota.
DR GeneTree; ENSGT00530000063868; -.
DR HOGENOM; CLU_031995_1_0_1; -.
DR InParanoid; Q91YR1; -.
DR OMA; VKKDWER; -.
DR OrthoDB; 1578109at2759; -.
DR PhylomeDB; Q91YR1; -.
DR TreeFam; TF352598; -.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR BioGRID-ORCS; 19230; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Twf1; mouse.
DR EvolutionaryTrace; Q91YR1; -.
DR PRO; PR:Q91YR1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91YR1; protein.
DR Bgee; ENSMUSG00000022451; Expressed in utricle of membranous labyrinth and 266 other tissues.
DR ExpressionAtlas; Q91YR1; baseline and differential.
DR Genevisible; Q91YR1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR GO; GO:0030016; C:myofibril; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:BHF-UCL.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:BHF-UCL.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0043538; P:regulation of actin phosphorylation; ISO:MGI.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:BHF-UCL.
DR Gene3D; 3.40.20.10; -; 2.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028458; Twinfilin.
DR PANTHER; PTHR13759; PTHR13759; 1.
DR Pfam; PF00241; Cofilin_ADF; 2.
DR SMART; SM00102; ADF; 2.
DR PROSITE; PS51263; ADF_H; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT CHAIN 2..350
FT /note="Twinfilin-1"
FT /id="PRO_0000214951"
FT DOMAIN 2..139
FT /note="ADF-H 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 175..313
FT /note="ADF-H 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 317..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12792"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJR2"
FT MOD_RES 309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:18034455"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT VARIANT 51
FT /note="Q -> H"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 345
FT /note="A -> R (in Ref. 1; AAB66592 and 2; AAP31404)"
FT /evidence="ECO:0000305"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1M4J"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:1M4J"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1M4J"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1M4J"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:1M4J"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1M4J"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:1M4J"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6RSW"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2D8B"
FT HELIX 266..287
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7DS2"
SQ SEQUENCE 350 AA; 40079 MW; 643CBBA18D38D4E0 CRC64;
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE QDYDSFVLPL
LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE
VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVSVDT KHQTLQGVAF
PISRDAFQAL EKLSKKQLNY VQLEIDIKNE TIILANTENT ELRDLPKRIP KDSARYHFFL
YKHSHEGDYL ESVVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD VIRKIEIDNG
DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD
