ID TWF1_HUMAN Reviewed; 350 AA. AC Q12792; A8K5A8; B3KXS6; B4DLX9; Q59G07; Q5U0B1; Q6FHJ1; Q6FHL6; Q6NUK9; AC Q86XL6; Q8TCD3; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 3. DT 27-MAR-2024, entry version 202. DE RecName: Full=Twinfilin-1; DE AltName: Full=Protein A6; DE AltName: Full=Protein tyrosine kinase 9; GN Name=TWF1; Synonyms=PTK9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC50062.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP PHOSPHORYLATION. RC TISSUE=Lung fibroblast; RX PubMed=7507208; DOI=10.1128/mcb.14.2.982-988.1994; RA Beeler J.F., LaRochelle W.J., Chedid M., Tronick S.R., Aaronson S.A.; RT "Prokaryotic expression cloning of a novel human tyrosine kinase."; RL Mol. Cell. Biol. 14:982-988(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Brain, Placenta, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Prostate, and Testis; 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 [7] {ECO:0000305} RP PROTEIN SEQUENCE OF 2-37 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 65-72; 99-105; RP 111-155; 172-192; 236-242 AND 279-285 (ISOFORMS 1/3), PROTEIN SEQUENCE OF RP 159-171 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Calvo F., Kolch W.; RL Submitted (MAR-2008) to UniProtKB. RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP VARIANT SER-349 (ISOFORM 3), CHARACTERIZATION OF VARIANT SER-349 (ISOFORM RP 3), AND INTERACTION WITH ACTG1. RX PubMed=28493397; DOI=10.1002/humu.23246; RG UK10K; RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D., RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M., RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G., RA FitzPatrick D.R.; RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma."; RL Hum. Mutat. 38:942-946(2017). 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 (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping protein CC (CP). May also be able to interact with TWF2 and phosphoinositides, CC PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated (By CC similarity). Interacts with ACTG1 (PubMed:28493397). CC {ECO:0000250|UniProtKB:Q91YR1, ECO:0000269|PubMed:28493397}. CC -!- INTERACTION: CC Q12792; P67870: CSNK2B; NbExp=3; IntAct=EBI-1056675, EBI-348169; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}. CC Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich CC cortical actin structures sublocalization. Also found at membrane CC ruffles and cell-cell contacts (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1 {ECO:0000305}; CC IsoId=Q12792-2; Sequence=Displayed; CC Name=3; CC IsoId=Q12792-3; Sequence=VSP_017899; CC Name=4; CC IsoId=Q12792-4; Sequence=VSP_038075; CC -!- TISSUE SPECIFICITY: Expressed at high levels in the colon, testis, CC ovary, prostate and lung. Expressed at lower levels in the brain, CC bladder and heart. Not detected in liver. {ECO:0000269|PubMed:7507208}. CC -!- PTM: Phosphorylated on serine and threonine residues. CC {ECO:0000269|PubMed:7507208}. CC -!- DISEASE: Note=Defects in TWF1 has been found in a patient with isolated CC coloboma, a defect of the eye characterized by the absence of ocular CC structures due to abnormal morphogenesis of the optic cup and stalk, CC and the fusion of the fetal fissure (optic fissure). Isolated colobomas CC may be associated with an abnormally small eye (microphthalmia) or CC small cornea. {ECO:0000269|PubMed:28493397}. CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. Twinfilin CC subfamily. {ECO:0000305}. CC -!- CAUTION: Was originally thought to have protein tyrosine kinase CC activity. {ECO:0000305|PubMed:7507208}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH43148.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH68548.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAD92539.1; Type=Erroneous initiation; Evidence={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"; 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; U02680; AAC50062.1; -; mRNA. DR EMBL; AK127868; BAG54588.1; -; mRNA. DR EMBL; AK291223; BAF83912.1; -; mRNA. DR EMBL; AK297206; BAG59691.1; -; mRNA. DR EMBL; CR541736; CAG46536.1; -; mRNA. DR EMBL; CR541761; CAG46561.1; -; mRNA. DR EMBL; BT019691; AAV38497.1; -; mRNA. DR EMBL; AB209302; BAD92539.1; ALT_INIT; mRNA. DR EMBL; BC022344; AAH22344.1; -; mRNA. DR EMBL; BC043148; AAH43148.2; ALT_INIT; mRNA. DR EMBL; BC068548; AAH68548.1; ALT_INIT; mRNA. DR CCDS; CCDS31780.2; -. [Q12792-2] DR CCDS; CCDS55818.1; -. [Q12792-3] DR PIR; A55922; A55922. DR RefSeq; NP_001229326.1; NM_001242397.1. [Q12792-3] DR RefSeq; NP_002813.3; NM_002822.4. [Q12792-2] DR PDB; 7CCC; X-ray; 3.20 A; B=1-350. DR PDBsum; 7CCC; -. DR AlphaFoldDB; Q12792; -. DR SMR; Q12792; -. DR BioGRID; 111723; 170. DR IntAct; Q12792; 74. DR MINT; Q12792; -. DR STRING; 9606.ENSP00000449428; -. DR GlyGen; Q12792; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q12792; -. DR PhosphoSitePlus; Q12792; -. DR SwissPalm; Q12792; -. DR BioMuta; TWF1; -. DR DMDM; 259016376; -. DR OGP; Q12792; -. DR EPD; Q12792; -. DR jPOST; Q12792; -. DR MassIVE; Q12792; -. DR MaxQB; Q12792; -. DR PaxDb; 9606-ENSP00000449428; -. DR PeptideAtlas; Q12792; -. DR ProteomicsDB; 58933; -. [Q12792-2] DR ProteomicsDB; 58934; -. [Q12792-3] DR ProteomicsDB; 58935; -. [Q12792-4] DR Pumba; Q12792; -. DR Antibodypedia; 13271; 433 antibodies from 30 providers. DR DNASU; 5756; -. DR Ensembl; ENST00000395510.7; ENSP00000378886.2; ENSG00000151239.14. [Q12792-2] DR Ensembl; ENST00000548315.5; ENSP00000449428.1; ENSG00000151239.14. [Q12792-3] DR Ensembl; ENST00000552521.5; ENSP00000448750.1; ENSG00000151239.14. [Q12792-4] DR GeneID; 5756; -. DR KEGG; hsa:5756; -. DR MANE-Select; ENST00000395510.7; ENSP00000378886.2; NM_002822.5; NP_002813.3. DR UCSC; uc001roa.4; human. [Q12792-2] DR AGR; HGNC:9620; -. DR CTD; 5756; -. DR DisGeNET; 5756; -. DR GeneCards; TWF1; -. DR HGNC; HGNC:9620; TWF1. DR HPA; ENSG00000151239; Low tissue specificity. DR MIM; 610932; gene. DR neXtProt; NX_Q12792; -. DR OpenTargets; ENSG00000151239; -. DR PharmGKB; PA162407406; -. DR VEuPathDB; HostDB:ENSG00000151239; -. DR eggNOG; KOG1747; Eukaryota. DR GeneTree; ENSGT00530000063868; -. DR InParanoid; Q12792; -. DR OMA; VKKDWER; -. DR OrthoDB; 5360875at2759; -. DR PhylomeDB; Q12792; -. DR TreeFam; TF352598; -. DR PathwayCommons; Q12792; -. DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; Q12792; -. DR BioGRID-ORCS; 5756; 103 hits in 1157 CRISPR screens. DR ChiTaRS; TWF1; human. DR GeneWiki; TWF1; -. DR GenomeRNAi; 5756; -. DR Pharos; Q12792; Tbio. DR PRO; PR:Q12792; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q12792; Protein. DR Bgee; ENSG00000151239; Expressed in secondary oocyte and 211 other cell types or tissues. DR ExpressionAtlas; Q12792; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0005911; C:cell-cell junction; ISS:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030175; C:filopodium; ISS:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL. DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0003785; F:actin monomer binding; ISS:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL. DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central. DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:BHF-UCL. DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl. DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central. DR GO; GO:0043538; P:regulation of actin phosphorylation; IDA:BHF-UCL. DR GO; GO:0010591; P:regulation of lamellipodium assembly; IBA:GO_Central. DR GO; GO:0042989; P:sequestering of actin monomers; ISS:BHF-UCL. DR CDD; cd11284; ADF_Twf-C_like; 1. DR CDD; cd11285; ADF_Twf-N_like; 1. DR Gene3D; 3.40.20.10; Severin; 2. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR028458; Twinfilin. DR PANTHER; PTHR13759; TWINFILIN; 1. DR PANTHER; PTHR13759:SF8; TWINFILIN-1; 1. DR Pfam; PF00241; Cofilin_ADF; 2. DR SMART; SM00102; ADF; 2. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 2. DR PROSITE; PS51263; ADF_H; 2. DR Genevisible; Q12792; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Disease variant; Phosphoprotein; KW Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..350 FT /note="Twinfilin-1" FT /id="PRO_0000214950" 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 316..350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" 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:19690332" FT MOD_RES 349 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..98 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_038075" FT VAR_SEQ 161 FT /note="E -> ESPEDHIG (in isoform 3)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_017899" FT CONFLICT 12 FT /note="D -> Y (in Ref. 3; CAG46561)" FT /evidence="ECO:0000305" FT CONFLICT 246 FT /note="E -> V (in Ref. 2; BAG54588)" FT /evidence="ECO:0000305" FT CONFLICT 269 FT /note="R -> W (in Ref. 3; CAG46536)" FT /evidence="ECO:0000305" FT CONFLICT 302 FT /note="E -> G (in Ref. 2; BAF83912)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="P -> H (in Ref. 2; BAG59691)" FT /evidence="ECO:0000305" FT HELIX 11..20 FT /evidence="ECO:0007829|PDB:7CCC" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 26..33 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 49..57 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 67..76 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 78..88 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 95..103 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 105..112 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 117..125 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 131..141 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 149..166 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 199..206 FT /evidence="ECO:0007829|PDB:7CCC" FT TURN 207..210 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:7CCC" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 235..245 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 248..258 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 266..286 FT /evidence="ECO:0007829|PDB:7CCC" FT STRAND 291..299 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:7CCC" FT HELIX 305..312 FT /evidence="ECO:0007829|PDB:7CCC" FT VARIANT Q12792-3:349 FT /note="P -> S (found in a patient with isolated coloboma, FT increases interaction with ACTG1)" FT /evidence="ECO:0000269|PubMed:28493397" FT /id="VAR_082792" SQ SEQUENCE 350 AA; 40283 MW; 5F68A6946E969A80 CRC64; MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVIG SYSQPSDSWD KDYDSFVLPL LEDKQPCYIL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVGVDT KHQTLQGVAF PISREAFQAL EKLNNRQLNY VQLEIDIKNE IIILANTTNT ELKDLPKRIP KDSARYHFFL YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSRLL EIVERQLQMD VIRKIEIDNG DELTADFLYE EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAETEATTD //