TWF1_HUMAN
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 03-AUG-2022, entry version 193.
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";
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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; 122.
DR IntAct; Q12792; 69.
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 BioMuta; TWF1; -.
DR DMDM; 259016376; -.
DR OGP; Q12792; -.
DR EPD; Q12792; -.
DR jPOST; Q12792; -.
DR MassIVE; Q12792; -.
DR MaxQB; Q12792; -.
DR PaxDb; Q12792; -.
DR PeptideAtlas; Q12792; -.
DR PRIDE; Q12792; -.
DR ProteomicsDB; 58933; -. [Q12792-2]
DR ProteomicsDB; 58934; -. [Q12792-3]
DR ProteomicsDB; 58935; -. [Q12792-4]
DR Antibodypedia; 13271; 377 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 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; 1578109at2759; -.
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; 101 hits in 1081 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 209 other tissues.
DR ExpressionAtlas; Q12792; baseline and differential.
DR Genevisible; Q12792; HS.
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 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; 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
