ID SCIN_HUMAN Reviewed; 715 AA. AC Q9Y6U3; A8K2U8; Q8NBZ6; Q8WU97; Q96JC7; Q96PY2; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 4. DT 27-MAR-2024, entry version 195. DE RecName: Full=Scinderin {ECO:0000303|PubMed:8547642}; DE AltName: Full=Adseverin {ECO:0000303|PubMed:19666531}; GN Name=SCIN {ECO:0000303|PubMed:8547642, ECO:0000312|HGNC:HGNC:21695}; GN Synonyms=KIAA1905; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Ladislas M.L., Hill S.J., Davis C.W.; RT "Isolation and characterization of human scinderin."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Tongue; 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] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11572484; DOI=10.1093/dnares/8.4.179; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXI. The RT complete sequences of 60 new cDNA clones from brain which code for large RT proteins."; RL DNA Res. 8:179-187(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-407 (ISOFORM 3), AND VARIANT ARG-61. RC TISSUE=Melanoma, and Skin; 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] RP FUNCTION. RX PubMed=8547642; RA Marcu M.G., Zhang L., Nau-Staudt K., Trifaro J.M.; RT "Recombinant scinderin, an F-actin severing protein, increases calcium- RT induced release of serotonin from permeabilized platelets, an effect RT blocked by two scinderin-derived actin-binding peptides and RT phosphatidylinositol 4,5-bisphosphate."; RL Blood 87:20-24(1996). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11568009; DOI=10.1182/blood.v98.7.2210; RA Zunino R., Li Q., Rose S.D., Romero-Benitez M.M., Lejen T., Brandan N.C., RA Trifaro J.M.; RT "Expression of scinderin in megakaryoblastic leukemia cells induces RT differentiation, maturation, and apoptosis with release of plateletlike RT particles and inhibits proliferation and tumorigenesis."; RL Blood 98:2210-2219(2001). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 345-715 IN COMPLEX WITH CALCIUM, RP AND MUTAGENESIS OF PHE-455. RX PubMed=19666531; DOI=10.1073/pnas.0812383106; RA Chumnarnsilpa S., Lee W.L., Nag S., Kannan B., Larsson M., Burtnick L.D., RA Robinson R.C.; RT "The crystal structure of the C-terminus of adseverin reveals the actin- RT binding interface."; RL Proc. Natl. Acad. Sci. U.S.A. 106:13719-13724(2009). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 6-350, FUNCTION, AND MUTAGENESIS RP OF MET-310 AND GLU-314. RX PubMed=26365202; DOI=10.1038/ncomms9254; RA Chumnarnsilpa S., Robinson R.C., Grimes J.M., Leyrat C.; RT "Calcium-controlled conformational choreography in the N-terminal half of RT adseverin."; RL Nat. Commun. 6:8254-8254(2015). CC -!- FUNCTION: Ca(2+)-dependent actin filament-severing protein that has a CC regulatory function in exocytosis by affecting the organization of the CC microfilament network underneath the plasma membrane (PubMed:8547642, CC PubMed:26365202). Severing activity is inhibited by CC phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity). In CC vitro, also has barbed end capping and nucleating activities in the CC presence of Ca(2+). Required for megakaryocyte differentiation, CC maturation, polyploidization and apoptosis with the release of CC platelet-like particles (PubMed:11568009). Plays a role in CC osteoclastogenesis (OCG) and actin cytoskeletal organization in CC osteoclasts (By similarity). Regulates chondrocyte proliferation and CC differentiation (By similarity). Inhibits cell proliferation and CC tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways CC (PubMed:11568009). {ECO:0000250|UniProtKB:Q28046, CC ECO:0000250|UniProtKB:Q5ZIV9, ECO:0000250|UniProtKB:Q60604, CC ECO:0000269|PubMed:11568009, ECO:0000269|PubMed:26365202, CC ECO:0000269|PubMed:8547642}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell CC projection, podosome {ECO:0000250|UniProtKB:Q60604}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y6U3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y6U3-2; Sequence=VSP_012427, VSP_012428; CC Name=3; CC IsoId=Q9Y6U3-3; Sequence=VSP_040548; CC -!- TISSUE SPECIFICITY: Expressed in megakaryocytes. CC {ECO:0000269|PubMed:11568009}. CC -!- MISCELLANEOUS: Scinderin comes from the latine world 'scincere', CC meaning 'to cut'. {ECO:0000305|PubMed:8547642}. CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB67798.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF276507; AAK60494.1; -; mRNA. DR EMBL; AK027778; BAB55361.1; -; mRNA. DR EMBL; AK075123; BAC11416.1; -; mRNA. DR EMBL; AK290363; BAF83052.1; -; mRNA. DR EMBL; AB067492; BAB67798.1; ALT_INIT; mRNA. DR EMBL; AC005281; AAD15423.1; -; Genomic_DNA. DR EMBL; CH471073; EAW93647.1; -; Genomic_DNA. DR EMBL; BC021090; AAH21090.1; -; mRNA. DR EMBL; BU193785; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS47545.1; -. [Q9Y6U3-1] DR CCDS; CCDS47546.1; -. [Q9Y6U3-3] DR RefSeq; NP_001106177.1; NM_001112706.2. [Q9Y6U3-1] DR RefSeq; NP_149119.1; NM_033128.3. [Q9Y6U3-3] DR PDB; 3FG6; X-ray; 3.00 A; A/B/C/D/E/F/G/H=345-715. DR PDB; 5A1K; X-ray; 2.90 A; A/B=6-349. DR PDB; 5A1M; X-ray; 1.81 A; A=247-350. DR PDBsum; 3FG6; -. DR PDBsum; 5A1K; -. DR PDBsum; 5A1M; -. DR AlphaFoldDB; Q9Y6U3; -. DR SMR; Q9Y6U3; -. DR BioGRID; 124552; 81. DR IntAct; Q9Y6U3; 16. DR MINT; Q9Y6U3; -. DR STRING; 9606.ENSP00000297029; -. DR CarbonylDB; Q9Y6U3; -. DR GlyGen; Q9Y6U3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y6U3; -. DR MetOSite; Q9Y6U3; -. DR PhosphoSitePlus; Q9Y6U3; -. DR BioMuta; SCIN; -. DR DMDM; 57015325; -. DR EPD; Q9Y6U3; -. DR jPOST; Q9Y6U3; -. DR MassIVE; Q9Y6U3; -. DR MaxQB; Q9Y6U3; -. DR PaxDb; 9606-ENSP00000297029; -. DR PeptideAtlas; Q9Y6U3; -. DR ProteomicsDB; 86789; -. [Q9Y6U3-1] DR ProteomicsDB; 86790; -. [Q9Y6U3-2] DR ProteomicsDB; 86791; -. [Q9Y6U3-3] DR Pumba; Q9Y6U3; -. DR Antibodypedia; 6300; 136 antibodies from 24 providers. DR DNASU; 85477; -. DR Ensembl; ENST00000297029.10; ENSP00000297029.5; ENSG00000006747.15. [Q9Y6U3-1] DR Ensembl; ENST00000341757.9; ENSP00000341375.5; ENSG00000006747.15. [Q9Y6U3-2] DR Ensembl; ENST00000519209.5; ENSP00000430997.1; ENSG00000006747.15. [Q9Y6U3-3] DR GeneID; 85477; -. DR KEGG; hsa:85477; -. DR MANE-Select; ENST00000297029.10; ENSP00000297029.5; NM_001112706.3; NP_001106177.1. DR UCSC; uc003ssn.5; human. [Q9Y6U3-1] DR AGR; HGNC:21695; -. DR CTD; 85477; -. DR DisGeNET; 85477; -. DR GeneCards; SCIN; -. DR HGNC; HGNC:21695; SCIN. DR HPA; ENSG00000006747; Tissue enhanced (intestine, kidney, placenta). DR MIM; 613416; gene. DR neXtProt; NX_Q9Y6U3; -. DR OpenTargets; ENSG00000006747; -. DR PharmGKB; PA134981389; -. DR VEuPathDB; HostDB:ENSG00000006747; -. DR eggNOG; KOG0443; Eukaryota. DR GeneTree; ENSGT00940000159083; -. DR HOGENOM; CLU_002568_3_0_1; -. DR InParanoid; Q9Y6U3; -. DR OMA; YPKEKET; -. DR OrthoDB; 25995at2759; -. DR PhylomeDB; Q9Y6U3; -. DR TreeFam; TF313468; -. DR PathwayCommons; Q9Y6U3; -. DR SignaLink; Q9Y6U3; -. DR BioGRID-ORCS; 85477; 14 hits in 1159 CRISPR screens. DR ChiTaRS; SCIN; human. DR EvolutionaryTrace; Q9Y6U3; -. DR GeneWiki; SCIN; -. DR GenomeRNAi; 85477; -. DR Pharos; Q9Y6U3; Tbio. DR PRO; PR:Q9Y6U3; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9Y6U3; Protein. DR Bgee; ENSG00000006747; Expressed in jejunal mucosa and 166 other cell types or tissues. DR ExpressionAtlas; Q9Y6U3; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell. DR GO; GO:0005545; F:1-phosphatidylinositol binding; TAS:UniProtKB. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB. DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB. DR GO; GO:0051693; P:actin filament capping; IMP:UniProtKB. DR GO; GO:0051014; P:actin filament severing; IMP:UniProtKB. DR GO; GO:0045010; P:actin nucleation; ISS:UniProtKB. DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central. DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:UniProtKB. DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central. DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0051127; P:positive regulation of actin nucleation; IMP:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB. DR GO; GO:0051047; P:positive regulation of secretion; ISS:UniProtKB. DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB. DR GO; GO:0042989; P:sequestering of actin monomers; IMP:UniProtKB. DR CDD; cd11290; gelsolin_S1_like; 1. DR CDD; cd11289; gelsolin_S2_like; 1. DR CDD; cd11292; gelsolin_S3_like; 1. DR CDD; cd11293; gelsolin_S4_like; 1. DR CDD; cd11288; gelsolin_S5_like; 1. DR CDD; cd11291; gelsolin_S6_like; 1. DR Gene3D; 3.40.20.10; Severin; 6. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR036180; Gelsolin-like_dom_sf. DR InterPro; IPR007122; Villin/Gelsolin. DR PANTHER; PTHR11977:SF78; SCINDERIN; 1. DR PANTHER; PTHR11977; VILLIN; 1. DR Pfam; PF00626; Gelsolin; 6. DR PRINTS; PR00597; GELSOLIN. DR SMART; SM00262; GEL; 6. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 5. DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1. DR Genevisible; Q9Y6U3; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin capping; Actin-binding; Alternative splicing; Calcium; KW Cell junction; Cell projection; Cytoplasm; Cytoskeleton; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..715 FT /note="Scinderin" FT /id="PRO_0000218744" FT REPEAT 27..76 FT /note="Gelsolin-like 1" FT REPEAT 148..188 FT /note="Gelsolin-like 2" FT REPEAT 265..307 FT /note="Gelsolin-like 3" FT REPEAT 398..451 FT /note="Gelsolin-like 4" FT REPEAT 523..564 FT /note="Gelsolin-like 5" FT REPEAT 626..668 FT /note="Gelsolin-like 6" FT REGION 1..363 FT /note="Actin-severing" FT /evidence="ECO:0000255" FT REGION 364..715 FT /note="Ca(2+)-dependent actin binding" FT BINDING 112..119 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000250" FT BINDING 138..146 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-4,5-bisphosphate)" FT /ligand_id="ChEBI:CHEBI:58456" FT /evidence="ECO:0000250" FT BINDING 538 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:3FG6" FT BINDING 539 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:3FG6" FT BINDING 562 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007744|PDB:3FG6" FT BINDING 643 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:3FG6" FT BINDING 644 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:3FG6" FT BINDING 666 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007744|PDB:3FG6" FT MOD_RES 102 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q60604" FT MOD_RES 599 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q60604" FT VAR_SEQ 1..247 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040548" FT VAR_SEQ 528..580 FT /note="VDVDANSLNSNDVFVLKLPQNSGYIWVGKGASQEEEKGAEYVASVLKCKTLR FT I -> RSSGIPLEGKKTTRPHHYWKPRLKTIHLGFTAALTKLEDLLLKRFQESSPRMI FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11572484" FT /id="VSP_012427" FT VAR_SEQ 581..715 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11572484" FT /id="VSP_012428" FT VARIANT 61 FT /note="H -> R (in dbSNP:rs2240572)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_059956" FT VARIANT 443 FT /note="A -> P (in dbSNP:rs35083013)" FT /id="VAR_059957" FT VARIANT 455 FT /note="F -> L (in dbSNP:rs17166250)" FT /id="VAR_057470" FT VARIANT 500 FT /note="K -> R (in dbSNP:rs35705332)" FT /id="VAR_059958" FT VARIANT 578 FT /note="L -> F (in dbSNP:rs1138957)" FT /id="VAR_057471" FT MUTAGEN 310 FT /note="M->D: Increases calcium-independent actin-severing FT activity." FT /evidence="ECO:0000269|PubMed:26365202" FT MUTAGEN 314 FT /note="E->S: Increases calcium-independent actin-severing FT activity." FT /evidence="ECO:0000269|PubMed:26365202" FT MUTAGEN 455 FT /note="F->D: Loss of actin-binding." FT /evidence="ECO:0000269|PubMed:19666531" FT CONFLICT 48 FT /note="V -> M (in Ref. 2; BAC11416)" FT /evidence="ECO:0000305" FT CONFLICT 476 FT /note="G -> D (in Ref. 1; AAK60494)" FT /evidence="ECO:0000305" FT CONFLICT 546 FT /note="P -> S (in Ref. 1; AAK60494)" FT /evidence="ECO:0000305" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:5A1K" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 15..24 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:5A1K" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 45..53 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:5A1K" FT HELIX 72..88 FT /evidence="ECO:0007829|PDB:5A1K" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:5A1K" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:5A1K" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:5A1K" FT TURN 122..125 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:5A1K" FT HELIX 184..202 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 206..212 FT /evidence="ECO:0007829|PDB:5A1K" FT HELIX 218..223 FT /evidence="ECO:0007829|PDB:5A1K" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 262..272 FT /evidence="ECO:0007829|PDB:5A1M" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:5A1M" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:5A1M" FT HELIX 303..319 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:5A1M" FT HELIX 338..341 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 344..346 FT /evidence="ECO:0007829|PDB:5A1M" FT STRAND 397..403 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 413..415 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 424..430 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 447..463 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 469..474 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 480..483 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 491..493 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 511..516 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 519..521 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 524..528 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 539..544 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 548..554 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 560..572 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 576..581 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 587..592 FT /evidence="ECO:0007829|PDB:3FG6" FT TURN 603..605 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 615..620 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 627..630 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 644..649 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 654..658 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 664..674 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 680..683 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 691..695 FT /evidence="ECO:0007829|PDB:3FG6" FT HELIX 701..704 FT /evidence="ECO:0007829|PDB:3FG6" FT STRAND 707..709 FT /evidence="ECO:0007829|PDB:3FG6" SQ SEQUENCE 715 AA; 80489 MW; 20420C82DB2E2D24 CRC64; MARELYHEEF ARAGKQAGLQ VWRIEKLELV PVPQSAHGDF YVGDAYLVLH TAKTSRGFTY HLHFWLGKEC SQDESTAAAI FTVQMDDYLG GKPVQNRELQ GYESNDFVSY FKGGLKYKAG GVASGLNHVL TNDLTAKRLL HVKGRRVVRA TEVPLSWDSF NKGDCFIIDL GTEIYQWCGS SCNKYERLKA NQVATGIRYN ERKGRSELIV VEEGSEPSEL IKVLGEKPEL PDGGDDDDII ADISNRKMAK LYMVSDASGS MRVTVVAEEN PFSMAMLLSE ECFILDHGAA KQIFVWKGKD ANPQERKAAM KTAEEFLQQM NYSKNTQIQV LPEGGETPIF KQFFKDWRDK DQSDGFGKVY VTEKVAQIKQ IPFDASKLHS SPQMAAQHNM VDDGSGKVEI WRVENNGRIQ VDQNSYGEFY GGDCYIILYT YPRGQIIYTW QGANATRDEL TTSAFLTVQL DRSLGGQAVQ IRVSQGKEPV HLLSLFKDKP LIIYKNGTSK KGGQAPAPPT RLFQVRRNLA SITRIVEVDV DANSLNSNDV FVLKLPQNSG YIWVGKGASQ EEEKGAEYVA SVLKCKTLRI QEGEEPEEFW NSLGGKKDYQ TSPLLETQAE DHPPRLYGCS NKTGRFVIEE IPGEFTQDDL AEDDVMLLDA WEQIFIWIGK DANEVEKKES LKSAKMYLET DPSGRDKRTP IVIIKQGHEP PTFTGWFLGW DSSKW //