SCIN_HUMAN
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 03-AUG-2022, entry version 186.
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};
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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; 59.
DR IntAct; Q9Y6U3; 15.
DR MINT; Q9Y6U3; -.
DR STRING; 9606.ENSP00000297029; -.
DR CarbonylDB; Q9Y6U3; -.
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; Q9Y6U3; -.
DR PeptideAtlas; Q9Y6U3; -.
DR PRIDE; Q9Y6U3; -.
DR ProteomicsDB; 86789; -. [Q9Y6U3-1]
DR ProteomicsDB; 86790; -. [Q9Y6U3-2]
DR ProteomicsDB; 86791; -. [Q9Y6U3-3]
DR Antibodypedia; 6300; 108 antibodies from 23 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 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; KNKMIFV; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q9Y6U3; -.
DR TreeFam; TF313468; -.
DR PathwayCommons; Q9Y6U3; -.
DR SignaLink; Q9Y6U3; -.
DR BioGRID-ORCS; 85477; 13 hits in 1081 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 164 other tissues.
DR ExpressionAtlas; Q9Y6U3; baseline and differential.
DR Genevisible; Q9Y6U3; HS.
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 Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR030012; Adseverin.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF78; PTHR11977:SF78; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SUPFAM; SSF82754; SSF82754; 1.
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
