ID PLST_HUMAN Reviewed; 630 AA. AC P13797; A8K579; B1AQ09; B4DGB4; B7Z6M1; Q86YI6; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 4. DT 02-NOV-2016, entry version 186. DE RecName: Full=Plastin-3; DE AltName: Full=T-plastin; GN Name=PLS3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=3211125; DOI=10.1128/MCB.8.11.4659; RA Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J.; RT "Molecular cloning and characterization of plastin, a human leukocyte RT protein expressed in transformed human fibroblasts."; RL Mol. Cell. Biol. 8:4659-4668(1988). RN [2] RP SEQUENCE REVISION. RX PubMed=2378651; DOI=10.1128/MCB.10.4.1818; RA Lin C.-S., Aebersold R.H., Leavitt J.; RT "Correction of the N-terminal sequences of the human plastin isoforms RT by using anchored polymerase chain reaction: identification of a RT potential calcium-binding domain."; RL Mol. Cell. Biol. 10:1818-1821(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 588-630. RX PubMed=8428952; RA Lin C.-S., Park T., Chen Z.P., Leavitt J.; RT "Human plastin genes. Comparative gene structure, chromosome location, RT and differential expression in normal and neoplastic cells."; RL J. Biol. Chem. 268:2781-2792(1993). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-391, AND RP IDENTIFICATION BY 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-326 AND RP THR-391, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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., RA Buerckstuemmer T., 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-326, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [12] RP POSSIBLE FUNCTION AS REGULATOR OF BONE DEVELOPMENT, POLYMORPHISM, AND RP VARIANT OSTEOP ASN-253 INS. RX PubMed=24088043; DOI=10.1056/NEJMoa1308223; RA van Dijk F.S., Zillikens M.C., Micha D., Riessland M., Marcelis C.L., RA de Die-Smulders C.E., Milbradt J., Franken A.A., Harsevoort A.J., RA Lichtenbelt K.D., Pruijs H.E., Rubio-Gozalbo M.E., Zwertbroek R., RA Moutaouakil Y., Egthuijsen J., Hammerschmidt M., Bijman R., RA Semeins C.M., Bakker A.D., Everts V., Klein-Nulend J., RA Campos-Obando N., Hofman A., te Meerman G.J., Verkerk A.J., RA Uitterlinden A.G., Maugeri A., Sistermans E.A., Waisfisz Q., RA Meijers-Heijboer H., Wirth B., Simon M.E., Pals G.; RT "PLS3 mutations in X-linked osteoporosis with fractures."; RL N. Engl. J. Med. 369:1529-1536(2013). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-375. RX PubMed=9302997; DOI=10.1038/nsb0997-708; RA Goldsmith S.C., Pokala N., Shen W., Fedorov A.A., Matsudaira P., RA Almo S.C.; RT "The structure of an actin-crosslinking domain from human fimbrin."; RL Nat. Struct. Biol. 4:708-712(1997). RN [15] RP STRUCTURE BY NMR OF 520-630. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fourth CH domain from human plastin 3 T- RT isoform."; RL Submitted (NOV-2004) to the PDB data bank. RN [16] RP VARIANT [LARGE SCALE ANALYSIS] ALA-488. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Actin-bundling protein found in intestinal microvilli, CC hair cell stereocilia, and fibroblast filopodia. May play a role CC in the regulation of bone development. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P13797-1; Sequence=Displayed; CC Name=2; CC IsoId=P13797-2; Sequence=VSP_056236, VSP_056237; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P13797-3; Sequence=VSP_056235; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in a variety of organs, including CC muscle, brain, uterus and esophagus. CC -!- POLYMORPHISM: Genetic variations in PLS3 define the bone mineral CC density quantitative trait locus 18 (BMND18) [MIM:300910]. CC Variance in bone mineral density influences bone mass, contributes CC to size determination in the general population, and is a CC susceptibility factor for osteoporotic fractures. CC {ECO:0000269|PubMed:24088043}. CC -!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal CC disorder characterized by decreased bone mass and deterioration of CC bone microarchitecture without alteration in the composition of CC bone. The result is fragile bones and an increased risk of CC fractures, even after minimal trauma. Osteoporosis is a chronic CC condition of multifactorial etiology and is usually clinically CC silent until a fracture occurs. {ECO:0000269|PubMed:24088043}. CC Note=Disease susceptibility is associated with variations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 2 actin-binding domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 4 CH (calponin-homology) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00044}. CC -!- SIMILARITY: Contains 2 EF-hand domains. {ECO:0000255|PROSITE- CC ProRule:PRU00448}. CC -!- SEQUENCE CAUTION: CC Sequence=CAI39884.1; Type=Erroneous initiation; 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; M22299; AAB02844.1; -; mRNA. DR EMBL; M34427; AAA36759.1; -; mRNA. DR EMBL; AK291194; BAF83883.1; -; mRNA. DR EMBL; AK294509; BAG57725.1; -; mRNA. DR EMBL; AK300575; BAH13307.1; -; mRNA. DR EMBL; AK312391; BAG35308.1; -; mRNA. DR EMBL; AC003983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL589842; CAI39884.1; ALT_INIT; Genomic_DNA. DR EMBL; AC005000; CAI39884.1; JOINED; Genomic_DNA. DR EMBL; CH471120; EAX02614.1; -; Genomic_DNA. DR EMBL; BC039049; AAH39049.1; -; mRNA. DR EMBL; BC056898; AAH56898.1; -; mRNA. DR EMBL; L05491; AAA61214.1; -; Genomic_DNA. DR CCDS; CCDS14568.1; -. [P13797-1] DR CCDS; CCDS78499.1; -. [P13797-2] DR PIR; A34789; A34789. DR RefSeq; NP_001129497.1; NM_001136025.4. [P13797-1] DR RefSeq; NP_001165806.1; NM_001172335.2. DR RefSeq; NP_001269266.1; NM_001282337.1. [P13797-2] DR RefSeq; NP_001269267.1; NM_001282338.1. [P13797-3] DR RefSeq; NP_005023.2; NM_005032.6. [P13797-1] DR RefSeq; XP_011535836.1; XM_011537534.1. [P13797-1] DR UniGene; Hs.496622; -. DR PDB; 1AOA; X-ray; 2.40 A; A=101-375. DR PDB; 1WJO; NMR; -; A=520-630. DR PDBsum; 1AOA; -. DR PDBsum; 1WJO; -. DR ProteinModelPortal; P13797; -. DR SMR; P13797; -. DR BioGrid; 111372; 49. DR IntAct; P13797; 14. DR MINT; MINT-3008106; -. DR STRING; 9606.ENSP00000348163; -. DR iPTMnet; P13797; -. DR PhosphoSitePlus; P13797; -. DR SwissPalm; P13797; -. DR BioMuta; PLS3; -. DR DMDM; 226694201; -. DR EPD; P13797; -. DR MaxQB; P13797; -. DR PaxDb; P13797; -. DR PeptideAtlas; P13797; -. DR PRIDE; P13797; -. DR DNASU; 5358; -. DR Ensembl; ENST00000289290; ENSP00000289290; ENSG00000102024. [P13797-2] DR Ensembl; ENST00000355899; ENSP00000348163; ENSG00000102024. [P13797-1] DR Ensembl; ENST00000539310; ENSP00000445339; ENSG00000102024. [P13797-1] DR GeneID; 5358; -. DR KEGG; hsa:5358; -. DR UCSC; uc004eqd.4; human. [P13797-1] DR CTD; 5358; -. DR DisGeNET; 5358; -. DR GeneCards; PLS3; -. DR HGNC; HGNC:9091; PLS3. DR HPA; HPA020433; -. DR MalaCards; PLS3; -. DR MIM; 166710; phenotype. DR MIM; 300131; gene. DR MIM; 300910; phenotype. DR neXtProt; NX_P13797; -. DR OpenTargets; ENSG00000102024; -. DR Orphanet; 391330; X-linked osteoporosis with fractures. DR PharmGKB; PA33418; -. DR eggNOG; KOG0046; Eukaryota. DR eggNOG; COG5069; LUCA. DR GeneTree; ENSGT00390000005691; -. DR HOGENOM; HOG000213447; -. DR HOVERGEN; HBG003082; -. DR InParanoid; P13797; -. DR KO; K17336; -. DR OMA; RNFNDPA; -. DR OrthoDB; EOG091G03YP; -. DR PhylomeDB; P13797; -. DR TreeFam; TF300680; -. DR BioCyc; ZFISH:ENSG00000102024-MONOMER; -. DR ChiTaRS; PLS3; human. DR EvolutionaryTrace; P13797; -. DR GeneWiki; PLS3; -. DR GenomeRNAi; 5358; -. DR PRO; PR:P13797; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000102024; -. DR CleanEx; HS_PLS3; -. DR ExpressionAtlas; P13797; baseline and differential. DR Genevisible; P13797; HS. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central. DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central. DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central. DR GO; GO:0060348; P:bone development; IMP:UniProtKB. DR Gene3D; 1.10.238.10; -; 1. DR Gene3D; 1.10.418.10; -; 4. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR Pfam; PF00307; CH; 4. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00033; CH; 4. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47473; SSF47473; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR PROSITE; PS00019; ACTININ_1; 2. DR PROSITE; PS00020; ACTININ_2; 2. DR PROSITE; PS50021; CH; 4. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; KW Disease mutation; Isopeptide bond; Metal-binding; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat. FT CHAIN 1 630 Plastin-3. FT /FTId=PRO_0000073747. FT DOMAIN 12 47 EF-hand 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 52 87 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 109 382 Actin-binding 1. FT DOMAIN 123 239 CH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00044}. FT DOMAIN 267 378 CH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00044}. FT DOMAIN 383 627 Actin-binding 2. FT DOMAIN 397 506 CH 3. {ECO:0000255|PROSITE- FT ProRule:PRU00044}. FT DOMAIN 518 627 CH 4. {ECO:0000255|PROSITE- FT ProRule:PRU00044}. FT CA_BIND 25 36 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 65 76 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT MOD_RES 10 10 Phosphoserine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 91 91 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 127 127 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 268 268 Phosphoserine. FT {ECO:0000250|UniProtKB:Q99K51}. FT MOD_RES 293 293 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 297 297 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 300 300 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 326 326 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 339 339 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 364 364 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 391 391 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 409 409 Phosphoserine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 475 475 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 477 477 Phosphoserine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 545 545 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT MOD_RES 582 582 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P13796}. FT VAR_SEQ 1 45 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_056235. FT VAR_SEQ 1 24 MDEMATTQISKDELDELKEAFAKV -> ME (in FT isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056236. FT VAR_SEQ 296 296 I -> IKLIDFSNSV (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056237. FT VARIANT 253 253 A -> AN (in OSTEOP; associated with FT disease susceptibility). FT {ECO:0000269|PubMed:24088043}. FT /FTId=VAR_070278. FT VARIANT 488 488 D -> A (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035462. FT HELIX 123 136 {ECO:0000244|PDB:1AOA}. FT TURN 137 139 {ECO:0000244|PDB:1AOA}. FT TURN 144 146 {ECO:0000244|PDB:1AOA}. FT TURN 151 154 {ECO:0000244|PDB:1AOA}. FT HELIX 155 159 {ECO:0000244|PDB:1AOA}. FT HELIX 160 162 {ECO:0000244|PDB:1AOA}. FT HELIX 164 173 {ECO:0000244|PDB:1AOA}. FT HELIX 180 182 {ECO:0000244|PDB:1AOA}. FT HELIX 190 206 {ECO:0000244|PDB:1AOA}. FT HELIX 216 220 {ECO:0000244|PDB:1AOA}. FT HELIX 224 244 {ECO:0000244|PDB:1AOA}. FT HELIX 261 265 {ECO:0000244|PDB:1AOA}. FT HELIX 269 283 {ECO:0000244|PDB:1AOA}. FT TURN 294 298 {ECO:0000244|PDB:1AOA}. FT HELIX 300 309 {ECO:0000244|PDB:1AOA}. FT STRAND 315 317 {ECO:0000244|PDB:1AOA}. FT TURN 326 329 {ECO:0000244|PDB:1AOA}. FT HELIX 333 344 {ECO:0000244|PDB:1AOA}. FT TURN 345 348 {ECO:0000244|PDB:1AOA}. FT HELIX 355 359 {ECO:0000244|PDB:1AOA}. FT HELIX 363 374 {ECO:0000244|PDB:1AOA}. FT HELIX 522 535 {ECO:0000244|PDB:1WJO}. FT HELIX 549 551 {ECO:0000244|PDB:1WJO}. FT HELIX 553 562 {ECO:0000244|PDB:1WJO}. FT TURN 569 571 {ECO:0000244|PDB:1WJO}. FT HELIX 579 595 {ECO:0000244|PDB:1WJO}. FT HELIX 604 609 {ECO:0000244|PDB:1WJO}. FT TURN 612 616 {ECO:0000244|PDB:1WJO}. FT HELIX 617 625 {ECO:0000244|PDB:1WJO}. SQ SEQUENCE 630 AA; 70811 MW; 631E6F803DC56A56 CRC64; MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV YALPEDLVEV KPKMVMTVFA CLMGRGMKRV //