PLST_HUMAN
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 03-AUG-2022, entry version 228.
DE RecName: Full=Plastin-3;
DE AltName: Full=T-plastin;
GN Name=PLS3;
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), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3211125; DOI=10.1128/mcb.8.11.4659-4668.1988;
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.10.4.1818-1821.1990;
RA Lin C.-S., Aebersold R.H., Leavitt J.;
RT "Correction of the N-terminal sequences of the human plastin isoforms by
RT using anchored polymerase chain reaction: identification of a potential
RT 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., 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 [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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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., 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 (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 project:
RT 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; DOI=10.1016/s0021-9258(18)53842-4;
RA Lin C.-S., Park T., Chen Z.P., Leavitt J.;
RT "Human plastin genes. Comparative gene structure, chromosome location, and
RT 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 THR-391, AND
RP IDENTIFICATION BY 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 [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., 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 [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., Semeins C.M.,
RA Bakker A.D., Everts V., Klein-Nulend J., Campos-Obando N., Hofman A.,
RA te Meerman G.J., Verkerk A.J., Uitterlinden A.G., Maugeri A.,
RA Sistermans E.A., Waisfisz Q., Meijers-Heijboer H., Wirth B., Simon M.E.,
RA 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 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 [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., 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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Actin-bundling protein found in intestinal microvilli, hair
CC cell stereocilia, and fibroblast filopodia. May play a role in the
CC 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 Name=3;
CC IsoId=P13797-3; Sequence=VSP_056235;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of organs, including muscle,
CC brain, uterus and esophagus.
CC -!- POLYMORPHISM: Genetic variations in PLS3 define the bone mineral
CC density quantitative trait locus 18 (BMND18) [MIM:300910]. Variance in
CC bone mineral density influences bone mass, contributes to size
CC determination in the general population, and is a susceptibility factor
CC for osteoporotic fractures. {ECO:0000269|PubMed:24088043}.
CC -!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal
CC disorder characterized by decreased bone mass and deterioration of bone
CC microarchitecture without alteration in the composition of bone. The
CC result is fragile bones and an increased risk of fractures, even after
CC minimal trauma. Osteoporosis is a chronic condition of multifactorial
CC etiology and is usually clinically silent until a fracture occurs.
CC {ECO:0000269|PubMed:24088043}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
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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; AC005000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589842; -; NOT_ANNOTATED_CDS; 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.
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 AlphaFoldDB; P13797; -.
DR BMRB; P13797; -.
DR SMR; P13797; -.
DR BioGRID; 111372; 132.
DR IntAct; P13797; 39.
DR MINT; P13797; -.
DR STRING; 9606.ENSP00000348163; -.
DR GlyGen; P13797; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13797; -.
DR MetOSite; P13797; -.
DR PhosphoSitePlus; P13797; -.
DR SwissPalm; P13797; -.
DR BioMuta; PLS3; -.
DR DMDM; 226694201; -.
DR EPD; P13797; -.
DR jPOST; P13797; -.
DR MassIVE; P13797; -.
DR MaxQB; P13797; -.
DR PaxDb; P13797; -.
DR PeptideAtlas; P13797; -.
DR PRIDE; P13797; -.
DR ProteomicsDB; 4120; -.
DR ProteomicsDB; 52987; -. [P13797-1]
DR ProteomicsDB; 6788; -.
DR Antibodypedia; 44530; 248 antibodies from 26 providers.
DR DNASU; 5358; -.
DR Ensembl; ENST00000289290.7; ENSP00000289290.4; ENSG00000102024.19. [P13797-2]
DR Ensembl; ENST00000355899.8; ENSP00000348163.3; ENSG00000102024.19. [P13797-1]
DR Ensembl; ENST00000539310.5; ENSP00000445339.2; ENSG00000102024.19. [P13797-1]
DR GeneID; 5358; -.
DR KEGG; hsa:5358; -.
DR MANE-Select; ENST00000355899.8; ENSP00000348163.3; NM_005032.7; NP_005023.2.
DR UCSC; uc004eqd.4; human. [P13797-1]
DR CTD; 5358; -.
DR DisGeNET; 5358; -.
DR GeneCards; PLS3; -.
DR HGNC; HGNC:9091; PLS3.
DR HPA; ENSG00000102024; Low tissue specificity.
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 VEuPathDB; HostDB:ENSG00000102024; -.
DR eggNOG; KOG0046; Eukaryota.
DR GeneTree; ENSGT00950000183097; -.
DR InParanoid; P13797; -.
DR OMA; TVNHLYV; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; P13797; -.
DR TreeFam; TF300680; -.
DR PathwayCommons; P13797; -.
DR SignaLink; P13797; -.
DR BioGRID-ORCS; 5358; 12 hits in 698 CRISPR screens.
DR ChiTaRS; PLS3; human.
DR EvolutionaryTrace; P13797; -.
DR GeneWiki; PLS3; -.
DR GenomeRNAi; 5358; -.
DR Pharos; P13797; Tbio.
DR PRO; PR:P13797; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P13797; protein.
DR Bgee; ENSG00000102024; Expressed in blood vessel layer and 208 other tissues.
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:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP02682; -.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR InterPro; IPR039956; PLS2/3.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR PANTHER; PTHR19961:SF32; PTHR19961:SF32; 1.
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; Actin-binding; Alternative splicing; Calcium; Cytoplasm;
KW Direct protein sequencing; Disease variant; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..630
FT /note="Plastin-3"
FT /id="PRO_0000073747"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..239
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 267..378
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 397..506
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 518..627
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 109..382
FT /note="Actin-binding 1"
FT REGION 383..627
FT /note="Actin-binding 2"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99K51"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056235"
FT VAR_SEQ 1..24
FT /note="MDEMATTQISKDELDELKEAFAKV -> ME (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056236"
FT VAR_SEQ 296
FT /note="I -> IKLIDFSNSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056237"
FT VARIANT 253
FT /note="A -> AN (in OSTEOP; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:24088043"
FT /id="VAR_070278"
FT VARIANT 488
FT /note="D -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035462"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 224..244
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 294..298
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1AOA"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:1AOA"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:1AOA"
FT HELIX 522..535
FT /evidence="ECO:0007829|PDB:1WJO"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:1WJO"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:1WJO"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:1WJO"
FT HELIX 579..595
FT /evidence="ECO:0007829|PDB:1WJO"
FT HELIX 604..609
FT /evidence="ECO:0007829|PDB:1WJO"
FT TURN 612..616
FT /evidence="ECO:0007829|PDB:1WJO"
FT HELIX 617..625
FT /evidence="ECO:0007829|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
