ID PLSL_HUMAN Reviewed; 627 AA. AC P13796; B2R613; B4DUA0; Q5TBN4; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 6. DT 27-MAR-2024, entry version 243. DE RecName: Full=Plastin-2; DE AltName: Full=L-plastin; DE AltName: Full=LC64P; DE AltName: Full=Lymphocyte cytosolic protein 1; DE Short=LCP-1; GN Name=LCP1; Synonyms=PLS2; 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 VARIANT GLU-533. RX PubMed=2252891; DOI=10.1021/bi00488a017; RA Zu Y., Shigesada K., Nishida E., Kubota I., Kohno M., Hanaoka M., Namba Y.; RT "65-kilodalton protein phosphorylated by interleukin 2 stimulation bears RT two putative actin-binding sites and two calcium-binding sites."; RL Biochemistry 29:8319-8324(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP GLU-533. RC TISSUE=Amygdala, and Prostate; 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 GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-533. RC TISSUE=Lymph, and Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-627 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, RP AND VARIANT GLU-533. 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-140 (ISOFORM 1), AND 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 [8] RP PROTEIN SEQUENCE OF 2-14; 20-31; 184-192 AND 534-541, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627. 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 [10] RP PROTEIN SEQUENCE OF 264-283; 517-533 AND 593-609, AND VARIANT GLU-533. RX PubMed=2111166; DOI=10.1021/bi00456a030; RA Zu Y., Kohno M., Kubota I., Nishida E., Hanaoka M., Namba Y.; RT "Characterization of interleukin 2 stimulated 65-kilodalton phosphoprotein RT in human T cells."; RL Biochemistry 29:1055-1062(1990). RN [11] RP PROTEIN SEQUENCE OF 590-611, AND TISSUE SPECIFICITY. RX PubMed=3261603; DOI=10.1021/bi00410a037; RA Matsushima K., Shiroo M., Kung H.F., Copeland T.D.; RT "Purification and characterization of a cytosolic 65-kilodalton RT phosphoprotein in human leukocytes whose phosphorylation is augmented by RT stimulation with interleukin 1."; RL Biochemistry 27:3765-3770(1988). RN [12] RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION RP WITH BCL6. RX PubMed=10469447; RX DOI=10.1002/(sici)1098-2264(199910)26:2<97::aid-gcc1>3.3.co;2-0; RA Galiegue-Zouitina S., Quief S., Hildebrand M.P., Denis C., RA Detourmignies L., Lai J.L., Kerckaert J.P.; RT "Nonrandom fusion of L-plastin(LCP1) and LAZ3(BCL6) genes by RT t(3;13)(q27;q14) chromosome translocation in two cases of B-cell non- RT Hodgkin lymphoma."; RL Genes Chromosomes Cancer 26:97-105(1999). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [15] RP FUNCTION, ACTIN-BINDING, INTERACTION WITH ACTIN FIBERS, SUBCELLULAR RP LOCATION, MUTAGENESIS OF SER-5, AND PHOSPHORYLATION AT SER-5. RX PubMed=16636079; DOI=10.1242/jcs.02874; RA Janji B., Giganti A., De Corte V., Catillon M., Bruyneel E., Lentz D., RA Plastino J., Gettemans J., Friederich E.; RT "Phosphorylation on Ser5 increases the F-actin-binding activity of L- RT plastin and promotes its targeting to sites of actin assembly in cells."; RL J. Cell Sci. 119:1947-1960(2006). RN [16] RP SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF SER-5, PHOSPHORYLATION AT RP SER-5, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17294403; DOI=10.1002/eji.200636320; RA Wabnitz G.H., Koecher T., Lohneis P., Stober C., Konstandin M.H., Funk B., RA Sester U., Wilm M., Klemke M., Samstag Y.; RT "Costimulation induced phosphorylation of L-plastin facilitates surface RT transport of the T cell activation molecules CD69 and CD25."; RL Eur. J. Immunol. 37:649-662(2007). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-28; SER-30; SER-257 RP AND SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-88; LYS-294; LYS-297; RP LYS-361; LYS-472; LYS-542 AND LYS-579, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-257; SER-290; THR-291; RP THR-353; SER-406 AND SER-474, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, 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 [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [25] RP STRUCTURE BY NMR OF 513-627. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fourth CH domain from human L-plastin."; RL Submitted (JUN-2006) to the PDB data bank. RN [26] RP VARIANT SER-608, CHARACTERIZATION OF VARIANT SER-608, FUNCTION, AND RP INTERACTION WITH ACTIN. RX PubMed=28493397; DOI=10.1002/humu.23246; RG UK10K; RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D., RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M., RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G., RA FitzPatrick D.R.; RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma."; RL Hum. Mutat. 38:942-946(2017). CC -!- FUNCTION: Actin-binding protein (PubMed:16636079, PubMed:17294403, CC PubMed:28493397). Plays a role in the activation of T-cells in response CC to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). CC Modulates the cell surface expression of IL2RA/CD25 and CD69 CC (PubMed:17294403). {ECO:0000269|PubMed:16636079, CC ECO:0000269|PubMed:17294403, ECO:0000269|PubMed:28493397}. CC -!- SUBUNIT: Monomer. Interacts with AIF1 (By similarity). Interacts with CC actin (PubMed:28493397). {ECO:0000250|UniProtKB:Q61233, CC ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:28493397}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:16636079}. Cell junction CC {ECO:0000269|PubMed:17294403}. Cell projection CC {ECO:0000269|PubMed:16636079}. Cell projection, ruffle membrane CC {ECO:0000250|UniProtKB:Q61233, ECO:0000269|PubMed:16636079}; Peripheral CC membrane protein {ECO:0000250|UniProtKB:Q61233}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q61233}. Note=Relocalizes to the immunological CC synapse between peripheral blood T-lymphocytes and antibody-presenting CC cells in response to costimulation through TCR/CD3 and CD2 or CD28 CC (PubMed:17294403). Associated with the actin cytoskeleton at membrane CC ruffles. Relocalizes to actin-rich cell projections upon serine CC phosphorylation (PubMed:16636079). {ECO:0000250|UniProtKB:Q61233, CC ECO:0000269|PubMed:16636079, ECO:0000269|PubMed:17294403}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P13796-1; Sequence=Displayed; CC Name=2; CC IsoId=P13796-2; Sequence=VSP_056450, VSP_056451; CC -!- TISSUE SPECIFICITY: Detected in intestinal microvilli, hair cell CC stereocilia, and fibroblast filopodia, in spleen and other lymph node- CC containing organs. Expressed in peripheral blood T-lymphocytes, CC neutrophils, monocytes, B-lymphocytes, and myeloid cells. CC {ECO:0000269|PubMed:3261603}. CC -!- PTM: Phosphorylated on a serine residue in response to costimulation CC through TCR/CD3 and CD2 or CD28. Serine phosphorylation promotes CC association with the actin cytoskeleton and targeting to peripheral CC cell projections. {ECO:0000269|PubMed:16636079, CC ECO:0000269|PubMed:17294403}. CC -!- DISEASE: Note=Chromosomal aberrations involving LCP1 is a cause of B- CC cell non-Hodgkin lymphomas (B-cell NHL). Translocation CC t(3;13)(q27;q14), with BCL6. {ECO:0000269|PubMed:10469447}. CC -!- DISEASE: Note=Defects in LCP1 has been found in a patient with isolated CC coloboma, a defect of the eye characterized by the absence of ocular CC structures due to abnormal morphogenesis of the optic cup and stalk, CC and the fusion of the fetal fissure (optic fissure). Isolated colobomas CC may be associated with an abnormally small eye (microphthalmia) or CC small cornea. {ECO:0000269|PubMed:28493397}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/95/LCP1"; 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; J02923; AAA63236.1; -; mRNA. DR EMBL; AK300556; BAG62262.1; -; mRNA. DR EMBL; AK312393; BAG35310.1; -; mRNA. DR EMBL; AL137141; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08757.1; -; Genomic_DNA. DR EMBL; BC007673; AAH07673.1; -; mRNA. DR EMBL; BC010271; AAH10271.1; -; mRNA. DR EMBL; M22300; AAB02845.1; -; mRNA. DR EMBL; AH002870; AAA59529.1; -; Genomic_DNA. DR EMBL; M34426; AAA36184.1; -; mRNA. DR CCDS; CCDS9403.1; -. [P13796-1] DR PIR; A35836; A35836. DR RefSeq; NP_002289.2; NM_002298.4. [P13796-1] DR RefSeq; XP_005266431.1; XM_005266374.1. [P13796-1] DR PDB; 2D85; NMR; -; A=517-627. DR PDB; 5JOJ; NMR; -; A=1-97. DR PDB; 5JOL; NMR; -; A=1-82. DR PDB; 6VEC; EM; 3.90 A; a/b/c/d/e/f/g/h/i/j/k=238-627. DR PDBsum; 2D85; -. DR PDBsum; 5JOJ; -. DR PDBsum; 5JOL; -. DR PDBsum; 6VEC; -. DR AlphaFoldDB; P13796; -. DR EMDB; EMD-21155; -. DR SMR; P13796; -. DR BioGRID; 110128; 105. DR DIP; DIP-34767N; -. DR ELM; P13796; -. DR IntAct; P13796; 23. DR MINT; P13796; -. DR STRING; 9606.ENSP00000381581; -. DR ChEMBL; CHEMBL4295718; -. DR GlyCosmos; P13796; 5 sites, 1 glycan. DR GlyGen; P13796; 8 sites, 1 O-linked glycan (8 sites). DR iPTMnet; P13796; -. DR MetOSite; P13796; -. DR PhosphoSitePlus; P13796; -. DR SwissPalm; P13796; -. DR BioMuta; LCP1; -. DR DMDM; 308153685; -. DR CPTAC; CPTAC-88; -. DR CPTAC; CPTAC-89; -. DR EPD; P13796; -. DR jPOST; P13796; -. DR MassIVE; P13796; -. DR MaxQB; P13796; -. DR PaxDb; 9606-ENSP00000381581; -. DR PeptideAtlas; P13796; -. DR PRIDE; P13796; -. DR ProteomicsDB; 5167; -. DR ProteomicsDB; 52986; -. [P13796-1] DR Pumba; P13796; -. DR Antibodypedia; 9112; 460 antibodies from 34 providers. DR DNASU; 3936; -. DR Ensembl; ENST00000323076.7; ENSP00000315757.2; ENSG00000136167.15. [P13796-1] DR Ensembl; ENST00000398576.6; ENSP00000381581.1; ENSG00000136167.15. [P13796-1] DR Ensembl; ENST00000674665.1; ENSP00000501964.1; ENSG00000136167.15. [P13796-2] DR GeneID; 3936; -. DR KEGG; hsa:3936; -. DR MANE-Select; ENST00000323076.7; ENSP00000315757.2; NM_002298.5; NP_002289.2. DR UCSC; uc001vba.5; human. [P13796-1] DR AGR; HGNC:6528; -. DR CTD; 3936; -. DR DisGeNET; 3936; -. DR GeneCards; LCP1; -. DR HGNC; HGNC:6528; LCP1. DR HPA; ENSG00000136167; Tissue enhanced (bone marrow, epididymis, lymphoid tissue). DR MalaCards; LCP1; -. DR MIM; 153430; gene. DR neXtProt; NX_P13796; -. DR OpenTargets; ENSG00000136167; -. DR PharmGKB; PA30312; -. DR VEuPathDB; HostDB:ENSG00000136167; -. DR eggNOG; KOG0046; Eukaryota. DR GeneTree; ENSGT00950000183097; -. DR HOGENOM; CLU_015284_2_0_1; -. DR InParanoid; P13796; -. DR OMA; WQLMRKN; -. DR OrthoDB; 5475188at2759; -. DR PhylomeDB; P13796; -. DR TreeFam; TF300680; -. DR PathwayCommons; P13796; -. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; P13796; -. DR SIGNOR; P13796; -. DR BioGRID-ORCS; 3936; 15 hits in 1154 CRISPR screens. DR ChiTaRS; LCP1; human. DR EvolutionaryTrace; P13796; -. DR GeneWiki; LCP1; -. DR GenomeRNAi; 3936; -. DR Pharos; P13796; Tbio. DR PRO; PR:P13796; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P13796; Protein. DR Bgee; ENSG00000136167; Expressed in monocyte and 150 other cell types or tissues. DR ExpressionAtlas; P13796; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005884; C:actin filament; IMP:UniProtKB. DR GO; GO:0032432; C:actin filament bundle; IMP:UniProtKB. DR GO; GO:0030054; C:cell junction; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0030175; C:filopodium; IMP:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB. DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ARUK-UCL. DR GO; GO:0001891; C:phagocytic cup; ISS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0002102; C:podosome; IDA:UniProtKB. DR GO; GO:0001726; C:ruffle; IMP:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; NAS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB. DR GO; GO:0005178; F:integrin binding; IPI:ARUK-UCL. DR GO; GO:0051764; P:actin crosslink formation; ISS:FlyBase. DR GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB. DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0016477; P:cell migration; IMP:UniProtKB. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:FlyBase. DR GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB. DR GO; GO:0071803; P:positive regulation of podosome assembly; IMP:UniProtKB. DR GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB. DR GO; GO:0033157; P:regulation of intracellular protein transport; IDA:UniProtKB. DR GO; GO:0002286; P:T cell activation involved in immune response; IDA:UniProtKB. DR CDD; cd21327; CH_PLS2_rpt2; 1. DR CDD; cd21333; CH_PLS2_rpt4; 1. DR CDD; cd21292; CH_PLS_rpt1; 1. DR CDD; cd00051; EFh; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 4. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. 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 PANTHER; PTHR19961; FIMBRIN/PLASTIN; 1. DR PANTHER; PTHR19961:SF35; PLASTIN-2; 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; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 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. DR Genevisible; P13796; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; KW Cell junction; Cell membrane; Cell projection; Chromosomal rearrangement; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..627 FT /note="Plastin-2" FT /id="PRO_0000073743" FT DOMAIN 9..44 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 49..84 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 120..236 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 264..375 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 394..503 FT /note="Calponin-homology (CH) 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 515..624 FT /note="Calponin-homology (CH) 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REGION 106..379 FT /note="Actin-binding 1" FT REGION 380..624 FT /note="Actin-binding 2" FT BINDING 22 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 24 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 26 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 62 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 64 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 66 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 68 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 73 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16636079, FT ECO:0000269|PubMed:17294403, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 28 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 76 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 88 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 124 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 291 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 294 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 297 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 323 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 472 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 474 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 542 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 579 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..25 FT /note="MARGSVSDEEMMELREAFAKVDTDG -> MCAEDGDSKFSMSISMNSPFLEI FT LH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056450" FT VAR_SEQ 26..456 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056451" FT VARIANT 24 FT /note="D -> E" FT /id="VAR_001371" FT VARIANT 533 FT /note="K -> E (in dbSNP:rs4941543)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2111166, FT ECO:0000269|PubMed:2252891, ECO:0000269|PubMed:3211125" FT /id="VAR_024398" FT VARIANT 544 FT /note="P -> A (in dbSNP:rs17067725)" FT /id="VAR_030826" FT VARIANT 608 FT /note="N -> S (found in a patient with isolated coloboma; FT increases interaction with actin)" FT /evidence="ECO:0000269|PubMed:28493397" FT /id="VAR_079850" FT MUTAGEN 5 FT /note="S->A: Abolishes phosphorylation and reduces the cell FT surface expression of CD69 and IL2RA. Reduces association FT with the actin cytoskeleton." FT /evidence="ECO:0000269|PubMed:16636079, FT ECO:0000269|PubMed:17294403" FT MUTAGEN 5 FT /note="S->E: Promotes association with the actin FT cytoskeleton." FT /evidence="ECO:0000269|PubMed:16636079, FT ECO:0000269|PubMed:17294403" FT CONFLICT 611 FT /note="M -> T (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 8..21 FT /evidence="ECO:0007829|PDB:5JOJ" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:5JOJ" FT HELIX 31..40 FT /evidence="ECO:0007829|PDB:5JOJ" FT HELIX 47..59 FT /evidence="ECO:0007829|PDB:5JOJ" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:5JOL" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:5JOL" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:5JOJ" FT HELIX 85..94 FT /evidence="ECO:0007829|PDB:5JOJ" FT HELIX 520..532 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 545..548 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 550..559 FT /evidence="ECO:0007829|PDB:2D85" FT TURN 566..568 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 576..593 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 601..604 FT /evidence="ECO:0007829|PDB:2D85" FT TURN 605..607 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 609..612 FT /evidence="ECO:0007829|PDB:2D85" FT HELIX 615..620 FT /evidence="ECO:0007829|PDB:2D85" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:2D85" SQ SEQUENCE 627 AA; 70288 MW; 668E4AA6A3FC7B58 CRC64; MARGSVSDEE MMELREAFAK VDTDGNGYIS FNELNDLFKA ACLPLPGYRV REITENLMAT GDLDQDGRIS FDEFIKIFHG LKSTDVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT NDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCNKIGNFS TDIKDSKAYY HLLEQVAPKG DEEGVPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP KLNLAFIANL FNRYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVELGKNQ AKFSLVGIGG QDLNEGNRTL TLALIWQLMR RYTLNILEEI GGGQKVNDDI IVNWVNETLR EAKKSSSISS FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLNDDEKL NNAKYAISMA RKIGARVYAL PEDLVEVNPK MVMTVFACLM GKGMKRV //