PLSL_HUMAN
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 03-AUG-2022, entry version 234.
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>3.0.co;2-9;
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="http://atlasgeneticsoncology.org/Genes/LCP1ID95.html";
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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 SMR; P13796; -.
DR BioGRID; 110128; 93.
DR DIP; DIP-34767N; -.
DR ELM; P13796; -.
DR IntAct; P13796; 22.
DR MINT; P13796; -.
DR STRING; 9606.ENSP00000381581; -.
DR ChEMBL; CHEMBL4295718; -.
DR GlyGen; P13796; 5 sites, 1 O-linked glycan (5 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; P13796; -.
DR PeptideAtlas; P13796; -.
DR PRIDE; P13796; -.
DR ProteomicsDB; 5167; -.
DR ProteomicsDB; 52986; -. [P13796-1]
DR Antibodypedia; 9112; 417 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 CTD; 3936; -.
DR DisGeNET; 3936; -.
DR GeneCards; LCP1; -.
DR HGNC; HGNC:6528; LCP1.
DR HPA; ENSG00000136167; Tissue enhanced (bone marrow, epididymis, lymphoid tissue).
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; DAEMVRW; -.
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 1076 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 148 other tissues.
DR ExpressionAtlas; P13796; baseline and differential.
DR Genevisible; P13796; HS.
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:UniProtKB.
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; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
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; 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
