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Plastin-2 (65 kDa macrophage protein) (L-plastin) (Lymphocyte cytosolic protein 1) (LCP-1) (pp65)

 PLSL_MOUSE              Reviewed;         627 AA.
Q61233; Q3UE24; Q8R1X3; Q9CV77;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 177.
RecName: Full=Plastin-2;
AltName: Full=65 kDa macrophage protein;
AltName: Full=L-plastin;
AltName: Full=Lymphocyte cytosolic protein 1;
Short=LCP-1;
AltName: Full=pp65;
Name=Lcp1; Synonyms=Pls2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
PHOSPHORYLATION AT SER-5 AND SER-7.
PubMed=7897227;
Shinomiya H., Hagi A., Fukuzumi M., Mizobuchi M., Hirata H.,
Utsumi S.;
"Complete primary structure and phosphorylation site of the 65-kDa
macrophage protein phosphorylated by stimulation with bacterial
lipopolysaccharide.";
J. Immunol. 154:3471-3478(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Thymus, and Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 234-244; 264-272 AND 344-357, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION.
PubMed=8060349; DOI=10.1006/bbrc.1994.2120;
Shinomiya H., Hirata H., Saito S., Yagisawa H., Nakano M.;
"Identification of the 65-kDa phosphoprotein in murine macrophages as
a novel protein: homology with human L-plastin.";
Biochem. Biophys. Res. Commun. 202:1631-1638(1994).
[6]
SUBCELLULAR LOCATION, AND INTERACTION WITH AIF1.
PubMed=14756805;
Ohsawa K., Imai Y., Sasaki Y., Kohsaka S.;
"Microglia/macrophage-specific protein Iba1 binds to fimbrin and
enhances its actin-bundling activity.";
J. Neurochem. 88:844-856(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-30 AND SER-257,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Actin-binding protein. Plays a role in the activation of
T-cells in response to costimulation through TCR/CD3 and CD2 or
CD28. Modulates the cell surface expression of IL2RA/CD25 and
CD69. {ECO:0000250|UniProtKB:P13796}.
-!- SUBUNIT: Monomer (By similarity). Interacts with AIF1
(PubMed:14756805). Interacts with actin (By similarity).
{ECO:0000250|UniProtKB:P13796, ECO:0000269|PubMed:14756805}.
-!- INTERACTION:
P47811:Mapk14; NbExp=5; IntAct=EBI-309345, EBI-298727;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:14756805}. Cell projection {ECO:0000250}. Cell
junction {ECO:0000250}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:14756805}; Peripheral membrane protein
{ECO:0000269|PubMed:14756805}; Cytoplasmic side
{ECO:0000269|PubMed:14756805}. Note=Relocalizes to the
immunological synapse between peripheral blood T-lymphocytes and
antibody-presenting cells in response to costimulation through
TCR/CD3 and CD2 or CD28. Relocalizes to actin-rich cell
projections upon serine phosphorylation (By similarity).
Associated with the actin cytoskeleton at membrane ruffles.
{ECO:0000250|UniProtKB:P13796}.
-!- PTM: Phosphorylated on a serine residue in response to
costimulation through TCR/CD3 and CD2 or CD28. Serine
phosphorylation promotes association with the actin cytoskeleton
and targeting to peripheral cell projections (By similarity).
{ECO:0000250}.
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EMBL; D37837; BAA07085.1; -; mRNA.
EMBL; AK009211; BAB26141.1; -; mRNA.
EMBL; AK030806; BAE20456.1; -; mRNA.
EMBL; AK030987; BAC27205.1; -; mRNA.
EMBL; AK030996; BAC27208.1; -; mRNA.
EMBL; AK088202; BAC40207.1; -; mRNA.
EMBL; AK149790; BAE29087.1; -; mRNA.
EMBL; AK151155; BAE30161.1; -; mRNA.
EMBL; AK152891; BAE31574.1; -; mRNA.
EMBL; AK153082; BAE31707.1; -; mRNA.
EMBL; AK153206; BAE31806.1; -; mRNA.
EMBL; AK169728; BAE41332.1; -; mRNA.
EMBL; AK169833; BAE41398.1; -; mRNA.
EMBL; BC022943; AAH22943.1; -; mRNA.
CCDS; CCDS27276.1; -.
PIR; I49445; I49445.
RefSeq; NP_001234913.1; NM_001247984.1.
RefSeq; NP_032905.2; NM_008879.4.
RefSeq; XP_006518762.1; XM_006518699.1.
RefSeq; XP_006518764.1; XM_006518701.3.
RefSeq; XP_006518765.1; XM_006518702.3.
RefSeq; XP_006518766.1; XM_006518703.3.
RefSeq; XP_006518767.1; XM_006518704.1.
RefSeq; XP_017171409.1; XM_017315920.1.
UniGene; Mm.153911; -.
UniGene; Mm.484415; -.
ProteinModelPortal; Q61233; -.
SMR; Q61233; -.
BioGrid; 202256; 5.
IntAct; Q61233; 7.
MINT; Q61233; -.
STRING; 10090.ENSMUSP00000116271; -.
CarbonylDB; Q61233; -.
iPTMnet; Q61233; -.
PhosphoSitePlus; Q61233; -.
SwissPalm; Q61233; -.
COMPLUYEAST-2DPAGE; Q61233; -.
REPRODUCTION-2DPAGE; Q61233; -.
EPD; Q61233; -.
MaxQB; Q61233; -.
PaxDb; Q61233; -.
PeptideAtlas; Q61233; -.
PRIDE; Q61233; -.
Ensembl; ENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998.
Ensembl; ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998.
Ensembl; ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
GeneID; 18826; -.
KEGG; mmu:18826; -.
UCSC; uc007uqm.2; mouse.
CTD; 3936; -.
MGI; MGI:104808; Lcp1.
eggNOG; KOG0046; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00390000005691; -.
HOGENOM; HOG000213447; -.
HOVERGEN; HBG003082; -.
InParanoid; Q61233; -.
KO; K17276; -.
OMA; MFDECKD; -.
OrthoDB; EOG091G03YP; -.
PhylomeDB; Q61233; -.
TreeFam; TF300680; -.
PRO; PR:Q61233; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000021998; Expressed in 269 organ(s), highest expression level in peripheral lymph node.
CleanEx; MM_LCP1; -.
ExpressionAtlas; Q61233; baseline and differential.
Genevisible; Q61233; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0032432; C:actin filament bundle; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001891; C:phagocytic cup; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0002102; C:podosome; ISO:MGI.
GO; GO:0001726; C:ruffle; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
GO; GO:0071803; P:positive regulation of podosome assembly; ISO:MGI.
GO; GO:0010737; P:protein kinase A signaling; ISO:MGI.
GO; GO:0033157; P:regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISO:MGI.
GO; GO:0002286; P:T cell activation involved in immune response; ISS:UniProtKB.
CDD; cd00014; CH; 2.
CDD; cd00051; EFh; 1.
Gene3D; 1.10.418.10; -; 4.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF00307; CH; 4.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00033; CH; 4.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF47576; SSF47576; 1.
PROSITE; PS00019; ACTININ_1; 2.
PROSITE; PS00020; ACTININ_2; 2.
PROSITE; PS50021; CH; 4.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
Acetylation; Actin-binding; Calcium; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P13796}.
CHAIN 2 627 Plastin-2.
/FTId=PRO_0000073744.
DOMAIN 9 44 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 49 84 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 120 236 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 264 375 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 394 503 Calponin-homology (CH) 3.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 515 624 Calponin-homology (CH) 4.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
CA_BIND 22 33 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 62 73 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 106 379 Actin-binding 1.
REGION 380 624 Actin-binding 2.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:7897227}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000269|PubMed:7897227}.
MOD_RES 28 28 Phosphotyrosine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 124 124 Phosphotyrosine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 291 291 Phosphothreonine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 294 294 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 297 297 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 361 361 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 472 472 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
MOD_RES 579 579 N6-acetyllysine.
{ECO:0000250|UniProtKB:P13796}.
CONFLICT 26 26 N -> K (in Ref. 2; BAC27208).
{ECO:0000305}.
CONFLICT 83 83 S -> T (in Ref. 1; BAA07085).
{ECO:0000305}.
CONFLICT 292 292 D -> H (in Ref. 1; BAA07085).
{ECO:0000305}.
CONFLICT 367 369 IAN -> ANL (in Ref. 1; BAA07085).
{ECO:0000305}.
CONFLICT 479 479 A -> G (in Ref. 1; BAA07085).
{ECO:0000305}.
CONFLICT 527 527 T -> M (in Ref. 1; BAA07085).
{ECO:0000305}.
CONFLICT 558 558 A -> S (in Ref. 2; BAB26141).
{ECO:0000305}.
SEQUENCE 627 AA; 70149 MW; F0A1E6CA1C11A8E6 CRC64;
MARGSVSDEE MMELREAFAK VDTDGNGYIS CNELNDLFKA ACLPLPGYRV REITENLMAT
GDLDQDGKIS FDEFIKVFHG LKSTEVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE
EEKYAFVNWI NKALENDPDC RHVIPMNPNT DDLFNAVGDG IVLCKMINLS VPDTIDERTI
NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI
ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCTKITNFS TDIKDSKAYY
HLLEQVAPKG DEEGIPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP
KLNLAFIANL FNKYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL
SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVDLGKNQ AKFSLVGIAG
QDLNEGNRTL TLALVWQLMR RYTLNILEDI GGGQKVNDDI IVNWVNTTLK EAQKSSSIAS
FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLDDEEKL NNAKYAISMA RKIGARVYAL
PEDLVEVNPK MVMTVFACLM GKGMKRV


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