Q61233 (PLSL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plastin-2

Alternative name(s):
65 kDa macrophage protein
L-plastin
Lymphocyte cytosolic protein 1
Short name=LCP-1
pp65

Gene names

Name:	Lcp1
Synonyms:	Pls2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity.
Subunit structure	Monomer By similarity. Interacts with AIF1. Ref.6
Subcellular location	Cytoplasm › cytoskeleton. Cell projection By similarity. Cell junction By similarity. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. 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. Ref.6
Post-translational modification	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. Ref.1 Ref.5
Sequence similarities	Contains 2 actin-binding domains. Contains 4 CH (calponin-homology) domains. Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Domain	Repeat
Ligand	Actin-binding Calcium Metal-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation involved in immune response Inferred from sequence or structural similarity. Source: UniProtKB actin filament bundle assembly Inferred from direct assay Ref.6. Source: MGI organ regeneration Inferred from electronic annotation. Source: Compara regulation of intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin filament Inferred from direct assay Ref.6. Source: MGI cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB phagocytic cup Inferred from direct assay Ref.6. Source: MGI ruffle Inferred from direct assay Ref.6. Source: MGI ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin filament binding Inferred from direct assay Ref.6. Source: MGI calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Mapk14	P47811	5	EBI-309345,EBI-298727

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 627	626	Plastin-2		PRO_0000073744
Regions
	Domain	9 – 44	36	EF-hand 1
	Domain	49 – 84	36	EF-hand 2
	Domain	106 – 379	274	Actin-binding 1
	Domain	120 – 236	117	CH 1
	Domain	264 – 375	112	CH 2
	Domain	380 – 624	245	Actin-binding 2
	Domain	394 – 503	110	CH 3
	Domain	515 – 624	110	CH 4
	Calcium binding	22 – 33	12	1 By similarity
	Calcium binding	62 – 73	12	2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	5	1	Phosphoserine Ref.1 Ref.8
	Modified residue	7	1	Phosphoserine Ref.1 Ref.7
	Modified residue	28	1	Phosphotyrosine By similarity
	Modified residue	30	1	Phosphoserine By similarity
	Modified residue	76	1	N6-acetyllysine By similarity
	Modified residue	88	1	N6-acetyllysine By similarity
	Modified residue	124	1	Phosphotyrosine By similarity
	Modified residue	257	1	Phosphoserine By similarity
	Modified residue	294	1	N6-acetyllysine By similarity
	Modified residue	297	1	N6-acetyllysine By similarity
	Modified residue	323	1	Phosphoserine By similarity
	Modified residue	361	1	N6-acetyllysine By similarity
	Modified residue	472	1	N6-acetyllysine By similarity
	Modified residue	542	1	N6-acetyllysine By similarity
	Modified residue	579	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	26	1	N → K in BAC27208. Ref.2
	Sequence conflict	83	1	S → T in BAA07085. Ref.1
	Sequence conflict	292	1	D → H in BAA07085. Ref.1
	Sequence conflict	367 – 369	3	IAN → ANL in BAA07085. Ref.1
	Sequence conflict	479	1	A → G in BAA07085. Ref.1
	Sequence conflict	527	1	T → M in BAA07085. Ref.1
	Sequence conflict	558	1	A → S in BAB26141. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q61233 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: F0A1E6CA1C11A8E6	FASTA	627	70,149
	10 20 30 40 50 60 MARGSVSDEE MMELREAFAK VDTDGNGYIS CNELNDLFKA ACLPLPGYRV REITENLMAT 70 80 90 100 110 120 GDLDQDGKIS FDEFIKVFHG LKSTEVAKTF RKAINKKEGI CAIGGTSEQS SVGTQHSYSE 130 140 150 160 170 180 EEKYAFVNWI NKALENDPDC RHVIPMNPNT DDLFNAVGDG IVLCKMINLS VPDTIDERTI 190 200 210 220 230 240 NKKKLTPFTI QENLNLALNS ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI 250 260 270 280 290 300 ELSRNEALIA LLREGESLED LMKLSPEELL LRWANYHLEN AGCTKITNFS TDIKDSKAYY 310 320 330 340 350 360 HLLEQVAPKG DEEGIPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV TATDVVRGNP 370 380 390 400 410 420 KLNLAFIANL FNKYPALHKP ENQDIDWGAL EGETREERTF RNWMNSLGVN PRVNHLYSDL 430 440 450 460 470 480 SDALVIFQLY EKIKVPVDWN RVNKPPYPKL GGNMKKLENC NYAVDLGKNQ AKFSLVGIAG 490 500 510 520 530 540 QDLNEGNRTL TLALVWQLMR RYTLNILEDI GGGQKVNDDI IVNWVNTTLK EAQKSSSIAS 550 560 570 580 590 600 FKDPKISTSL PVLDLIDAIQ PGSINYDLLK TENLDDEEKL NNAKYAISMA RKIGARVYAL 610 620 PEDLVEVNPK MVMTVFACLM GKGMKRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide." Shinomiya H., Hagi A., Fukuzumi M., Mizobuchi M., Hirata H., Utsumi S. J. Immunol. 154:3471-3478(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-5 AND SER-7.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Thymus and Tongue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 234-244; 264-272 AND 344-357, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[5]	"Identification of the 65-kDa phosphoprotein in murine macrophages as a novel protein: homology with human L-plastin." Shinomiya H., Hirata H., Saito S., Yagisawa H., Nakano M. Biochem. Biophys. Res. Commun. 202:1631-1638(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION.
[6]	"Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances its actin-bundling activity." Ohsawa K., Imai Y., Sasaki Y., Kohsaka S. J. Neurochem. 88:844-856(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AIF1.
[7]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D37837 mRNA. Translation: BAA07085.1. AK009211 mRNA. Translation: BAB26141.1. AK030806 mRNA. Translation: BAE20456.1. AK030987 mRNA. Translation: BAC27205.1. AK030996 mRNA. Translation: BAC27208.1. AK088202 mRNA. Translation: BAC40207.1. AK149790 mRNA. Translation: BAE29087.1. AK151155 mRNA. Translation: BAE30161.1. AK152891 mRNA. Translation: BAE31574.1. AK153082 mRNA. Translation: BAE31707.1. AK153206 mRNA. Translation: BAE31806.1. AK169728 mRNA. Translation: BAE41332.1. AK169833 mRNA. Translation: BAE41398.1. BC022943 mRNA. Translation: AAH22943.1.
IPI	IPI00118892.
PIR	I49445.
RefSeq	NP_001234913.1. NM_001247984.1. NP_032905.2. NM_008879.4.
UniGene	Mm.153911. Mm.484415.
3D structure databases
ProteinModelPortal	Q61233.
SMR	Q61233. Positions 7-77, 118-627.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61233. 4 interactions.
MINT	MINT-217293.
PTM databases
PhosphoSite	Q61233.
2D gel databases
COMPLUYEAST-2DPAGE	Q61233.
REPRODUCTION-2DPAGE	Q61233.
Proteomic databases
PaxDb	Q61233.
PRIDE	Q61233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998. ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998. ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
GeneID	18826.
KEGG	mmu:18826.
UCSC	uc007uqm.2. mouse.
Organism-specific databases
CTD	3936.
MGI	MGI:104808. Lcp1.
Phylogenomic databases
eggNOG	COG5069.
GeneTree	ENSGT00390000005691.
HOGENOM	HOG000213447.
HOVERGEN	HBG003082.
InParanoid	Q61233.
OMA	LNAGNRT.
Gene expression databases
ArrayExpress	Q61233.
Bgee	Q61233.
CleanEx	MM_LCP1.
Genevestigator	Q61233.
GermOnline	ENSMUSG00000021998. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.10.418.10. 4 hits.
InterPro	IPR001589. Actinin_actin-bd_CS. IPR001715. CH-domain. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. [Graphical view]
Pfam	PF00307. CH. 4 hits. PF13499. EF_hand_5. 1 hit. [Graphical view]
SMART	SM00033. CH. 4 hits. SM00054. EFh. 2 hits. [Graphical view]
SUPFAM	SSF47576. Calponin-homology. 1 hit.
PROSITE	PS00019. ACTININ_1. 2 hits. PS00020. ACTININ_2. 2 hits. PS50021. CH. 4 hits. PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	295196.
SOURCE	Search...

Entry information

Entry name

PLSL_MOUSE

Accession

Primary (citable) accession number: Q61233
Secondary accession number(s): Q3UE24, Q8R1X3, Q9CV77

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program