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Q61233 (PLSL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length627 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytoskeleton. Cell projection By similarity. Cell junction By similarity. Cell projectionruffle 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 componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT 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: Ensembl

regulation of intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactin filament

Inferred from direct assay Ref.6. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.6. Source: MGI

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_functionactin filament binding

Inferred from direct assay Ref.6. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from physical interaction PubMed 11591653. Source: MGI

protein binding

Inferred from physical interaction PubMed 15102471. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mapk14P478115EBI-309345,EBI-298727

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 627626Plastin-2
PRO_0000073744

Regions

Domain9 – 4436EF-hand 1
Domain49 – 8436EF-hand 2
Domain106 – 379274Actin-binding 1
Domain120 – 236117CH 1
Domain264 – 375112CH 2
Domain380 – 624245Actin-binding 2
Domain394 – 503110CH 3
Domain515 – 624110CH 4
Calcium binding22 – 33121 By similarity
Calcium binding62 – 73122 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue51Phosphoserine Ref.1 Ref.7
Modified residue71Phosphoserine Ref.1
Modified residue281Phosphotyrosine By similarity
Modified residue301Phosphoserine By similarity
Modified residue761N6-acetyllysine By similarity
Modified residue881N6-acetyllysine By similarity
Modified residue1241Phosphotyrosine By similarity
Modified residue2571Phosphoserine By similarity
Modified residue2941N6-acetyllysine By similarity
Modified residue2971N6-acetyllysine By similarity
Modified residue3231Phosphoserine By similarity
Modified residue3611N6-acetyllysine By similarity
Modified residue4721N6-acetyllysine By similarity
Modified residue5421N6-acetyllysine By similarity
Modified residue5791N6-acetyllysine By similarity

Experimental info

Sequence conflict261N → K in BAC27208. Ref.2
Sequence conflict831S → T in BAA07085. Ref.1
Sequence conflict2921D → H in BAA07085. Ref.1
Sequence conflict367 – 3693IAN → ANL in BAA07085. Ref.1
Sequence conflict4791A → G in BAA07085. Ref.1
Sequence conflict5271T → M in BAA07085. Ref.1
Sequence conflict5581A → S in BAB26141. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61233 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F0A1E6CA1C11A8E6

FASTA62770,149
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS27276.1.
PIRI49445.
RefSeqNP_001234913.1. NM_001247984.1.
NP_032905.2. NM_008879.4.
XP_006518762.1. XM_006518699.1.
XP_006518763.1. XM_006518700.1.
XP_006518764.1. XM_006518701.1.
XP_006518765.1. XM_006518702.1.
XP_006518766.1. XM_006518703.1.
XP_006518767.1. XM_006518704.1.
UniGeneMm.153911.
Mm.484415.

3D structure databases

ProteinModelPortalQ61233.
SMRQ61233. Positions 7-77, 118-627.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202256. 3 interactions.
IntActQ61233. 7 interactions.
MINTMINT-217293.

PTM databases

PhosphoSiteQ61233.

2D gel databases

COMPLUYEAST-2DPAGEQ61233.
REPRODUCTION-2DPAGEQ61233.

Proteomic databases

MaxQBQ61233.
PaxDbQ61233.
PRIDEQ61233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998.
ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998.
ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
GeneID18826.
KEGGmmu:18826.
UCSCuc007uqm.2. mouse.

Organism-specific databases

CTD3936.
MGIMGI:104808. Lcp1.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00390000005691.
HOGENOMHOG000213447.
HOVERGENHBG003082.
InParanoidQ61233.
KOK17276.
OMAHLYADID.
OrthoDBEOG7K9K2D.
PhylomeDBQ61233.
TreeFamTF300680.

Gene expression databases

ArrayExpressQ61233.
BgeeQ61233.
CleanExMM_LCP1.
GenevestigatorQ61233.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF00307. CH. 4 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. 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]
ProtoNetSearch...

Other

NextBio295196.
PROQ61233.
SOURCESearch...

Entry information

Entry namePLSL_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot