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Protein

Plastin-2

Gene

Lcp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi22 – 33121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi62 – 73122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. actin filament binding Source: MGI
  2. calcium ion binding Source: InterPro
  3. identical protein binding Source: MGI

GO - Biological processi

  1. actin filament bundle assembly Source: MGI
  2. cell migration Source: MGI
  3. organ regeneration Source: Ensembl
  4. protein kinase A signaling Source: MGI
  5. regulation of intracellular protein transport Source: UniProtKB
  6. response to wounding Source: MGI
  7. T cell activation involved in immune response Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Plastin-2
Alternative name(s):
65 kDa macrophage protein
L-plastin
Lymphocyte cytosolic protein 1
Short name:
LCP-1
pp65
Gene namesi
Name:Lcp1
Synonyms:Pls2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:104808. Lcp1.

Subcellular locationi

  1. Cytoplasmcytoskeleton 1 Publication
  2. Cell projection By similarity
  3. Cell junction By similarity
  4. Cell projectionruffle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

  5. 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.By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. actin filament Source: MGI
  3. actin filament bundle Source: MGI
  4. cytoplasm Source: MGI
  5. cytosol Source: UniProtKB
  6. extracellular space Source: MGI
  7. extracellular vesicular exosome Source: MGI
  8. filopodium Source: MGI
  9. focal adhesion Source: MGI
  10. phagocytic cup Source: MGI
  11. plasma membrane Source: MGI
  12. ruffle Source: MGI
  13. ruffle membrane Source: UniProtKB-SubCell
  14. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 627626Plastin-2PRO_0000073744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51Phosphoserine2 Publications
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei28 – 281PhosphotyrosineBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei76 – 761N6-acetyllysineBy similarity
Modified residuei88 – 881N6-acetyllysineBy similarity
Modified residuei124 – 1241PhosphotyrosineBy similarity
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei294 – 2941N6-acetyllysineBy similarity
Modified residuei297 – 2971N6-acetyllysineBy similarity
Modified residuei323 – 3231PhosphoserineBy similarity
Modified residuei361 – 3611N6-acetyllysineBy similarity
Modified residuei406 – 4061PhosphoserineBy similarity
Modified residuei472 – 4721N6-acetyllysineBy similarity
Modified residuei542 – 5421N6-acetyllysineBy similarity
Modified residuei579 – 5791N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61233.
PaxDbiQ61233.
PRIDEiQ61233.

2D gel databases

COMPLUYEAST-2DPAGEQ61233.
REPRODUCTION-2DPAGEQ61233.

PTM databases

PhosphoSiteiQ61233.

Expressioni

Gene expression databases

BgeeiQ61233.
CleanExiMM_LCP1.
ExpressionAtlasiQ61233. baseline and differential.
GenevestigatoriQ61233.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with AIF1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk14P478115EBI-309345,EBI-298727

Protein-protein interaction databases

BioGridi202256. 4 interactions.
IntActiQ61233. 7 interactions.
MINTiMINT-217293.

Structurei

3D structure databases

ProteinModelPortaliQ61233.
SMRiQ61233. Positions 7-80, 118-627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 4436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini49 – 8436EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini106 – 379274Actin-binding 1Add
BLAST
Domaini120 – 236117CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini264 – 375112CH 2PROSITE-ProRule annotationAdd
BLAST
Domaini380 – 624245Actin-binding 2Add
BLAST
Domaini394 – 503110CH 3PROSITE-ProRule annotationAdd
BLAST
Domaini515 – 624110CH 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 actin-binding domains.Curated
Contains 4 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00390000005691.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiQ61233.
KOiK17276.
OMAiQPGSIKY.
OrthoDBiEOG7K9K2D.
PhylomeDBiQ61233.
TreeFamiTF300680.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGSVSDEE MMELREAFAK VDTDGNGYIS CNELNDLFKA ACLPLPGYRV
60 70 80 90 100
REITENLMAT GDLDQDGKIS FDEFIKVFHG LKSTEVAKTF RKAINKKEGI
110 120 130 140 150
CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT
160 170 180 190 200
DDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS
210 220 230 240 250
ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA
260 270 280 290 300
LLREGESLED LMKLSPEELL LRWANYHLEN AGCTKITNFS TDIKDSKAYY
310 320 330 340 350
HLLEQVAPKG DEEGIPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV
360 370 380 390 400
TATDVVRGNP KLNLAFIANL FNKYPALHKP ENQDIDWGAL EGETREERTF
410 420 430 440 450
RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL
460 470 480 490 500
GGNMKKLENC NYAVDLGKNQ AKFSLVGIAG QDLNEGNRTL TLALVWQLMR
510 520 530 540 550
RYTLNILEDI GGGQKVNDDI IVNWVNTTLK EAQKSSSIAS FKDPKISTSL
560 570 580 590 600
PVLDLIDAIQ PGSINYDLLK TENLDDEEKL NNAKYAISMA RKIGARVYAL
610 620
PEDLVEVNPK MVMTVFACLM GKGMKRV
Length:627
Mass (Da):70,149
Last modified:January 23, 2007 - v4
Checksum:iF0A1E6CA1C11A8E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261N → K in BAC27208 (PubMed:16141072).Curated
Sequence conflicti83 – 831S → T in BAA07085 (PubMed:7897227).Curated
Sequence conflicti292 – 2921D → H in BAA07085 (PubMed:7897227).Curated
Sequence conflicti367 – 3693IAN → ANL in BAA07085 (PubMed:7897227).Curated
Sequence conflicti479 – 4791A → G in BAA07085 (PubMed:7897227).Curated
Sequence conflicti527 – 5271T → M in BAA07085 (PubMed:7897227).Curated
Sequence conflicti558 – 5581A → S in BAB26141 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27276.1.
PIRiI49445.
RefSeqiNP_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_006518701.2.
XP_006518765.1. XM_006518702.2.
XP_006518766.1. XM_006518703.2.
XP_006518767.1. XM_006518704.1.
UniGeneiMm.153911.
Mm.484415.

Genome annotation databases

EnsembliENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998.
ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998.
ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
GeneIDi18826.
KEGGimmu:18826.
UCSCiuc007uqm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27276.1.
PIRiI49445.
RefSeqiNP_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_006518701.2.
XP_006518765.1. XM_006518702.2.
XP_006518766.1. XM_006518703.2.
XP_006518767.1. XM_006518704.1.
UniGeneiMm.153911.
Mm.484415.

3D structure databases

ProteinModelPortaliQ61233.
SMRiQ61233. Positions 7-80, 118-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202256. 4 interactions.
IntActiQ61233. 7 interactions.
MINTiMINT-217293.

PTM databases

PhosphoSiteiQ61233.

2D gel databases

COMPLUYEAST-2DPAGEQ61233.
REPRODUCTION-2DPAGEQ61233.

Proteomic databases

MaxQBiQ61233.
PaxDbiQ61233.
PRIDEiQ61233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000124499; ENSMUSP00000121201; ENSMUSG00000021998.
ENSMUST00000131802; ENSMUSP00000117137; ENSMUSG00000021998.
ENSMUST00000145303; ENSMUSP00000116271; ENSMUSG00000021998.
GeneIDi18826.
KEGGimmu:18826.
UCSCiuc007uqm.2. mouse.

Organism-specific databases

CTDi3936.
MGIiMGI:104808. Lcp1.

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00390000005691.
HOGENOMiHOG000213447.
HOVERGENiHBG003082.
InParanoidiQ61233.
KOiK17276.
OMAiQPGSIKY.
OrthoDBiEOG7K9K2D.
PhylomeDBiQ61233.
TreeFamiTF300680.

Miscellaneous databases

NextBioi295196.
PROiQ61233.
SOURCEiSearch...

Gene expression databases

BgeeiQ61233.
CleanExiMM_LCP1.
ExpressionAtlasiQ61233. baseline and differential.
GenevestigatoriQ61233.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, 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].

Entry informationi

Entry nameiPLSL_MOUSE
AccessioniPrimary (citable) accession number: Q61233
Secondary accession number(s): Q3UE24, Q8R1X3, Q9CV77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.