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Q61233

- PLSL_MOUSE

UniProt

Q61233 - PLSL_MOUSE

Protein

Plastin-2

Gene

Lcp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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
    4. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament bundle assembly Source: MGI
    2. organ regeneration Source: Ensembl
    3. regulation of intracellular protein transport Source: UniProtKB
    4. T cell activation involved in immune response Source: UniProtKB

    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: Chromosome 14

    Organism-specific databases

    MGIiMGI:104808. Lcp1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell projection By similarity. Cell junction By similarity. Cell projectionruffle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
    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 filament Source: MGI
    2. cell junction Source: UniProtKB-SubCell
    3. cytoplasm Source: MGI
    4. cytosol Source: UniProtKB
    5. phagocytic cup Source: MGI
    6. ruffle Source: MGI
    7. ruffle membrane Source: UniProtKB-SubCell

    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 – 51Phosphoserine3 Publications
    Modified residuei7 – 71Phosphoserine2 Publications
    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 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

    ArrayExpressiQ61233.
    BgeeiQ61233.
    CleanExiMM_LCP1.
    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. 3 interactions.
    IntActiQ61233. 7 interactions.
    MINTiMINT-217293.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61233.
    SMRiQ61233. Positions 7-77, 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.
    OMAiHLYADID.
    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

    MARGSVSDEE MMELREAFAK VDTDGNGYIS CNELNDLFKA ACLPLPGYRV    50
    REITENLMAT GDLDQDGKIS FDEFIKVFHG LKSTEVAKTF RKAINKKEGI 100
    CAIGGTSEQS SVGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT 150
    DDLFNAVGDG IVLCKMINLS VPDTIDERTI NKKKLTPFTI QENLNLALNS 200
    ASAIGCHVVN IGAEDLKEGK PYLVLGLLWQ VIKIGLFADI ELSRNEALIA 250
    LLREGESLED LMKLSPEELL LRWANYHLEN AGCTKITNFS TDIKDSKAYY 300
    HLLEQVAPKG DEEGIPAVVI DMSGLREKDD IQRAECMLQQ AERLGCRQFV 350
    TATDVVRGNP KLNLAFIANL FNKYPALHKP ENQDIDWGAL EGETREERTF 400
    RNWMNSLGVN PRVNHLYSDL SDALVIFQLY EKIKVPVDWN RVNKPPYPKL 450
    GGNMKKLENC NYAVDLGKNQ AKFSLVGIAG QDLNEGNRTL TLALVWQLMR 500
    RYTLNILEDI GGGQKVNDDI IVNWVNTTLK EAQKSSSIAS FKDPKISTSL 550
    PVLDLIDAIQ PGSINYDLLK TENLDDEEKL NNAKYAISMA RKIGARVYAL 600
    PEDLVEVNPK MVMTVFACLM GKGMKRV 627
    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:
    EMBL
    GenBank
    DDBJ
    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_006518701.1.
    XP_006518765.1. XM_006518702.1.
    XP_006518766.1. XM_006518703.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS27276.1.
    PIRi I49445.
    RefSeqi NP_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.
    UniGenei Mm.153911.
    Mm.484415.

    3D structure databases

    ProteinModelPortali Q61233.
    SMRi Q61233. Positions 7-77, 118-627.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202256. 3 interactions.
    IntActi Q61233. 7 interactions.
    MINTi MINT-217293.

    PTM databases

    PhosphoSitei Q61233.

    2D gel databases

    COMPLUYEAST-2DPAGE Q61233.
    REPRODUCTION-2DPAGE Q61233.

    Proteomic databases

    MaxQBi Q61233.
    PaxDbi Q61233.
    PRIDEi Q61233.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000124499 ; ENSMUSP00000121201 ; ENSMUSG00000021998 .
    ENSMUST00000131802 ; ENSMUSP00000117137 ; ENSMUSG00000021998 .
    ENSMUST00000145303 ; ENSMUSP00000116271 ; ENSMUSG00000021998 .
    GeneIDi 18826.
    KEGGi mmu:18826.
    UCSCi uc007uqm.2. mouse.

    Organism-specific databases

    CTDi 3936.
    MGIi MGI:104808. Lcp1.

    Phylogenomic databases

    eggNOGi COG5069.
    GeneTreei ENSGT00390000005691.
    HOGENOMi HOG000213447.
    HOVERGENi HBG003082.
    InParanoidi Q61233.
    KOi K17276.
    OMAi HLYADID.
    OrthoDBi EOG7K9K2D.
    PhylomeDBi Q61233.
    TreeFami TF300680.

    Miscellaneous databases

    NextBioi 295196.
    PROi Q61233.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61233.
    Bgeei Q61233.
    CleanExi MM_LCP1.
    Genevestigatori Q61233.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.418.10. 4 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF00307. CH. 4 hits.
    PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00033. CH. 4 hits.
    SM00054. EFh. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 142 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