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Q9JJ00

- PLS1_MOUSE

UniProt

Q9JJ00 - PLS1_MOUSE

Protein

Phospholipid scramblase 1

Gene

Plscr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.1 Publication
    May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation.1 Publication

    Cofactori

    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei127 – 1282Breakpoint for translocation to form MMTRA1A

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. CD4 receptor binding Source: UniProtKB
    3. DNA binding Source: UniProtKB-KW
    4. epidermal growth factor receptor binding Source: UniProtKB
    5. phospholipid scramblase activity Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
    7. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: UniProtKB
    2. cellular response to cytokine stimulus Source: UniProtKB
    3. cellular response to lipopolysaccharide Source: UniProtKB
    4. defense response to virus Source: UniProtKB
    5. intrinsic apoptotic signaling pathway Source: UniProtKB
    6. myeloid cell differentiation Source: MGI
    7. negative regulation of protein binding Source: MGI
    8. negative regulation of viral genome replication Source: UniProtKB
    9. phosphatidylserine biosynthetic process Source: UniProtKB
    10. phosphatidylserine exposure on apoptotic cell surface Source: MGI
    11. phospholipid scrambling Source: UniProtKB
    12. positive regulation of apoptotic process Source: MGI
    13. positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
    14. positive regulation of innate immune response Source: UniProtKB
    15. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
    16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    17. regulation of Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
    18. regulation of mast cell activation Source: UniProtKB
    19. response to interferon-alpha Source: UniProtKB

    Keywords - Biological processi

    Antiviral defense

    Keywords - Ligandi

    Calcium, DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipid scramblase 1
    Short name:
    PL scramblase 1
    Alternative name(s):
    Ca(2+)-dependent phospholipid scramblase 1
    Transplantability-associated protein 1
    Short name:
    NOR1
    Short name:
    TRA1
    Gene namesi
    Name:Plscr1
    Synonyms:Tra1b, Tras1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:893575. Plscr1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular matrix Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. membrane raft Source: UniProtKB
    6. nucleolus Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Participates in a chromosomal translocation that produces MMTRA1A which is leukemogenic to syngenic SL mice and athymic nude mice.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Phospholipid scramblase 1PRO_0000100785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphotyrosine; by ABLBy similarity
    Modified residuei170 – 1701Phosphothreonine; by PKCBy similarity
    Lipidationi193 – 1931S-palmitoyl cysteineBy similarity
    Lipidationi194 – 1941S-palmitoyl cysteineBy similarity
    Lipidationi197 – 1971S-palmitoyl cysteineBy similarity
    Lipidationi198 – 1981S-palmitoyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JJ00.
    PaxDbiQ9JJ00.
    PRIDEiQ9JJ00.

    PTM databases

    PhosphoSiteiQ9JJ00.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney, lung, liver and bone marrow, slightly in spleen, heart and macrophage.

    Inductioni

    Up-regulated by SCF/KITL and GCSF/CSF3.1 Publication

    Gene expression databases

    ArrayExpressiQ9JJ00.
    BgeeiQ9JJ00.
    CleanExiMM_PLSCR1.
    GenevestigatoriQ9JJ00.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9JJ00. 1 interaction.
    STRINGi10090.ENSMUSP00000108671.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJ00.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 297297CytoplasmicBy similarityAdd
    BLAST
    Topological domaini315 – 32814ExtracellularBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei298 – 31417HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9393Proline-rich domain (PRD)By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi18 – 269SH3-binding 1Sequence Analysis
    Motifi22 – 254WW-bindingSequence Analysis
    Motifi56 – 649SH3-binding 2Sequence Analysis
    Motifi93 – 1019SH3-binding 3Sequence Analysis
    Motifi269 – 2757Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi96 – 1016Poly-Pro
    Compositional biasi190 – 1989Cys-rich

    Domaini

    The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.By similarity

    Sequence similaritiesi

    Belongs to the phospholipid scramblase family.Curated

    Keywords - Domaini

    Repeat, SH3-binding, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG119855.
    GeneTreeiENSGT00390000002884.
    HOGENOMiHOG000237356.
    HOVERGENiHBG019157.
    OMAiFFESTGS.
    OrthoDBiEOG77T14X.
    TreeFamiTF314939.

    Family and domain databases

    InterProiIPR005552. Scramblase.
    [Graphical view]
    PANTHERiPTHR23248. PTHR23248. 1 hit.
    PfamiPF03803. Scramblase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JJ00-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENHSKQTEA PHPGTYMPAG YPPPYPPAAF QGPSDHAAYP IPQAGYQGPP    50
    GPYPGPQPGY PVPPGGYAGG GPSGFPVQNQ PAYNHPGGPG GTPWMPAPPP 100
    PLNCPPGLEY LAQIDQLLVH QQIELLEVLT GFETNNKYEI KNSLGQRVYF 150
    AVEDTDCCTR NCCGASRPFT LRILDNLGRE VMTLERPLRC SSCCFPCCLQ 200
    EIEIQAPPGV PVGYVTQTWH PCLPKFTLQN EKKQDVLKVV GPCVVCSCCS 250
    DIDFELKSLD EESVVGKISK QWSGFVREAF TDADNFGIQF PLDLDVKMKA 300
    VMLGACFLID FMFFERTGNE EQRSGAWQ 328
    Length:328
    Mass (Da):35,914
    Last modified:October 1, 2000 - v1
    Checksum:i6CA35DF8DBF72ACF
    GO

    Sequence cautioni

    The sequence BAA23664.1 differs from that shown. Reason: Frameshift at position 92.
    The sequence BAA23663.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 274PYPP → GLCV(PubMed:9108418)Curated
    Sequence conflicti130 – 1301T → A in BAB22897. (PubMed:16141072)Curated
    Sequence conflicti267 – 2671K → R in BAB22897. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159593 mRNA. Translation: AAF77076.1.
    AK003628 mRNA. Translation: BAB22897.1.
    D78354 mRNA. Translation: BAA23663.1. Different initiation.
    D78355 mRNA. Translation: BAA23664.1. Frameshift.
    CCDSiCCDS52886.1.
    RefSeqiNP_035766.2. NM_011636.2.
    XP_006511115.1. XM_006511052.1.
    UniGeneiMm.421956.
    Mm.441702.

    Genome annotation databases

    EnsembliENSMUST00000093801; ENSMUSP00000091318; ENSMUSG00000032369.
    GeneIDi22038.
    KEGGimmu:22038.
    UCSCiuc009ram.2. mouse.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159593 mRNA. Translation: AAF77076.1 .
    AK003628 mRNA. Translation: BAB22897.1 .
    D78354 mRNA. Translation: BAA23663.1 . Different initiation.
    D78355 mRNA. Translation: BAA23664.1 . Frameshift.
    CCDSi CCDS52886.1.
    RefSeqi NP_035766.2. NM_011636.2.
    XP_006511115.1. XM_006511052.1.
    UniGenei Mm.421956.
    Mm.441702.

    3D structure databases

    ProteinModelPortali Q9JJ00.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JJ00. 1 interaction.
    STRINGi 10090.ENSMUSP00000108671.

    PTM databases

    PhosphoSitei Q9JJ00.

    Proteomic databases

    MaxQBi Q9JJ00.
    PaxDbi Q9JJ00.
    PRIDEi Q9JJ00.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000093801 ; ENSMUSP00000091318 ; ENSMUSG00000032369 .
    GeneIDi 22038.
    KEGGi mmu:22038.
    UCSCi uc009ram.2. mouse.

    Organism-specific databases

    CTDi 5359.
    MGIi MGI:893575. Plscr1.

    Phylogenomic databases

    eggNOGi NOG119855.
    GeneTreei ENSGT00390000002884.
    HOGENOMi HOG000237356.
    HOVERGENi HBG019157.
    OMAi FFESTGS.
    OrthoDBi EOG77T14X.
    TreeFami TF314939.

    Miscellaneous databases

    NextBioi 301814.
    PROi Q9JJ00.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JJ00.
    Bgeei Q9JJ00.
    CleanExi MM_PLSCR1.
    Genevestigatori Q9JJ00.

    Family and domain databases

    InterProi IPR005552. Scramblase.
    [Graphical view ]
    PANTHERi PTHR23248. PTHR23248. 1 hit.
    Pfami PF03803. Scramblase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of three new members of the phospholipid scramblase gene family."
      Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.
      Biochim. Biophys. Acta 1467:244-253(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.
      Tissue: Embryo.
    3. "TRA1, a novel mRNA highly expressed in leukemogenic mouse monocytic sublines but not in nonleukemogenic sublines."
      Kasukabe T., Okabe-Kado J., Honma Y.
      Blood 89:2975-2985(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-328, CHROMOSOMAL TRANSLOCATION.
      Strain: BALB/c.
      Tissue: Kidney.
    4. "Normal hemostasis but defective hematopoietic response to growth factors in mice deficient in phospholipid scramblase 1."
      Zhou Q., Zhao J., Wiedmer T., Sims P.J.
      Blood 99:4030-4038(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiPLS1_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJ00
    Secondary accession number(s): O54730, O54731, Q9D1F8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Knockout newborn mice display a reduced granulocyte production. Hematopoietic precursor cell from knockout mice display defective colony formation and impaired differentiation to mature granulocytes as stimulated by SCF/KITL and GCSF/CSF3.

    Keywords - Technical termi

    Complete proteome, 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