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Q9JMD3

- PCTL_MOUSE

UniProt

Q9JMD3 - PCTL_MOUSE

Protein

PCTP-like protein

Gene

Stard10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes By similarity. May play metabolic roles in sperm maturation or fertilization.By similarity1 Publication

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. bile acid secretion Source: MGI
    2. positive regulation of peroxisome proliferator activated receptor signaling pathway Source: MGI

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PCTP-like protein
    Short name:
    PCTP-L
    Alternative name(s):
    START domain-containing protein 10
    Short name:
    StARD10
    Serologically defined colon cancer antigen 28 homolog
    StAR-related lipid transfer protein 10
    Gene namesi
    Name:Stard10
    Synonyms:Pctpl, Sdccag28, Sdccagg28
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1860093. Stard10.

    Subcellular locationi

    Cell projectionciliumflagellum 1 Publication. Cytoplasm By similarity. Membrane By similarity
    Note: Mainly cytosolic By similarity. In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm.By similarity

    GO - Cellular componenti

    1. cilium Source: UniProtKB-KW
    2. cytosol Source: MGI
    3. intercellular canaliculus Source: MGI
    4. membrane Source: MGI
    5. microvillus Source: MGI

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Flagellum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 291291PCTP-like proteinPRO_0000220662Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei94 – 941N6-succinyllysine1 Publication
    Modified residuei197 – 1971N6-succinyllysine1 Publication
    Modified residuei202 – 2021N6-succinyllysine1 Publication
    Modified residuei284 – 2841Phosphoserine; by CK2

    Post-translational modificationi

    Phosphorylation at Ser-284 by CK2 negatively regulates lipid transfer activity, possibly by decreasing membrane association.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JMD3.
    PaxDbiQ9JMD3.
    PRIDEiQ9JMD3.

    PTM databases

    PhosphoSiteiQ9JMD3.

    Expressioni

    Tissue specificityi

    Testis, kidney, liver, and intestine with the highest level in the testis.

    Developmental stagei

    During male germ cell development, it was detected first in the 23-day-old mouse testis, and the signal increased with age.

    Gene expression databases

    ArrayExpressiQ9JMD3.
    BgeeiQ9JMD3.
    CleanExiMM_STARD10.
    GenevestigatoriQ9JMD3.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9JMD3. 1 interaction.
    MINTiMINT-1855443.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JMD3.
    SMRiQ9JMD3. Positions 42-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 224211STARTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 START domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG292439.
    GeneTreeiENSGT00510000047611.
    HOVERGENiHBG031807.
    InParanoidiQ9JMD3.
    PhylomeDBiQ9JMD3.
    TreeFamiTF354285.

    Family and domain databases

    Gene3Di3.30.530.20. 1 hit.
    InterProiIPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view]
    PfamiPF01852. START. 1 hit.
    [Graphical view]
    SMARTiSM00234. START. 1 hit.
    [Graphical view]
    PROSITEiPS50848. START. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JMD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKPAASTEP QGSRPALGRE SVQVPDDQDF RSFRSECEAE VGWNLTYSKA    50
    GVSVWVQAVE MDRTLHKIKC RMECCDVPAE TLYDVLHDIE YRKKWDSNVI 100
    ETFDIARLTV NADVGYYSWR CPKPLKNRDV ITLRSWLPMG ADYIIMNYSV 150
    KHPKYPPRKD LVRAVSIQTG YLIQSTGPKS CVITYLAQVD PKGSLPKWVV 200
    NKSSQFLAPK AMKKMYKACI KYPEWKQKHQ PHFKPWLHPE QSPLPSLALS 250
    ELSVQHADSL ENIDESAVTE SREERAGGAG GEGSDDDTSL T 291
    Length:291
    Mass (Da):32,951
    Last modified:October 1, 2000 - v1
    Checksum:i598467C430D97080
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031550 mRNA. Translation: BAA92233.1.
    CCDSiCCDS21509.1.
    RefSeqiNP_064374.1. NM_019990.4.
    UniGeneiMm.28896.

    Genome annotation databases

    EnsembliENSMUST00000032927; ENSMUSP00000032927; ENSMUSG00000030688.
    ENSMUST00000164479; ENSMUSP00000133002; ENSMUSG00000030688.
    GeneIDi56018.
    KEGGimmu:56018.
    UCSCiuc009ioi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031550 mRNA. Translation: BAA92233.1 .
    CCDSi CCDS21509.1.
    RefSeqi NP_064374.1. NM_019990.4.
    UniGenei Mm.28896.

    3D structure databases

    ProteinModelPortali Q9JMD3.
    SMRi Q9JMD3. Positions 42-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JMD3. 1 interaction.
    MINTi MINT-1855443.

    PTM databases

    PhosphoSitei Q9JMD3.

    Proteomic databases

    MaxQBi Q9JMD3.
    PaxDbi Q9JMD3.
    PRIDEi Q9JMD3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032927 ; ENSMUSP00000032927 ; ENSMUSG00000030688 .
    ENSMUST00000164479 ; ENSMUSP00000133002 ; ENSMUSG00000030688 .
    GeneIDi 56018.
    KEGGi mmu:56018.
    UCSCi uc009ioi.1. mouse.

    Organism-specific databases

    CTDi 10809.
    MGIi MGI:1860093. Stard10.

    Phylogenomic databases

    eggNOGi NOG292439.
    GeneTreei ENSGT00510000047611.
    HOVERGENi HBG031807.
    InParanoidi Q9JMD3.
    PhylomeDBi Q9JMD3.
    TreeFami TF354285.

    Miscellaneous databases

    ChiTaRSi STARD10. mouse.
    NextBioi 311762.
    PROi Q9JMD3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JMD3.
    Bgeei Q9JMD3.
    CleanExi MM_STARD10.
    Genevestigatori Q9JMD3.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR023393. START-like_dom.
    IPR002913. START_lipid-bd_dom.
    [Graphical view ]
    Pfami PF01852. START. 1 hit.
    [Graphical view ]
    SMARTi SM00234. START. 1 hit.
    [Graphical view ]
    PROSITEi PS50848. START. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of phosphatidylcholine transfer protein-like protein gene expressed in murine haploid germ cells."
      Yamanaka M., Koga M., Tanaka H., Nakamura Y., Ohta H., Yomogida K., Tsuchida J., Iguchi N., Nojima H., Nozaki M., Matsumiya K., Okuyama A., Toshimori K., Nishimune Y.
      Biol. Reprod. 62:1694-1701(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Testis.
    2. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-197 AND LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPCTL_MOUSE
    AccessioniPrimary (citable) accession number: Q9JMD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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