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Q8VDG5

- PPCS_MOUSE

UniProt

Q8VDG5 - PPCS_MOUSE

Protein

Phosphopantothenate--cysteine ligase

Gene

Ppcs

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine.By similarity

    Catalytic activityi

    CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.

    Pathwayi

    GO - Molecular functioni

    1. phosphopantothenate--cysteine ligase activity Source: UniProtKB-EC

    GO - Biological processi

    1. coenzyme A biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Enzyme and pathway databases

    ReactomeiREACT_216415. Coenzyme A biosynthesis.
    UniPathwayiUPA00241; UER00353.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphopantothenate--cysteine ligase (EC:6.3.2.5)
    Alternative name(s):
    Phosphopantothenoylcysteine synthetase
    Short name:
    PPC synthetase
    Gene namesi
    Name:Ppcs
    Synonyms:Coab
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1915237. Ppcs.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 311310Phosphopantothenate--cysteine ligasePRO_0000182041Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8VDG5.
    PaxDbiQ8VDG5.
    PRIDEiQ8VDG5.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00135484.

    PTM databases

    PhosphoSiteiQ8VDG5.

    Expressioni

    Gene expression databases

    BgeeiQ8VDG5.
    CleanExiMM_PPCS.
    GenevestigatoriQ8VDG5.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiQ8VDG5. 1 interaction.
    MINTiMINT-4108416.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VDG5.
    SMRiQ8VDG5. Positions 7-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPC synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0452.
    GeneTreeiENSGT00390000015263.
    HOGENOMiHOG000194726.
    HOVERGENiHBG049438.
    InParanoidiQ8VDG5.
    KOiK01922.
    OMAiRSAFPYA.
    OrthoDBiEOG7TTQ82.
    PhylomeDBiQ8VDG5.
    TreeFamiTF105615.

    Family and domain databases

    Gene3Di3.40.50.10300. 1 hit.
    InterProiIPR007085. DNA/pantothenate-metab_flavo_C.
    [Graphical view]
    PfamiPF04127. DFP. 2 hits.
    [Graphical view]
    SUPFAMiSSF102645. SSF102645. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8VDG5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEMDLVAEL PRPAGAARWA EVMARFAARL GEQGRRVVLI TSGGTKVPLE    50
    ARAVRFLDNF SSGRRGAASA EVFLAAGYGV LFLYRARSAF PYAHRFPPQA 100
    WLSALRPSGP AQSGKLSLEA EENALPGFAA ALQSYQEAAA AGTFLAVEFT 150
    TLADYLHLLQ AAALALSPLG SSAMFYLAAA VSDFYIPVSE MPEHKIHSSG 200
    GPLQITMKMV PKMLSPLVKD WAPKAFVVSF KLETDPDIII SRARNALEVY 250
    QHQVVVANIL ESIKSFVIIV TKDSETELLL SEEEVAKGLV IEEKIVDDLR 300
    SRHTAFICDK N 311
    Length:311
    Mass (Da):33,794
    Last modified:March 1, 2002 - v1
    Checksum:i082E03CB2E3A11E6
    GO
    Isoform 2 (identifier: Q8VDG5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-173: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:139
    Mass (Da):15,675
    Checksum:iEC8707370992774E
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 173172Missing in isoform 2. 1 PublicationVSP_010244Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006290 mRNA. Translation: BAB24509.1.
    AK159952 mRNA. Translation: BAE35508.1.
    BC021894 mRNA. Translation: AAH21894.1.
    CCDSiCCDS18581.1. [Q8VDG5-1]
    RefSeqiNP_080770.2. NM_026494.3. [Q8VDG5-1]
    XP_006502700.1. XM_006502637.1.
    XP_006502701.1. XM_006502638.1.
    UniGeneiMm.27245.

    Genome annotation databases

    EnsembliENSMUST00000030385; ENSMUSP00000030385; ENSMUSG00000028636. [Q8VDG5-1]
    ENSMUST00000106316; ENSMUSP00000101923; ENSMUSG00000028636.
    GeneIDi106564.
    KEGGimmu:106564.
    UCSCiuc008umm.1. mouse. [Q8VDG5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006290 mRNA. Translation: BAB24509.1 .
    AK159952 mRNA. Translation: BAE35508.1 .
    BC021894 mRNA. Translation: AAH21894.1 .
    CCDSi CCDS18581.1. [Q8VDG5-1 ]
    RefSeqi NP_080770.2. NM_026494.3. [Q8VDG5-1 ]
    XP_006502700.1. XM_006502637.1.
    XP_006502701.1. XM_006502638.1.
    UniGenei Mm.27245.

    3D structure databases

    ProteinModelPortali Q8VDG5.
    SMRi Q8VDG5. Positions 7-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8VDG5. 1 interaction.
    MINTi MINT-4108416.

    PTM databases

    PhosphoSitei Q8VDG5.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00135484.

    Proteomic databases

    MaxQBi Q8VDG5.
    PaxDbi Q8VDG5.
    PRIDEi Q8VDG5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030385 ; ENSMUSP00000030385 ; ENSMUSG00000028636 . [Q8VDG5-1 ]
    ENSMUST00000106316 ; ENSMUSP00000101923 ; ENSMUSG00000028636 .
    GeneIDi 106564.
    KEGGi mmu:106564.
    UCSCi uc008umm.1. mouse. [Q8VDG5-1 ]

    Organism-specific databases

    CTDi 79717.
    MGIi MGI:1915237. Ppcs.

    Phylogenomic databases

    eggNOGi COG0452.
    GeneTreei ENSGT00390000015263.
    HOGENOMi HOG000194726.
    HOVERGENi HBG049438.
    InParanoidi Q8VDG5.
    KOi K01922.
    OMAi RSAFPYA.
    OrthoDBi EOG7TTQ82.
    PhylomeDBi Q8VDG5.
    TreeFami TF105615.

    Enzyme and pathway databases

    UniPathwayi UPA00241 ; UER00353 .
    Reactomei REACT_216415. Coenzyme A biosynthesis.

    Miscellaneous databases

    NextBioi 358258.
    PROi Q8VDG5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8VDG5.
    CleanExi MM_PPCS.
    Genevestigatori Q8VDG5.

    Family and domain databases

    Gene3Di 3.40.50.10300. 1 hit.
    InterProi IPR007085. DNA/pantothenate-metab_flavo_C.
    [Graphical view ]
    Pfami PF04127. DFP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF102645. SSF102645. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Testis.
    2. "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] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiPPCS_MOUSE
    AccessioniPrimary (citable) accession number: Q8VDG5
    Secondary accession number(s): Q3TVW0, Q9D376, Q9DA06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The mammalian enzyme has a preference for ATP over CTP, in contrast to the E.coli ortholog.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3