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O70579

- PM34_MOUSE

UniProt

O70579 - PM34_MOUSE

Protein

Peroxisomal membrane protein PMP34

Gene

Slc25a17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extend for nicotinamide adenine dinucleotide (NAD+), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD+ from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. Inhibited by pyridoxal 5'-phosphate and bathophenanthroline in vitro By similarity.By similarity

    GO - Molecular functioni

    1. ADP transmembrane transporter activity Source: UniProtKB
    2. AMP transmembrane transporter activity Source: UniProtKB
    3. ATP transmembrane transporter activity Source: Ensembl
    4. coenzyme A transmembrane transporter activity Source: UniProtKB
    5. FAD transmembrane transporter activity Source: UniProtKB
    6. FMN transmembrane transporter activity Source: UniProtKB
    7. NAD transporter activity Source: UniProtKB

    GO - Biological processi

    1. ADP transport Source: UniProtKB
    2. AMP transport Source: UniProtKB
    3. coenzyme A transmembrane transport Source: UniProtKB
    4. FAD transmembrane transport Source: UniProtKB
    5. fatty acid beta-oxidation Source: Ensembl
    6. fatty acid transport Source: Ensembl
    7. NAD transport Source: UniProtKB

    Keywords - Biological processi

    Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal membrane protein PMP34
    Alternative name(s):
    34 kDa peroxisomal membrane protein
    Solute carrier family 25 member 17
    Gene namesi
    Name:Slc25a17
    Synonyms:Pmp34, Pmp35
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1342248. Slc25a17.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of peroxisomal membrane Source: UniProtKB
    2. mitochondrion Source: MGI
    3. peroxisomal membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 307307Peroxisomal membrane protein PMP34PRO_0000090706Add
    BLAST

    Proteomic databases

    MaxQBiO70579.
    PaxDbiO70579.
    PRIDEiO70579.

    PTM databases

    PhosphoSiteiO70579.

    Expressioni

    Tissue specificityi

    Expressed in liver.

    Gene expression databases

    BgeeiO70579.
    GenevestigatoriO70579.

    Interactioni

    Subunit structurei

    Interacts (via N- and C-terminus peroxisomal targeting regions) with PEX19; the interaction occurs with the newly synthesized SLC25A17 in the cytosol.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000023040.

    Structurei

    3D structure databases

    ProteinModelPortaliO70579.
    SMRiO70579. Positions 13-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicBy similarity
    Topological domaini31 – 6636LumenalSequence AnalysisAdd
    BLAST
    Topological domaini88 – 10417CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini126 – 16035LumenalSequence AnalysisAdd
    BLAST
    Topological domaini182 – 20221CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini224 – 28057LumenalSequence AnalysisAdd
    BLAST
    Topological domaini302 – 3076CytoplasmicBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei67 – 8721Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei105 – 12521Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei161 – 18121Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei203 – 22321Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei281 – 30121Helical; Name=6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati7 – 9286Solcar 1Add
    BLAST
    Repeati99 – 19294Solcar 2Add
    BLAST
    Repeati200 – 29495Solcar 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 147147Necessary for targeting to peroxisomes and interaction with PEX19By similarityAdd
    BLAST
    Regioni244 – 30764Necessary for targeting to peroxisomes and interaction with PEX19By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi190 – 19910Peroxisome localization signalBy similarity

    Domaini

    The N- and C-terminal portions are exposed to the cytoplasm. A region between helical transmembrane domains (TM) 4 and 5 and TM1-TM3 or TM4-TM6 are necessary for the peroxisome-targeting activity By similarity. Lacks a typical peroxisomal sorting signal.By similarity

    Sequence similaritiesi

    Contains 3 Solcar repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG258628.
    GeneTreeiENSGT00600000084419.
    HOGENOMiHOG000159426.
    HOVERGENiHBG003235.
    InParanoidiO70579.
    KOiK13354.
    OMAiKNEGPQA.
    OrthoDBiEOG7Q8CNK.
    PhylomeDBiO70579.
    TreeFamiTF324772.

    Family and domain databases

    Gene3Di1.50.40.10. 1 hit.
    InterProiIPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view]
    PfamiPF00153. Mito_carr. 3 hits.
    [Graphical view]
    PRINTSiPR00926. MITOCARRIER.
    SUPFAMiSSF103506. SSF103506. 1 hit.
    PROSITEiPS50920. SOLCAR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O70579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVLSYESL VHAVAGAVGS VTAMTVFFPL DTARLRLQVD EKRKSKTTHA    50
    VLLEIIKEEG LLAPYRGWFP VISSLCCSNF VYFYTFNSLK AVWVKGQRSS 100
    TGKDLVVGFV AGVVNVLLTT PLWVVNTRLK LQGAKFRNED IIPTNYKGII 150
    DAFHQIIRDE GILALWNGTF PSLLLVFNPA IQFMFYEGLK RQLLKKRMKL 200
    SSLDVFIIGA IAKAIATTVT YPMQTVQSIL RFGRHRLNPE NRTLGSLRNV 250
    LSLLHQRVKR FGIMGLYKGL EAKLLQTVLT AALMFLVYEK LTAATFTVMG 300
    LKSTHKH 307
    Length:307
    Mass (Da):34,413
    Last modified:August 1, 1998 - v1
    Checksum:i8CE406CE66D0EB06
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006341 mRNA. Translation: CAA06984.1.
    AK002388 mRNA. Translation: BAB22062.1.
    BC008571 mRNA. Translation: AAH08571.1.
    BC011292 mRNA. Translation: AAH11292.1.
    CCDSiCCDS27666.1.
    RefSeqiNP_035529.1. NM_011399.3.
    UniGeneiMm.222536.

    Genome annotation databases

    EnsembliENSMUST00000023040; ENSMUSP00000023040; ENSMUSG00000022404.
    GeneIDi20524.
    KEGGimmu:20524.
    UCSCiuc007wwk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006341 mRNA. Translation: CAA06984.1 .
    AK002388 mRNA. Translation: BAB22062.1 .
    BC008571 mRNA. Translation: AAH08571.1 .
    BC011292 mRNA. Translation: AAH11292.1 .
    CCDSi CCDS27666.1.
    RefSeqi NP_035529.1. NM_011399.3.
    UniGenei Mm.222536.

    3D structure databases

    ProteinModelPortali O70579.
    SMRi O70579. Positions 13-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000023040.

    PTM databases

    PhosphoSitei O70579.

    Proteomic databases

    MaxQBi O70579.
    PaxDbi O70579.
    PRIDEi O70579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023040 ; ENSMUSP00000023040 ; ENSMUSG00000022404 .
    GeneIDi 20524.
    KEGGi mmu:20524.
    UCSCi uc007wwk.1. mouse.

    Organism-specific databases

    CTDi 10478.
    MGIi MGI:1342248. Slc25a17.

    Phylogenomic databases

    eggNOGi NOG258628.
    GeneTreei ENSGT00600000084419.
    HOGENOMi HOG000159426.
    HOVERGENi HBG003235.
    InParanoidi O70579.
    KOi K13354.
    OMAi KNEGPQA.
    OrthoDBi EOG7Q8CNK.
    PhylomeDBi O70579.
    TreeFami TF324772.

    Miscellaneous databases

    ChiTaRSi SLC25A17. mouse.
    NextBioi 298759.
    PROi O70579.
    SOURCEi Search...

    Gene expression databases

    Bgeei O70579.
    Genevestigatori O70579.

    Family and domain databases

    Gene3Di 1.50.40.10. 1 hit.
    InterProi IPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view ]
    Pfami PF00153. Mito_carr. 3 hits.
    [Graphical view ]
    PRINTSi PR00926. MITOCARRIER.
    SUPFAMi SSF103506. SSF103506. 1 hit.
    PROSITEi PS50920. SOLCAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of human PMP34, a protein closely related to the peroxisomal integral membrane protein PMP47 of Candida boidinii."
      Wylin T., Baes M., Brees C., Mannaerts G.P., Fransen M., Van Veldhoven P.P.
      Eur. J. Biochem. 258:332-338(1998) [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: Kidney.
    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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiPM34_MOUSE
    AccessioniPrimary (citable) accession number: O70579
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 109 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