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Q6PEM8

- PCFT_MOUSE

UniProt

Q6PEM8 - PCFT_MOUSE

Protein

Proton-coupled folate transporter

Gene

Slc46a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Has been shown to act both as an intestinal proton-coupled high-affinity folate transporter and as an intestinal heme transporter which mediates heme uptake from the gut lumen into duodenal epithelial cells. The iron is then released from heme and may be transported into the bloodstream. Dietary heme iron is an important nutritional source of iron. Shows a higher affinity for folate than heme.1 Publication

    GO - Molecular functioni

    1. folic acid binding Source: UniProtKB-KW
    2. folic acid transporter activity Source: UniProtKB
    3. heme transporter activity Source: UniProtKB
    4. methotrexate transporter activity Source: Ensembl

    GO - Biological processi

    1. folic acid transport Source: UniProtKB
    2. heme transport Source: UniProtKB
    3. transmembrane transport Source: InterPro

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Folate-binding

    Enzyme and pathway databases

    ReactomeiREACT_205755. Iron uptake and transport.
    REACT_220137. Metabolism of folate and pterines.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proton-coupled folate transporter
    Alternative name(s):
    Heme carrier protein 1
    PCFT/HCP1
    Solute carrier family 46 member 1
    Gene namesi
    Name:Slc46a1
    Synonyms:D11Ertd18e, Hcp1, Pcft
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1098733. Slc46a1.

    Subcellular locationi

    Apical cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cytoplasm 1 Publication
    Note: Localizes to the apical membrane of intestinal cells in iron-deficient cells, while it resides in internal cellular compartments in iron-replete cells.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. brush border membrane Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Proton-coupled folate transporterPRO_0000084852Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Glycosylationi58 – 581N-linked (GlcNAc...)1 Publication
    Modified residuei458 – 4581Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiQ6PEM8.

    PTM databases

    PhosphoSiteiQ6PEM8.

    Expressioni

    Tissue specificityi

    Highly expressed in duodenum, especially in duodenal mucosa, the main site of intestinal heme absorption. Weakly expressed in the kidney. Not expressed in duodenum before weaning or in placenta. Weakly or not expressed in brain, heart, lung, skeletal muscle, testis and neonatal liver.1 Publication

    Inductioni

    Up-regulated in response to hypoxia, it is however unclear whether such up-regulation is direct or not. Not induced in the duodenum of iron-deficient mice.1 Publication

    Gene expression databases

    ArrayExpressiQ6PEM8.
    BgeeiQ6PEM8.
    CleanExiMM_SLC46A1.
    GenevestigatoriQ6PEM8.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000001126.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PEM8.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei115 – 13521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei149 – 16921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei183 – 20321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei211 – 23121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei267 – 28721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei303 – 32523HelicalSequence AnalysisAdd
    BLAST
    Transmembranei337 – 35721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei390 – 41021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei423 – 44321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG306680.
    GeneTreeiENSGT00530000063076.
    HOGENOMiHOG000054191.
    HOVERGENiHBG055334.
    InParanoidiQ6PEM8.
    KOiK14613.
    OMAiQRGGCSN.
    OrthoDBiEOG7DNNVC.
    PhylomeDBiQ6PEM8.
    TreeFamiTF315701.

    Family and domain databases

    InterProiIPR011701. MFS.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view]
    PfamiPF07690. MFS_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF103473. SSF103473. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6PEM8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGRVSSVGS PHSFLNAPVL FRGPVEPLVF LANFALVLQG PLTTQYLWHR    50
    FSTELGYNGT RHRENCGNQS ADPLMKEVET LTSHWTLYMN VGGFLVGLFW 100
    STLLGAWSDR VGRRPLLVLA SLGLLLQAVV SIFVVQLELH VGFFVLGRAL 150
    CALLGDFNGL LAASFASVAD VSSNHSRTFR MALLEACIGV AGTLASLLGG 200
    HWLRAQGYAN PFWLALALLI VMALYAAFCF GETVKEPKST RLFTLRHHRS 250
    IARLYVVPAP EKSRMHLALY SLAIFVVVTV HFGAQDILTL YELSAPLCWD 300
    SKLIGYGSAA QHLPYLTSLL GLRLLQFCLA DTWVAEIGLA FNILGMVVFA 350
    FATITPLMFT GYGLLFLSLV TTPVIRAKLS KLVSESEQGA LFSAVACVNS 400
    LAMLMASGIF NSIYPATLNF MKGFPFLLGA GLLFIPAILI GVLEKVNPHP 450
    EFQQFPQSP 459
    Length:459
    Mass (Da):50,089
    Last modified:July 5, 2004 - v1
    Checksum:iA251124B3B9846AF
    GO

    Sequence cautioni

    The sequence BAD90126.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI25543.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti402 – 4021A → V in BAB22685. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003278 mRNA. Translation: BAB22685.1.
    AK170505 mRNA. Translation: BAE41843.1.
    AK220201 mRNA. Translation: BAD90126.1. Different initiation.
    AL591177 Genomic DNA. Translation: CAI25542.1.
    AL591177 Genomic DNA. Translation: CAI25543.1. Sequence problems.
    BC024522 mRNA. Translation: AAH24522.1.
    BC057976 mRNA. Translation: AAH57976.1.
    CCDSiCCDS25104.1.
    RefSeqiNP_081016.2. NM_026740.2.
    UniGeneiMm.131618.

    Genome annotation databases

    EnsembliENSMUST00000001126; ENSMUSP00000001126; ENSMUSG00000020829.
    GeneIDi52466.
    KEGGimmu:52466.
    UCSCiuc007kjg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003278 mRNA. Translation: BAB22685.1 .
    AK170505 mRNA. Translation: BAE41843.1 .
    AK220201 mRNA. Translation: BAD90126.1 . Different initiation.
    AL591177 Genomic DNA. Translation: CAI25542.1 .
    AL591177 Genomic DNA. Translation: CAI25543.1 . Sequence problems.
    BC024522 mRNA. Translation: AAH24522.1 .
    BC057976 mRNA. Translation: AAH57976.1 .
    CCDSi CCDS25104.1.
    RefSeqi NP_081016.2. NM_026740.2.
    UniGenei Mm.131618.

    3D structure databases

    ProteinModelPortali Q6PEM8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000001126.

    PTM databases

    PhosphoSitei Q6PEM8.

    Proteomic databases

    PRIDEi Q6PEM8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001126 ; ENSMUSP00000001126 ; ENSMUSG00000020829 .
    GeneIDi 52466.
    KEGGi mmu:52466.
    UCSCi uc007kjg.2. mouse.

    Organism-specific databases

    CTDi 113235.
    MGIi MGI:1098733. Slc46a1.

    Phylogenomic databases

    eggNOGi NOG306680.
    GeneTreei ENSGT00530000063076.
    HOGENOMi HOG000054191.
    HOVERGENi HBG055334.
    InParanoidi Q6PEM8.
    KOi K14613.
    OMAi QRGGCSN.
    OrthoDBi EOG7DNNVC.
    PhylomeDBi Q6PEM8.
    TreeFami TF315701.

    Enzyme and pathway databases

    Reactomei REACT_205755. Iron uptake and transport.
    REACT_220137. Metabolism of folate and pterines.

    Miscellaneous databases

    ChiTaRSi SLC46A1. mouse.
    NextBioi 308995.
    PROi Q6PEM8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PEM8.
    Bgeei Q6PEM8.
    CleanExi MM_SLC46A1.
    Genevestigatori Q6PEM8.

    Family and domain databases

    InterProi IPR011701. MFS.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view ]
    Pfami PF07690. MFS_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103473. SSF103473. 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].
      Strain: C57BL/6J and NOD.
    2. Okazaki N., Kikuno F.R., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Spleen.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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: FVB/N.
      Tissue: Colon and Liver.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    6. "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-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58.

    Entry informationi

    Entry nameiPCFT_MOUSE
    AccessioniPrimary (citable) accession number: Q6PEM8
    Secondary accession number(s): Q571I8
    , Q5SYG0, Q8R1H7, Q9D1P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 97 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