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Protein

Proton-coupled folate transporter

Gene

Slc46a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Folate-binding

Enzyme and pathway databases

ReactomeiREACT_292451. Iron uptake and transport.
REACT_300004. 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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1098733. Slc46a1.

Subcellular locationi

  1. Apical cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
  2. Cytoplasm 1 Publication

  3. Note: Localizes to the apical membrane of intestinal cells in iron-deficient cells, while it resides in internal cellular compartments in iron-replete cells.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei25 – 4824HelicalSequence AnalysisAdd
BLAST
Topological domaini49 – 8436ExtracellularSequence AnalysisAdd
BLAST
Transmembranei85 – 10723HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 1136CytoplasmicSequence Analysis
Transmembranei114 – 13724HelicalSequence AnalysisAdd
BLAST
Topological domaini138 – 1458ExtracellularSequence Analysis
Transmembranei146 – 16823HelicalSequence AnalysisAdd
BLAST
Topological domaini169 – 18012CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei181 – 20323HelicalSequence AnalysisAdd
BLAST
Topological domaini204 – 2129ExtracellularSequence Analysis
Transmembranei213 – 23624HelicalSequence AnalysisAdd
BLAST
Topological domaini237 – 26529CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei266 – 28823HelicalSequence AnalysisAdd
BLAST
Topological domaini289 – 30921ExtracellularSequence AnalysisAdd
BLAST
Transmembranei310 – 32819HelicalSequence AnalysisAdd
BLAST
Topological domaini329 – 3313CytoplasmicSequence Analysis
Transmembranei332 – 35625HelicalSequence AnalysisAdd
BLAST
Topological domaini357 – 3593ExtracellularSequence Analysis
Transmembranei360 – 38122HelicalSequence AnalysisAdd
BLAST
Topological domaini382 – 39312CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei394 – 41219HelicalSequence AnalysisAdd
BLAST
Topological domaini413 – 42412ExtracellularSequence AnalysisAdd
BLAST
Transmembranei425 – 44925HelicalSequence AnalysisAdd
BLAST
Topological domaini450 – 45910CytoplasmicSequence Analysis

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. brush border membrane Source: Ensembl
  3. cell surface Source: MGI
  4. cytoplasm Source: UniProtKB
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
Modified residuei458 – 4581Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ6PEM8.
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

BgeeiQ6PEM8.
CleanExiMM_SLC46A1.
ExpressionAtlasiQ6PEM8. baseline and differential.
GenevestigatoriQ6PEM8.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001126.

Structurei

3D structure databases

ProteinModelPortaliQ6PEM8.
ModBaseiSearch...
MobiDBiSearch...

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.
IPR020846. MFS_dom.
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

        10         20         30         40         50
MEGRVSSVGS PHSFLNAPVL FRGPVEPLVF LANFALVLQG PLTTQYLWHR
60 70 80 90 100
FSTELGYNGT RHRENCGNQS ADPLMKEVET LTSHWTLYMN VGGFLVGLFW
110 120 130 140 150
STLLGAWSDR VGRRPLLVLA SLGLLLQAVV SIFVVQLELH VGFFVLGRAL
160 170 180 190 200
CALLGDFNGL LAASFASVAD VSSNHSRTFR MALLEACIGV AGTLASLLGG
210 220 230 240 250
HWLRAQGYAN PFWLALALLI VMALYAAFCF GETVKEPKST RLFTLRHHRS
260 270 280 290 300
IARLYVVPAP EKSRMHLALY SLAIFVVVTV HFGAQDILTL YELSAPLCWD
310 320 330 340 350
SKLIGYGSAA QHLPYLTSLL GLRLLQFCLA DTWVAEIGLA FNILGMVVFA
360 370 380 390 400
FATITPLMFT GYGLLFLSLV TTPVIRAKLS KLVSESEQGA LFSAVACVNS
410 420 430 440 450
LAMLMASGIF NSIYPATLNF MKGFPFLLGA GLLFIPAILI GVLEKVNPHP

EFQQFPQSP
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. Curated
The sequence CAI25543.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ6PEM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001126.

PTM databases

PhosphoSiteiQ6PEM8.

Proteomic databases

MaxQBiQ6PEM8.
PRIDEiQ6PEM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi113235.
MGIiMGI:1098733. Slc46a1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_292451. Iron uptake and transport.
REACT_300004. Metabolism of folate and pterines.

Miscellaneous databases

ChiTaRSiSlc46a1. mouse.
NextBioi308995.
PROiQ6PEM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PEM8.
CleanExiMM_SLC46A1.
ExpressionAtlasiQ6PEM8. baseline and differential.
GenevestigatoriQ6PEM8.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 103 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.