PCFT_MOUSE
ID PCFT_MOUSE Reviewed; 459 AA.
AC Q6PEM8; Q571I8; Q5SYG0; Q8R1H7; Q9D1P1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Proton-coupled folate transporter {ECO:0000303|PubMed:21346251};
DE AltName: Full=Heme carrier protein 1 {ECO:0000303|PubMed:16143108};
DE AltName: Full=PCFT/HCP1 {ECO:0000250|UniProtKB:Q96NT5};
DE AltName: Full=Solute carrier family 46 member 1 {ECO:0000305};
GN Name=Slc46a1 {ECO:0000312|MGI:MGI:1098733};
GN Synonyms=D11Ertd18e {ECO:0000312|MGI:MGI:1098733},
GN Hcp1 {ECO:0000303|PubMed:16143108}, Pcft {ECO:0000303|PubMed:21346251};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Okazaki N., Kikuno F.R., Nagase T., Ohara O., Koga H.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16143108; DOI=10.1016/j.cell.2005.06.025;
RA Shayeghi M., Latunde-Dada G.O., Oakhill J.S., Laftah A.H., Takeuchi K.,
RA Halliday N., Khan Y., Warley A., McCann F.E., Hider R.C., Frazer D.M.,
RA Anderson G.J., Vulpe C.D., Simpson R.J., McKie A.T.;
RT "Identification of an intestinal heme transporter.";
RL Cell 122:789-801(2005).
RN [6]
RP FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17962486; DOI=10.1167/iovs.07-0288;
RA Umapathy N.S., Gnana-Prakasam J.P., Martin P.M., Mysona B., Dun Y.,
RA Smith S.B., Ganapathy V., Prasad P.D.;
RT "Cloning and functional characterization of the proton-coupled electrogenic
RT folate transporter and analysis of its expression in retinal cell types.";
RL Invest. Ophthalmol. Vis. Sci. 48:5299-5305(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19074442; DOI=10.1074/jbc.m807665200;
RA Zhao R., Min S.H., Wang Y., Campanella E., Low P.S., Goldman I.D.;
RT "A role for the proton-coupled folate transporter (PCFT-SLC46A1) in folate
RT receptor-mediated endocytosis.";
RL J. Biol. Chem. 284:4267-4274(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21346251; DOI=10.1182/blood-2010-04-279653;
RA Salojin K.V., Cabrera R.M., Sun W., Chang W.C., Lin C., Duncan L.,
RA Platt K.A., Read R., Vogel P., Liu Q., Finnell R.H., Oravecz T.;
RT "A mouse model of hereditary folate malabsorption: deletion of the PCFT
RT gene leads to systemic folate deficiency.";
RL Blood 117:4895-4904(2011).
RN [11]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=22058337; DOI=10.1167/iovs.11-8264;
RA Gnana-Prakasam J.P., Reddy S.K., Veeranan-Karmegam R., Smith S.B.,
RA Martin P.M., Ganapathy V.;
RT "Polarized distribution of heme transporters in retinal pigment epithelium
RT and their regulation in the iron-overload disease hemochromatosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9279-9286(2011).
CC -!- FUNCTION: Proton-coupled folate symporter that mediates folate
CC absorption using an H(+) gradient as a driving force (PubMed:17962486).
CC Involved in the intestinal absorption of folates at the brush-border
CC membrane of the proximal jejunum, and the transport from blood to
CC cerebrospinal fluid across the choroid plexus (PubMed:17962486).
CC Functions at acidic pH via alternate outward- and inward-open
CC conformation states (By similarity). Protonation of residues in the
CC outward open state primes the protein for transport (By similarity).
CC Binding of folate promotes breaking of salt bridge network and
CC subsequent closure of the extracellular gate, leading to the inward-
CC open state and release of protons and folate (By similarity). Also able
CC to transport antifolate drugs, such as methotrexate and pemetrexed
CC (PubMed:17962486). Involved in FOLR1-mediated endocytosis by serving as
CC a route of export of folates from acidified endosomes (By similarity).
CC Also acts as a lower-affinity, pH-independent heme carrier protein and
CC constitutes the main importer of heme in the intestine
CC (PubMed:16143108). Imports heme in the retina and retinal pigment
CC epithelium, in neurons of the hippocampus, in hepatocytes and in the
CC renal epithelial cells (PubMed:22058337). Hence, participates in the
CC trafficking of heme and increases intracellular iron content (By
CC similarity). {ECO:0000250|UniProtKB:Q96NT5,
CC ECO:0000269|PubMed:16143108, ECO:0000269|PubMed:17962486,
CC ECO:0000269|PubMed:22058337}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=folate(in) + H(+)(in) = folate(out) + H(+)(out);
CC Xref=Rhea:RHEA:70159, ChEBI:CHEBI:15378, ChEBI:CHEBI:62501;
CC Evidence={ECO:0000269|PubMed:17962486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate(in) + H(+)(in) = (6S)-
CC 5-methyl-5,6,7,8-tetrahydrofolate(out) + H(+)(out);
CC Xref=Rhea:RHEA:70167, ChEBI:CHEBI:15378, ChEBI:CHEBI:18608;
CC Evidence={ECO:0000269|PubMed:17962486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + methotrexate(in) = H(+)(out) + methotrexate(out);
CC Xref=Rhea:RHEA:70163, ChEBI:CHEBI:15378, ChEBI:CHEBI:50681;
CC Evidence={ECO:0000269|PubMed:17962486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + pemetrexed(in) = H(+)(out) + pemetrexed(out);
CC Xref=Rhea:RHEA:70171, ChEBI:CHEBI:15378, ChEBI:CHEBI:63724;
CC Evidence={ECO:0000250|UniProtKB:Q96NT5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96NT5};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:16143108}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:19074442};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q96NT5}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:16143108}. Note=Shifts
CC from the apical membrane of intestinal cells iron-deficient cells to
CC the cytoplasm in response to increased in iron stores
CC (PubMed:16143108). Localizes to the basolateral membrane of choroid
CC plexus (PubMed:19074442). {ECO:0000269|PubMed:16143108,
CC ECO:0000269|PubMed:19074442}.
CC -!- TISSUE SPECIFICITY: Highly expressed in duodenum, especially in
CC duodenal mucosa, the main site of intestinal heme absorption
CC (PubMed:16143108). Expressed in the retina and retinal pigment
CC epithelium (PubMed:17962486, PubMed:22058337). Weakly expressed in the
CC kidney (PubMed:16143108). Not expressed in duodenum before weaning or
CC in placenta (PubMed:16143108). Weakly or not expressed in brain, heart,
CC lung, skeletal muscle, testis and neonatal liver (PubMed:16143108).
CC {ECO:0000269|PubMed:16143108, ECO:0000269|PubMed:17962486,
CC ECO:0000269|PubMed:22058337}.
CC -!- INDUCTION: Up-regulated in response to hypoxia, it is however unclear
CC whether such up-regulation is direct or not (PubMed:16143108). Not
CC induced in the duodenum of iron-deficient mice (PubMed:16143108).
CC {ECO:0000269|PubMed:16143108}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant mice develop severe macrocytic
CC normochromic anemia and ineffective erythropoiesis (PubMed:21346251).
CC More than 90% of mice die by 10 to 12 weeks of age (PubMed:21346251).
CC {ECO:0000269|PubMed:21346251}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. SLC46A
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90126.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI25543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK003278; BAB22685.1; -; mRNA.
DR EMBL; AK170505; BAE41843.1; -; mRNA.
DR EMBL; AK220201; BAD90126.1; ALT_INIT; mRNA.
DR EMBL; AL591177; CAI25542.1; -; Genomic_DNA.
DR EMBL; AL591177; CAI25543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC024522; AAH24522.1; -; mRNA.
DR EMBL; BC057976; AAH57976.1; -; mRNA.
DR CCDS; CCDS25104.1; -.
DR RefSeq; NP_081016.2; NM_026740.2.
DR AlphaFoldDB; Q6PEM8; -.
DR SMR; Q6PEM8; -.
DR STRING; 10090.ENSMUSP00000001126; -.
DR GlyGen; Q6PEM8; 2 sites.
DR iPTMnet; Q6PEM8; -.
DR PhosphoSitePlus; Q6PEM8; -.
DR jPOST; Q6PEM8; -.
DR MaxQB; Q6PEM8; -.
DR PaxDb; Q6PEM8; -.
DR PRIDE; Q6PEM8; -.
DR ProteomicsDB; 294344; -.
DR Antibodypedia; 26300; 120 antibodies from 26 providers.
DR DNASU; 52466; -.
DR Ensembl; ENSMUST00000001126; ENSMUSP00000001126; ENSMUSG00000020829.
DR GeneID; 52466; -.
DR KEGG; mmu:52466; -.
DR UCSC; uc007kjg.2; mouse.
DR CTD; 113235; -.
DR MGI; MGI:1098733; Slc46a1.
DR VEuPathDB; HostDB:ENSMUSG00000020829; -.
DR eggNOG; KOG2816; Eukaryota.
DR GeneTree; ENSGT00950000183096; -.
DR HOGENOM; CLU_028365_1_0_1; -.
DR InParanoid; Q6PEM8; -.
DR OMA; SPRANDE; -.
DR OrthoDB; 763423at2759; -.
DR PhylomeDB; Q6PEM8; -.
DR TreeFam; TF315701; -.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR Reactome; R-MMU-9707616; Heme signaling.
DR BioGRID-ORCS; 52466; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Slc46a1; mouse.
DR PRO; PR:Q6PEM8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PEM8; protein.
DR Bgee; ENSMUSG00000020829; Expressed in duodenum and 191 other tissues.
DR ExpressionAtlas; Q6PEM8; baseline and differential.
DR Genevisible; Q6PEM8; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0008517; F:folic acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0140211; F:folic acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015350; F:methotrexate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015078; F:proton transmembrane transporter activity; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904447; P:folate import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0098838; P:folate transmembrane transport; ISO:MGI.
DR GO; GO:0015884; P:folic acid transport; ISS:UniProtKB.
DR GO; GO:0015886; P:heme transport; IDA:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Disulfide bond; Endosome;
KW Folate-binding; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..459
FT /note="Proton-coupled folate transporter"
FT /id="PRO_0000084852"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 26..44
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 45..82
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 83..108
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 109..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 113..135
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 136..140
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 141..154
FT /note="Helical; Name=TM4"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 155..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 178..203
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 204..208
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 209..227
FT /note="Helical; Name=TM6"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 228..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 267..289
FT /note="Helical; Name=TM7"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 290..302
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 303..325
FT /note="Helical; Name=TM8"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 326..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 332..351
FT /note="Helical; Name=TM9"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 352..355
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 356..376
FT /note="Helical; Name=TM10"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 377..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 389..414
FT /note="Helical; Name=TM11"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 415..422
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TRANSMEM 423..441
FT /note="Helical; Name=TM12"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT TOPO_DOM 442..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT BINDING 156
FT /ligand="H(+)"
FT /ligand_id="ChEBI:CHEBI:15378"
FT /note="reversibly protonated residue during proton
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q96NT5"
FT BINDING 185
FT /ligand="H(+)"
FT /ligand_id="ChEBI:CHEBI:15378"
FT /note="reversibly protonated residue during proton
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q96NT5"
FT BINDING 281
FT /ligand="H(+)"
FT /ligand_id="ChEBI:CHEBI:15378"
FT /note="reversibly protonated residue during proton
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q96NT5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96NT5"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NT5"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..298
FT /evidence="ECO:0000250|UniProtKB:F1NJ67"
FT CONFLICT 402
FT /note="A -> V (in Ref. 1; BAB22685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50089 MW; A251124B3B9846AF CRC64;
MEGRVSSVGS PHSFLNAPVL FRGPVEPLVF LANFALVLQG PLTTQYLWHR FSTELGYNGT
RHRENCGNQS ADPLMKEVET LTSHWTLYMN VGGFLVGLFW STLLGAWSDR VGRRPLLVLA
SLGLLLQAVV SIFVVQLELH VGFFVLGRAL CALLGDFNGL LAASFASVAD VSSNHSRTFR
MALLEACIGV AGTLASLLGG HWLRAQGYAN PFWLALALLI VMALYAAFCF GETVKEPKST
RLFTLRHHRS IARLYVVPAP EKSRMHLALY SLAIFVVVTV HFGAQDILTL YELSAPLCWD
SKLIGYGSAA QHLPYLTSLL GLRLLQFCLA DTWVAEIGLA FNILGMVVFA FATITPLMFT
GYGLLFLSLV TTPVIRAKLS KLVSESEQGA LFSAVACVNS LAMLMASGIF NSIYPATLNF
MKGFPFLLGA GLLFIPAILI GVLEKVNPHP EFQQFPQSP
