PHO4_NEUCR
ID PHO4_NEUCR Reviewed; 590 AA.
AC P15710; Q7RV96; V5IMB0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phosphate-repressible phosphate permease pho-4 {ECO:0000303|PubMed:2531109};
GN Name=pho-4 {ECO:0000303|PubMed:2531109};
GN Synonyms=van {ECO:0000303|PubMed:6217193};
GN ORFNames=NCU09564 {ECO:0000303|PubMed:12712197};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ORSa / FGSC 2490;
RX PubMed=2531109; DOI=10.1016/0378-1119(89)90114-5;
RA Mann B.J., Bowman B.J., Grotelueschen J., Metzenberg R.L.;
RT "Nucleotide sequence of pho-4+, encoding a phosphate-repressible phosphate
RT permease of Neurospora crassa.";
RL Gene 83:281-289(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=6217193; DOI=10.1128/jb.153.1.292-296.1983;
RA Bowman B.J., Allen K.E., Slayman C.W.;
RT "Vanadate-resistant mutants of Neurospora crassa are deficient in a high-
RT affinity phosphate transport system.";
RL J. Bacteriol. 153:292-296(1983).
RN [4]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=59-29;
RX PubMed=7883177; DOI=10.1016/0378-1119(94)00814-9;
RA Versaw W.K.;
RT "A phosphate-repressible, high-affinity phosphate permease is encoded by
RT the pho-5+ gene of Neurospora crassa.";
RL Gene 153:135-139(1995).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=7732001; DOI=10.1073/pnas.92.9.3884;
RA Versaw W.K., Metzenberg R.L.;
RT "Repressible cation-phosphate symporters in Neurospora crassa.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3884-3887(1995).
CC -!- FUNCTION: High-affinity transporter for external inorganic phosphate.
CC Acts probably as a sodium-phosphate symporter. Component of the high
CC affinity phosphate transport system II (ptsII) necessary for scavenging
CC phosphorus from the environment under conditions of limiting
CC phosphorus. {ECO:0000269|PubMed:6217193, ECO:0000269|PubMed:7732001}.
CC -!- ACTIVITY REGULATION: Phosphate transport activity is competitively
CC inhibited by vanadate and arsenate. {ECO:0000269|PubMed:7732001}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.56 uM for phosphate {ECO:0000269|PubMed:7732001};
CC Vmax=7.0 nmol/min/mg enzyme {ECO:0000269|PubMed:7732001};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Transcription is controlled by the phosphorus-acquisition
CC regulatory system. {ECO:0000269|PubMed:7883177}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth at low phosphate conditions when
CC pho-5 is also absent. Prevents vanadate uptake.
CC {ECO:0000269|PubMed:6217193, ECO:0000269|PubMed:7883177}.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {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; M31364; AAA33607.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA41860.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA41861.1; -; Genomic_DNA.
DR PIR; JQ0116; JQ0116.
DR RefSeq; XP_011395302.1; XM_011397000.1.
DR RefSeq; XP_011395303.1; XM_011397001.1.
DR AlphaFoldDB; P15710; -.
DR SMR; P15710; -.
DR STRING; 5141.EFNCRP00000009174; -.
DR TCDB; 2.A.20.2.1; the inorganic phosphate transporter (pit) family.
DR EnsemblFungi; ESA41860; ESA41860; NCU09564.
DR EnsemblFungi; ESA41861; ESA41861; NCU09564.
DR GeneID; 3875636; -.
DR KEGG; ncr:NCU09564; -.
DR VEuPathDB; FungiDB:NCU09564; -.
DR HOGENOM; CLU_015355_3_0_1; -.
DR InParanoid; P15710; -.
DR OMA; MQAFCIA; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015319; F:sodium:inorganic phosphate symporter activity; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphate transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..590
FT /note="Phosphate-repressible phosphate permease pho-4"
FT /id="PRO_0000080780"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 297..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 63201 MW; 875429D4CE491A94 CRC64;
MVLHQFDYLL AIGTIFAALD AWNIGANDVA NSWATSVAAR SVTYLQAMIL GSIMEFAGSV
GVGARVADTI RTKVVDTTLF ADDPALLMLG MVCAVVASSI YLTMATRFGL PVSTTHSIMG
GVIGMGIAAV GADGVQWVGS SINDGVVSVF LAWVIAPGLA GAFASIIFLV TKYGVLLRSN
PVYKAFVMVP IYFGITAALL CMLLLWKGGS YKVTLTNPEI AGTIIGVGAA WALLVTIFLM
PWLYRIVILE DWQLRFWHIP LGPLLLRRGE VPPPPADGSG VVQDFYAGRL TKEQLAARRA
AQNGDSEMAA GAVTSSTSNP SAPTDGEKGA TITKDDSSYS HDHSEPAQAA QPQIKTMVGP
RPAGPWHSGA VLFWYVKWAL FRGVDQDVLS SQQEKSVISS DVEELHAHAT HYDNKTEYMY
SFLQIMTAAA ASFTHGANDI ANAIGPYATV FQLWKDGALP EKGKADVPVW ILVFGASCLV
IGLWTYGYNI MRNLGNRITL QSPSRGFSME LGSAVTVILA TRLKLPVSTT QCITGATVGV
GLCSGTWRTI NWRLVAWIYM GWFITLPVAG IISGCLMGII INAPRWGYSG
