PHO5_NEUCR
ID PHO5_NEUCR Reviewed; 570 AA.
AC Q7RVX9; Q01395;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Repressible high-affinity phosphate permease {ECO:0000303|PubMed:7883177};
GN Name=pho-5 {ECO:0000303|PubMed:7883177};
GN ORFNames=NCU08325 {ECO:0000312|EMBL:EAA33302.2};
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], INDUCTION, AND DISRUPTION PHENOTYPE.
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 [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 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 H(+)-phosphate symporter.
CC {ECO:0000269|PubMed:7732001}.
CC -!- ACTIVITY REGULATION: Phosphate transport activity is competitively
CC inhibited by arsenate. {ECO:0000269|PubMed:7732001}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37.4 uM for phosphate {ECO:0000269|PubMed:7732001};
CC Vmax=26.1 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-4 is also absent. {ECO:0000269|PubMed:7883177}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74899.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L36127; AAA74899.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CM002239; EAA33302.2; -; Genomic_DNA.
DR RefSeq; XP_962538.2; XM_957445.3.
DR AlphaFoldDB; Q7RVX9; -.
DR SMR; Q7RVX9; -.
DR STRING; 5141.EFNCRP00000008440; -.
DR TCDB; 2.A.1.9.2; the major facilitator superfamily (mfs).
DR PRIDE; Q7RVX9; -.
DR EnsemblFungi; EAA33302; EAA33302; NCU08325.
DR GeneID; 3878688; -.
DR KEGG; ncr:NCU08325; -.
DR VEuPathDB; FungiDB:NCU08325; -.
DR HOGENOM; CLU_001265_46_14_1; -.
DR InParanoid; Q7RVX9; -.
DR OMA; IAQTCIG; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0097079; F:selenite:proton symporter activity; IEA:EnsemblFungi.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR GO; GO:0097080; P:plasma membrane selenite transport; IEA:EnsemblFungi.
DR GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004738; Phos_permease.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00887; 2A0109; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphate transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..570
FT /note="Repressible high-affinity phosphate permease"
FT /id="PRO_0000431098"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..95
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..143
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 326..346
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..374
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 404..424
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..433
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 469..489
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..505
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 506..526
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 537..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 61702 MW; 80226A98DD52A563 CRC64;
MSTPQKTAGG NNAYHNFYND FLHIKDPNER RRLALAEVDR APFGWYHVRA VAVAGVGFFT
DSYDIFTVSL LTLMLGIVYF PGEGKMPTTS DTAIKLATSA GTVIGQVGFG AAADVFGRKS
MYGLELLFII FATLAQALAS GSPSINIIGI IIFWRVLMGV GIGGDYPLSS IITSEFATTK
WRGAMMGAVF AMQGLGQLAA AFVMLFVTLG FKKSLEAAPT LASCTGDCAV AVDKMWRTVI
GVGAVPGCIA LYYRLTIPET PRYTFDVKRD VEQASDDIEA FKTGKPKGQP DEATRIVAKQ
EAEKEMEIPK ASWGDFFRHY SKRKNAMLLA GTALSWCFLD IAYYGVSLNN ATILNVIGYS
TTGAKNTYEI LYNTAVGNLI IVLAGAVPGY WVTVFTVDTV GRKPIQFMGF GILTILFVVM
GFAYKHLSPH ALLAIFVLAQ FFFNFGPNAT TFIVPGEVFP TRYRSTSHGL SAAMGKIGSI
IGQGAIAPLR TRGAVKGGNP NPWMNHVLEI YALFMLLGVG TTFLIPETKR KTLEELSGEF
DMSGEEEAQR DTTLTEHKTE APTSSAAVNA
