PALH_NEUCR
ID PALH_NEUCR Reviewed; 778 AA.
AC Q7RY98;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=pH-response regulator protein palH/prr-4;
GN Name=prr-4; Synonyms=rim21; ORFNames=NCU00007;
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 [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).
CC -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC factor pacc-1 in response to alkaline ambient pH. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the palH/RIM21 family. {ECO:0000305}.
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DR EMBL; CM002238; EAA27758.1; -; Genomic_DNA.
DR RefSeq; XP_956994.1; XM_951901.2.
DR AlphaFoldDB; Q7RY98; -.
DR STRING; 5141.EFNCRP00000000319; -.
DR EnsemblFungi; EAA27758; EAA27758; NCU00007.
DR GeneID; 3873170; -.
DR KEGG; ncr:NCU00007; -.
DR VEuPathDB; FungiDB:NCU00007; -.
DR HOGENOM; CLU_014594_1_0_1; -.
DR InParanoid; Q7RY98; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071467; P:cellular response to pH; IBA:GO_Central.
DR InterPro; IPR014844; PalH.
DR PANTHER; PTHR35779; PTHR35779; 1.
DR Pfam; PF08733; PalH; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..778
FT /note="pH-response regulator protein palH/prr-4"
FT /id="PRO_0000058203"
FT TOPO_DOM 1..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..160
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..237
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..314
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..778
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 394..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 83992 MW; 682E9F473113A974 CRC64;
MEPRQLFSDP TADPISTAGA ASNALSCASF NLPEGGILQL PNGEIITLSA PAAFKPPSCN
LALRSVPNII ASGGVVGGTA SGTMGLKADD DSHFSDWRDP FYASTFPQCY ALAATTIIAY
TLVIMLFITP RSFLDGGVVV LGRKGFTNGG GGTSIGGRPW LQKVAALSVA ISLTIANAAT
FRAAEQQYSW GVQNAKQLQE DVLGGAELKI IRIISDTFLW LAQAQTLIRL FPRQREKVII
KWTAFALITL DVIFQSLNSF KYGGSDLTRP KFTEAVPALS YLFALALGVL YAAWVLYYSI
MKKRYAFYHP LMKNMILVAV LSVVSILVPV VFFILDISKP DFAGWGDYVR WVGAAAASVI
VWEWVERIEA LEREEKKDGI LGREVFDGDE MLEASQSEHA WPKMKRKGSG GSDSQDTESG
GGGKDGGPSL SRFGAWSKIS TLTSKHRTEP SSRNEPNEGS SPVAETTNDD ERPRFLSPPL
WPARPTPAAT PVSRTDTTSA ASTMYAVRYH TMTELTSYGT PPPTRNMGRL SGSESRGSSR
HRDYGSASPG SAPAQDARST QNSHVGAKAS SAGSRWHALT PTVSSRDFVT RSEPRSSKMQ
RDENSRWDLR ARVEEFAATQ AENLREKFRP TLDTNNLPVT VIPAPPRRGA AIAQLCEEEE
LNHSSREGTV REESRNSNAS GTVIAVGGAQ TPIQTSFSPP PRAANSSMST AQMPRPQLSP
IVTQGSFTNN RYNHLPVTVI PAPPRQDPAR APSQPQSPSL VALGKQPARS DSSTTPSP
