ID   PIL1_SCHPO              Reviewed;         351 AA.
AC   O74960;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Probable sphingolipid long chain base-responsive protein pil1;
DE   AltName: Full=Protein kinase inhibitor pil1;
GN   Name=pil1; ORFNames=SPCC736.15;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAA19279.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-15; SER-17; SER-39;
RP   THR-230 AND THR-233, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Negative regulator of cell wall integrity (CWI) in unstressed
CC       cells, probably by inhibiting protein kinase ksg1/ppk21 activity and
CC       regulating their downstream CWI pathways pck2-MAP kinase pathway and
CC       protein kinase gad8 pathway. Activity may be regulated by the transient
CC       increase of sphingolipid long chain bases (LCBs) during heat stress (By
CC       similarity). {ECO:0000250|UniProtKB:P53252}.
CC   -!- PTM: Phosphorylated by ksg1 and ppk21. Phosphorylation is regulated by
CC       sphingolipid long chain bases (LCBs) (By similarity).
CC       {ECO:0000250|UniProtKB:P53252, ECO:0000305}.
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DR   EMBL; CU329672; CAA19279.1; -; Genomic_DNA.
DR   PIR; T41572; T41572.
DR   RefSeq; NP_587786.1; NM_001022779.2.
DR   AlphaFoldDB; O74960; -.
DR   SMR; O74960; -.
DR   BioGRID; 275665; 25.
DR   STRING; 4896.SPCC736.15.1; -.
DR   iPTMnet; O74960; -.
DR   MaxQB; O74960; -.
DR   PaxDb; O74960; -.
DR   PRIDE; O74960; -.
DR   EnsemblFungi; SPCC736.15.1; SPCC736.15.1:pep; SPCC736.15.
DR   GeneID; 2539093; -.
DR   KEGG; spo:SPCC736.15; -.
DR   PomBase; SPCC736.15; pil1.
DR   VEuPathDB; FungiDB:SPCC736.15; -.
DR   eggNOG; ENOG502QQ1T; Eukaryota.
DR   HOGENOM; CLU_046464_0_0_1; -.
DR   InParanoid; O74960; -.
DR   OMA; WGEGCDD; -.
DR   PhylomeDB; O74960; -.
DR   PRO; PR:O74960; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0036362; C:ascus membrane; IDA:PomBase.
DR   GO; GO:0032126; C:eisosome; IDA:PomBase.
DR   GO; GO:0036286; C:eisosome filament; IDA:PomBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR   GO; GO:0070941; P:eisosome assembly; IDA:PomBase.
DR   GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR   GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IMP:PomBase.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR028245; PIL1/LSP1.
DR   PANTHER; PTHR31962; PTHR31962; 1.
DR   Pfam; PF13805; Pil1; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Probable sphingolipid long chain base-responsive
FT                   protein pil1"
FT                   /id="PRO_0000308182"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         15
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53252"
FT   MOD_RES         230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   351 AA;  39806 MW;  8B245D5FF62C4B06 CRC64;
     MMNRAYSLRN SRAPTASQLL NPPPPSSSTR SGRLFAPLSH TMRINHAATF TPDLAKRLAV
     LVKMEKNVMR SMEVTIRGRR DCARQLSYWG EDCDDDISDV TDKLGVLFYE MAELENYLID
     RYDQYRMTLK SIRNIESSVQ PSREKKQKLL DQIYALKHKD PESPRLVTME QELVREEAAC
     LVAEAQLSNT TREKFKQAMT FNLDALHEHA EKLNLIATYG RHLLNLIDDT PVTPGEARPA
     YDGYETSRQI VMDAEHALSS WVPSQPAVNF VKPQIEDDAQ SDARSWNEYE AQGEPVPVEQ
     VTHLQDDVQS DTSEIIENEP GMHPHVHAER MSRIASESSD AVPQQTAVQV A