PIL2_SCHPO
ID PIL2_SCHPO Reviewed; 383 AA.
AC O14128;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Probable sphingolipid long chain base-responsive protein pil2;
DE AltName: Full=Protein kinase inhibitor pil2;
GN Name=pil2; ORFNames=SPAC3C7.02c;
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:CAB16733.1}
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).
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; CU329670; CAB16733.1; -; Genomic_DNA.
DR PIR; T38688; T38688.
DR RefSeq; NP_593603.1; NM_001019034.1.
DR AlphaFoldDB; O14128; -.
DR SMR; O14128; -.
DR BioGRID; 278204; 49.
DR IntAct; O14128; 4.
DR STRING; 4896.SPAC3C7.02c.1; -.
DR PaxDb; O14128; -.
DR EnsemblFungi; SPAC3C7.02c.1; SPAC3C7.02c.1:pep; SPAC3C7.02c.
DR GeneID; 2541709; -.
DR KEGG; spo:SPAC3C7.02c; -.
DR PomBase; SPAC3C7.02c; pil2.
DR VEuPathDB; FungiDB:SPAC3C7.02c; -.
DR eggNOG; ENOG502QQ1T; Eukaryota.
DR HOGENOM; CLU_046464_0_1_1; -.
DR InParanoid; O14128; -.
DR OMA; ANQLSYW; -.
DR PhylomeDB; O14128; -.
DR PRO; PR:O14128; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0036286; C:eisosome filament; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0070941; P:eisosome assembly; ISO:PomBase.
DR GO; GO:0006897; P:endocytosis; ISO: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 3: Inferred from homology;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..383
FT /note="Probable sphingolipid long chain base-responsive
FT protein pil2"
FT /id="PRO_0000308181"
FT REGION 292..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53252"
SQ SEQUENCE 383 AA; 43301 MW; DFF0FB846D77BEBA CRC64;
MGTQPSYSIH TLRAPPKAKQ NQIPPSTTRR AVNVNKLGRQ FRYPSVGMFT PEMAKRLAAL
VKMEKDLLRS YENVAMERKE CANQLSYWGE DCDDDISDIS DKLGVLLYEI GELEEHMVDR
YDQYRVSLKT IRDIEASVQP TRVKKEKLLN SIYDVRSRDP ESPKLITMEQ ELVREEAACL
VAEAQLTNIT RENFKRAFTL HIGTLLEHSE KVAILCGYAK KILDLLDDTP IVPGEPRPIY
DGYNITRDYI VEAERELANW QNPFQTPEPL TDIDGLPSQS HYQTQFQASV VPRTDVINEP
PRRYSHANGV TTSGTTHSYT STGSKRYSQM GTEDYQPSFQ PNILQSTQVV DNFEIGEEDD
EEVGSQGVAE TSMPSTSAQP IAA
