PAL1_SCHPO
ID PAL1_SCHPO Reviewed; 425 AA.
AC Q9UU83;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein pal1;
DE AltName: Full=Pears and lemons protein 1;
GN Name=pal1; ORFNames=SPCP1E11.04c;
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]
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 INTERACTION WITH SAD1.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH END4.
RX PubMed=15975911; DOI=10.1091/mbc.e04-11-0976;
RA Ge W., Chew T.G., Wachtler V., Naqvi S.N., Balasubramanian M.K.;
RT "The novel fission yeast protein Pal1p interacts with Hip1-related
RT Sla2p/End4p and is involved in cellular morphogenesis.";
RL Mol. Biol. Cell 16:4124-4138(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-119; SER-301;
RP SER-339; THR-358 AND SER-370, 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: Involved in cellular morphogenesis and cell wall integrity.
CC Important for the maintenance of a cylindrical cell shape.
CC {ECO:0000269|PubMed:15975911}.
CC -!- SUBUNIT: Interacts with end4 and sad1. {ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:15975911}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15975911};
CC Peripheral membrane protein {ECO:0000269|PubMed:15975911}.
CC Note=Localizes to cell tips during interphase and to the medial ring
CC during mitosis and cytokinesis.
CC -!- SIMILARITY: Belongs to the pal1 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; CU329672; CAB54863.1; -; Genomic_DNA.
DR PIR; T41683; T41683.
DR RefSeq; NP_588557.1; NM_001023544.2.
DR AlphaFoldDB; Q9UU83; -.
DR BioGRID; 276099; 11.
DR IntAct; Q9UU83; 1.
DR STRING; 4896.SPCP1E11.04c.1; -.
DR iPTMnet; Q9UU83; -.
DR MaxQB; Q9UU83; -.
DR PaxDb; Q9UU83; -.
DR PRIDE; Q9UU83; -.
DR EnsemblFungi; SPCP1E11.04c.1; SPCP1E11.04c.1:pep; SPCP1E11.04c.
DR GeneID; 2539537; -.
DR KEGG; spo:SPCP1E11.04c; -.
DR PomBase; SPCP1E11.04c; pal1.
DR VEuPathDB; FungiDB:SPCP1E11.04c; -.
DR eggNOG; ENOG502QPHY; Eukaryota.
DR HOGENOM; CLU_573854_0_0_1; -.
DR InParanoid; Q9UU83; -.
DR OMA; CRPHRNR; -.
DR PhylomeDB; Q9UU83; -.
DR PRO; PR:Q9UU83; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:PomBase.
DR InterPro; IPR013226; Pal1.
DR PANTHER; PTHR28307; PTHR28307; 1.
DR Pfam; PF08316; Pal1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..425
FT /note="Protein pal1"
FT /id="PRO_0000116895"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 425 AA; 46629 MW; A298ED69F4FE0FA7 CRC64;
MMVIENPFLS TATSSQTPQE DGVYTSSLHN SNNPFLAPKT ERVADPVMES MADDLFNSIQ
KKKEPSPASS ASASPVKKSA EALAERSNSS MGTFDPPPRY SKIARARSTH VASSSRHRSP
SHNDSSPSTQ SSLKSRGSIR RYKSVREGSH RPGRSSKEPL DQIDRLDVTG LYGSGSFHHD
GPFDACRPHR NRNSKKAPVA AFPKDSIANS IPKVGETYND PSVPKDFSRK AIHESLRTKN
ILQSPYKSVG IEEEFPSSGN NDTPGLTDST RIEGAMASKN AIARNEEMLA MEKAGLGRKN
SLIRKLGLNR SASMMSRTPN TLNRPSNYRS HSSMGTRRSP LNSPSQLDPI SNENESDTDD
SNTGLRNRTS PTAAPPPPSR RKTGGLNTRP YPQHAESQMS LPLTAKERSK PKKMGFFRRL
FHKKS
