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MOD5P_SCHPO
ID   MOD5P_SCHPO             Reviewed;         522 AA.
AC   O59740;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cell polarity protein mod5;
DE   AltName: Full=Tea1-anchoring protein mod5;
GN   Name=mod5; ORFNames=SPBC530.04;
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   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-519.
RX   PubMed=12789340; DOI=10.1038/nature01672;
RA   Snaith H.A., Sawin K.E.;
RT   "Fission yeast mod5p regulates polarized growth through anchoring of tea1p
RT   at cell tips.";
RL   Nature 423:647-651(2003).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TEA1 AND TEA3.
RX   PubMed=16222337; DOI=10.1038/sj.emboj.7600838;
RA   Snaith H.A., Samejima I., Sawin K.E.;
RT   "Multistep and multimode cortical anchoring of tea1p at cell tips in
RT   fission yeast.";
RL   EMBO J. 24:3690-3699(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-303 AND SER-350, AND
RP   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: With tea1, acts in a positive-feedback loop in the
CC       microtubule-mediated regulation of cell polarity. Involved in the
CC       anchoring of tea1 at the cortex as well as the correct localization of
CC       tea3. {ECO:0000269|PubMed:12789340, ECO:0000269|PubMed:16222337}.
CC   -!- SUBUNIT: Interacts with tea1 and tea3. {ECO:0000269|PubMed:16222337}.
CC   -!- INTERACTION:
CC       O59740; O14248: tea3; NbExp=3; IntAct=EBI-875310, EBI-875326;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12789340};
CC       Peripheral membrane protein {ECO:0000269|PubMed:12789340}; Cytoplasmic
CC       side {ECO:0000269|PubMed:12789340}. Note=localizes to the cell tips.
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DR   EMBL; CU329671; CAA19170.1; -; Genomic_DNA.
DR   PIR; T40520; T40520.
DR   RefSeq; NP_595317.1; NM_001021224.2.
DR   AlphaFoldDB; O59740; -.
DR   BioGRID; 277410; 14.
DR   IntAct; O59740; 2.
DR   STRING; 4896.SPBC530.04.1; -.
DR   iPTMnet; O59740; -.
DR   MaxQB; O59740; -.
DR   PaxDb; O59740; -.
DR   PRIDE; O59740; -.
DR   EnsemblFungi; SPBC530.04.1; SPBC530.04.1:pep; SPBC530.04.
DR   GeneID; 2540894; -.
DR   KEGG; spo:SPBC530.04; -.
DR   PomBase; SPBC530.04; mod5.
DR   VEuPathDB; FungiDB:SPBC530.04; -.
DR   HOGENOM; CLU_535461_0_0_1; -.
DR   OMA; MKSAATY; -.
DR   PRO; PR:O59740; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IDA:PomBase.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0031520; C:plasma membrane of cell tip; IC:PomBase.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IMP:PomBase.
DR   GO; GO:0097248; P:maintenance of protein location in cell cortex of cell tip; IMP:PomBase.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..522
FT                   /note="Cell polarity protein mod5"
FT                   /id="PRO_0000351429"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MUTAGEN         519
FT                   /note="C->S: Prevents normal localization at the cell
FT                   tips."
FT                   /evidence="ECO:0000269|PubMed:12789340"
SQ   SEQUENCE   522 AA;  56542 MW;  AC84C95009BDB64F CRC64;
     MSALSESPAI PSFWRPETSE ISKKPRPNTT VGFQFDNRNV GTSAPSTPAI RRNNTDSFER
     GLSLPLPSSK QDTGSSVLDP DGDAYVNRYA RPVTAGSIYI PSNYHKSFSP NTFSGFNVKR
     SASKSPKRSA NGSTSEDISI EGSPSETAKG ARSSFNSNFR TFDIGSERRR RILEASQDSS
     RPGRYSYRTK SASPALIDTS TLDSRLNFTM GRLERSIAQL SKNTMRAVSH LENPPKDITL
     PKLNVKNSAW PLQPYSPPAN ETPASSSSSA KARPVSVPDM SSPVPASSVE YESLKAAVTY
     SPSQNPKKVA ETDSESRKSS FQSSYNDADR PFQVGAQTQS TPNRISRSDS PIVYDVDTHS
     EDNASTASSE AISQSMRSFQ PQPNTGSPFP RFTSTNTEDE QESDIPQSDA NDSTVNLNQP
     NYANLTPTPQ VSPKRPTYSR SSPLPSASVP ALGDGSPDPP AAPSIQNSLS VHESEMPPHV
     TRDYTQPAAS ATPVPKEKPS EKSEKPPKKK GSKLEKFCCI LM
 
 
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