TEA3_SCHPO
ID TEA3_SCHPO Reviewed; 1125 AA.
AC O14248;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Tip elongation aberrant protein 3;
DE AltName: Full=Cell polarity protein tea3;
GN Name=tea3; ORFNames=SPAC6G10.02c;
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]
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, AND SUBCELLULAR LOCATION.
RX PubMed=12007420; DOI=10.1016/s0960-9822(02)00821-7;
RA Arellano M., Niccoli T., Nurse P.;
RT "Tea3p is a cell end marker activating polarized growth in
RT Schizosaccharomyces pombe.";
RL Curr. Biol. 12:751-756(2002).
RN [3]
RP FUNCTION.
RX PubMed=14663827; DOI=10.1002/yea.1054;
RA Niccoli T., Arellano M., Nurse P.;
RT "Role of Tea1p, Tea3p and Pom1p in the determination of cell ends in
RT Schizosaccharomyces pombe.";
RL Yeast 20:1349-1358(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-437; SER-460;
RP SER-523; SER-980; SER-982; SER-983; SER-984; SER-1078 AND SER-1080, 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: Acts as a cell end marker required for efficient new end
CC take-off (NETO), whereby growth is activated at the cell end to
CC generate bipolarity in extending cells. Also required for proper
CC placement of the septum. {ECO:0000269|PubMed:12007420,
CC ECO:0000269|PubMed:14663827}.
CC -!- INTERACTION:
CC O14248; O59740: mod5; NbExp=3; IntAct=EBI-875326, EBI-875310;
CC O14248; P87061: tea1; NbExp=2; IntAct=EBI-875326, EBI-875376;
CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:12007420}. Cell
CC septum {ECO:0000269|PubMed:12007420}. Note=Present at both poles of the
CC cell throughout the cell cycle whether they are growing or not. Located
CC at the septum at time of cytokinesis.
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DR EMBL; CU329670; CAB11288.1; -; Genomic_DNA.
DR PIR; T39052; T39052.
DR RefSeq; NP_594099.1; NM_001019523.2.
DR AlphaFoldDB; O14248; -.
DR SMR; O14248; -.
DR BioGRID; 279073; 51.
DR IntAct; O14248; 3.
DR STRING; 4896.SPAC6G10.02c.1; -.
DR iPTMnet; O14248; -.
DR MaxQB; O14248; -.
DR PaxDb; O14248; -.
DR PRIDE; O14248; -.
DR EnsemblFungi; SPAC6G10.02c.1; SPAC6G10.02c.1:pep; SPAC6G10.02c.
DR GeneID; 2542619; -.
DR KEGG; spo:SPAC6G10.02c; -.
DR PomBase; SPAC6G10.02c; tea3.
DR VEuPathDB; FungiDB:SPAC6G10.02c; -.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_287452_0_0_1; -.
DR InParanoid; O14248; -.
DR OMA; CSDESFQ; -.
DR PhylomeDB; O14248; -.
DR PRO; PR:O14248; -.
DR Proteomes; UP000002485; Chromosome I.
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:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000935; C:division septum; EXP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0061246; P:establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF50965; SSF50965; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Kelch repeat; Phosphoprotein;
KW Reference proteome; Repeat; Septation.
FT CHAIN 1..1125
FT /note="Tip elongation aberrant protein 3"
FT /id="PRO_0000119149"
FT REPEAT 73..123
FT /note="Kelch 1"
FT REPEAT 124..179
FT /note="Kelch 2"
FT REPEAT 181..226
FT /note="Kelch 3"
FT REPEAT 259..308
FT /note="Kelch 4"
FT REPEAT 310..360
FT /note="Kelch 5"
FT REGION 507..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1125 AA; 127755 MW; 56DF209D681ED2EA CRC64;
MVQKVLSRQS DNSQDVSAEQ LDVVESGSID QQNIRAWVVR KVKENDKRTS TNQSFKWEAV
KPASCLDAAN EKFMYLHGGR EKSGISNSLF KLDLDSCTVY SHNRGEDNDS PARVGHSIVC
SADTIYLFGG CDSETDSTFE VGDNSLYAYN FKSNQWNLVS TQSPLPSPRT GHSMLLVDSK
LWIFGGECQG KYLNDIHLFD TKGVDRRTQS ELKQKANANN VEKANMEFDE TDWSWETPFL
HSSSPPPRSN HSVTLVQGKI FVHGGHNDTG PLSDLWLFDL ETLSWTEVRS IGRFPGPREG
HQATTIDDTV YIYGGRDNKG LILNELWAFN YSQQRWSLVS NPIPILLSDS SSYKIVSKNN
HILLLYLNAL DAPKQLLCYE ADPKNLYWDK DKFSDIPVLQ HISMKPSNAS NHTVSLGYLN
DRPNHSKKNS VTSTSSSQFN NFLEQNQKAV RSARHRHYAS LDEQGLHSLR NLSKTSGMNH
SADFSLHEFG QADPFAYEIE KPIASLPLPN GNDTISRSSE SSSPINESES NSLLKLQSDF
KFSNSDDRVA WLEEQLLYCM QQGYTLKPPN LFQHVDEKLR LEKKEQLSYL EILKVIEQML
ESNEQKFKKQ IVSLASENAK LAAQRDAAVE NANYSRSLIQ KKTTDETVGS LIEKVGKLEY
EVQGTLEEAT SYYQKNTELQ QLLKQNESAS ELLKSRNEKL CVDYDKLRSV FEEDSSKILS
LQKENENLQS QILQISEELV DYRSRCEALE YGNYELETKL IEMHDRVEMQ TNVIEASASA
LDVSNTAILS FEDSLRRERD EKSTLQQKCL NLQYEYENVR IELENLQSRA LELESALEQS
VSDAKYSKAI MQSGLSKLLS SINENKDNLK EFSKSKQKIS YLESQLEGLH ELLRESQRLC
EGRTKELLNS QQKLYDLKHS YSSVMTEKSK LSDQVNDLTE QAKITQRKLS EVQIALADSK
MNQQLSGKDS TDVHLPTDFS ASSSPLRSYF NEEDSFNNAS AAHSSKESDI PSGGVFTKYR
NHFGNLMTSE ETKAPDNNDL HKRLSDVINS QQKFLSLSPQ VSKDYYDVRS KLNDTAGSFS
GEEMRAIDDN YYASRIKQLE DDYQKAITYA NCSDESFQQL SHSFM
