TEA1_SCHPO
ID TEA1_SCHPO Reviewed; 1147 AA.
AC P87061;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tip elongation aberrant protein 1;
DE AltName: Full=Altered polarity protein 8;
DE AltName: Full=Cell polarity protein tea1;
GN Name=tea1; Synonyms=alp8; ORFNames=SPCC1223.06;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9200612; DOI=10.1016/s0092-8674(00)80279-2;
RA Mata J., Nurse P.;
RT "tea1 and the microtubular cytoskeleton are important for generating global
RT spatial order within the fission yeast cell.";
RL Cell 89:939-949(1997).
RN [2]
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12034771; DOI=10.1083/jcb.200112027;
RA Behrens R., Nurse P.;
RT "Roles of fission yeast tea1p in the localization of polarity factors and
RT in organizing the microtubular cytoskeleton.";
RL J. Cell Biol. 157:783-793(2002).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TEA4.
RX PubMed=15936270; DOI=10.1016/j.cub.2005.04.061;
RA Tatebe H., Shimada K., Uzawa S., Morigasaki S., Shiozaki K.;
RT "Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of
RT Tea1 and protects cell polarity under environmental stress in S. pombe.";
RL Curr. Biol. 15:1006-1015(2005).
RN [6]
RP FUNCTION, INTERACTION WITH FOR3; TEA4 AND TIP1, AND SUBCELLULAR LOCATION.
RX PubMed=15809031; DOI=10.1016/j.devcel.2005.02.008;
RA Martin S.G., McDonald W.H., Yates J.R. III, Chang F.;
RT "Tea4p links microtubule plus ends with the formin for3p in the
RT establishment of cell polarity.";
RL Dev. Cell 8:479-491(2005).
RN [7]
RP INTERACTION WITH RAX2.
RX PubMed=17085965;
RA Choi E., Lee K., Song K.;
RT "Function of rax2p in the polarized growth of fission yeast.";
RL Mol. Cells 22:146-153(2006).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP 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: Cell polarity protein. Acts as an end marker, directing the
CC growth machinery to the cell poles. Involved in the regulation of
CC microtubular organization, affecting the maintenance of a single
CC central axis. Prevents the curling of microtubule tips around the cell
CC ends and is required for the retention of polarity factors such as
CC pom1, tip1 and tea2 at the cell ends, necessary for the cell to grow in
CC a straight line. Links tip1 and tea4 in a common complex.
CC {ECO:0000269|PubMed:12034771, ECO:0000269|PubMed:14663827,
CC ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270,
CC ECO:0000269|PubMed:9200612}.
CC -!- SUBUNIT: Major component of the tea1 cell-end complex. Interacts with
CC rax2, tea4 and tip1. Interacts with for3 in the presence of tea4.
CC {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270,
CC ECO:0000269|PubMed:17085965}.
CC -!- INTERACTION:
CC P87061; O14248: tea3; NbExp=2; IntAct=EBI-875376, EBI-875326;
CC P87061; O60132: tea4; NbExp=10; IntAct=EBI-875376, EBI-1099982;
CC P87061; P79065: tip1; NbExp=5; IntAct=EBI-875376, EBI-1102463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12034771, ECO:0000269|PubMed:15809031,
CC ECO:0000269|PubMed:15936270, ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:9200612}. Note=Present at both poles of the cell
CC throughout the cell cycle whether they are growing or not. Located at
CC the ends of microtubules growing towards the cell poles. An intact
CC microtubular skeleton is required to maintain the location at the cell
CC tips; on the other hand, a normally organized actin cytoskeleton is not
CC required.
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; Y12709; CAA73246.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20875.1; -; Genomic_DNA.
DR PIR; T40866; T40866.
DR RefSeq; NP_588351.1; NM_001023342.2.
DR AlphaFoldDB; P87061; -.
DR SMR; P87061; -.
DR BioGRID; 275620; 256.
DR IntAct; P87061; 5.
DR STRING; 4896.SPCC1223.06.1; -.
DR iPTMnet; P87061; -.
DR SwissPalm; P87061; -.
DR MaxQB; P87061; -.
DR PaxDb; P87061; -.
DR PRIDE; P87061; -.
DR EnsemblFungi; SPCC1223.06.1; SPCC1223.06.1:pep; SPCC1223.06.
DR GeneID; 2539047; -.
DR KEGG; spo:SPCC1223.06; -.
DR PomBase; SPCC1223.06; tea1.
DR VEuPathDB; FungiDB:SPCC1223.06; -.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_275217_0_0_1; -.
DR InParanoid; P87061; -.
DR OMA; WNRIKLQ; -.
DR PhylomeDB; P87061; -.
DR PRO; PR:P87061; -.
DR Proteomes; UP000002485; Chromosome III.
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:0005881; C:cytoplasmic microtubule; EXP:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:1990752; C:microtubule end; IDA:PomBase.
DR GO; GO:0035839; C:non-growing cell tip; IDA:PomBase.
DR GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:PomBase.
DR GO; GO:0061246; P:establishment or maintenance of bipolar cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:1990896; P:protein localization to cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011498; Kelch_2.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kelch repeat; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1147
FT /note="Tip elongation aberrant protein 1"
FT /id="PRO_0000119146"
FT REPEAT 94..144
FT /note="Kelch 1"
FT REPEAT 146..198
FT /note="Kelch 2"
FT REPEAT 199..253
FT /note="Kelch 3"
FT REPEAT 254..303
FT /note="Kelch 4"
FT REPEAT 305..351
FT /note="Kelch 5"
FT REPEAT 355..402
FT /note="Kelch 6"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..1147
FT /note="Interaction with tea4"
FT REGION 948..1147
FT /note="Retention at microtubule cell ends"
FT COILED 611..649
FT /evidence="ECO:0000255"
FT COILED 716..838
FT /evidence="ECO:0000255"
FT COILED 879..990
FT /evidence="ECO:0000255"
FT COILED 1084..1105
FT /evidence="ECO:0000255"
FT COMPBIAS 14..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1147 AA; 127436 MW; 7BE65F6C666EF4F8 CRC64;
MSFLFKRNKG SAHKPTKPNF SKTSTTPSTS QLKHSHESNV KMSTSTVTEH RKKPTGSGSH
ITASPWSKLT VRGSSNVLPR YSHASHLYAE GGQEIYIFGG VASDSQPKND LWVLNLATSQ
FTSLRSLGET PSPRLGHASI LIGNAFIVFG GLTNHDVADR QDNSLYLLNT SSLVWQKANA
SGARPSGRYG HTISCLGSKI CLFGGRLLDY YFNDLVCFDL NNLNTSDSRW ELASVVNDPP
PARAGHVAFT FSDKLYIFGG TDGANFFNDL WCYHPKQSAW SKVETFGVAP NPRAGHAASV
VEGILYVFGG RASDGTFLND LYAFRLSSKH WYKLSDLPFT PSPRSSHTLS CSGLTLVLIG
GKQGKGASDS NVYMLDTSRF RLGSVPTTSG RQRNTSFFSN STGNTNPSAF NGLLTSSRIP
SYNGSKVRST SHPSRQQYIG SSNSRFNTRH QTISTPVSGR ASNDLPSPVV PTRSNSSSIL
QPSYNLNSHS SDRRNTNDDD QSSLNSQQLS NQAKAQGEVS PTLSFVPSSH SMEQGNGSVA
SANNAQSEAA TRSINSISEV SEVRFPEQSS VKTVDERKSL DGRITSVTLE TLVEKYSELS
KQQIVEWFKS KLYEILRDSA SKIDSLTEKL KVANAEKNAA LCEAALEKVP LAKHNKLSDG
TFSTPDKENV QSTNDAHIMQ ENFSLHKALE VMRETSSDLD KQLKDATASQ KELIVQTSSF
QKELVEERER HNAISKRLQE IESLYRDREL LVTNLEDQLV DQTVTINKFA FERDQFRERS
MGFENTIKDL TRKMEATDML NVSLHESLRS VQTENSELVT EMALLKAELV KKQAIIDANA
NIYDKLTADH TNYETVSADI NQNLKETLDK LLNGSSDFKN NEIELLHDQI RITNAKLEKR
EKLINASKYI EDTLRSEIQE AAEKVSNLEF SNFNLKEENS NMQLQLMKAL EQRNTGAKQL
VNLRMQLSTA TSELDMLKLK LRTTALALEE SPDDYSDILS ILRADMSPFH DLHKQCGVLI
DTLNGVKRGF GIFEKKFTDY HKFLENISDK LKSEEDTSLE TPIHENQSIQ SDQIKEVGEV
LSAIKSLSDS VMLLKNQIDD LAKEKLPLSS SDDEKVNIKE KTDFMKLLVK SGLSNPPAKE
PVHDNEN
