ID   TEA4_SCHPO              Reviewed;         821 AA.
AC   O60132;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Tip elongation aberrant protein Tea4;
DE   AltName: Full=Cell polarity protein tea4;
DE   AltName: Full=Win1-interacting SH3 domain protein;
GN   Name=tea4 {ECO:0000312|PomBase:SPBC1706.01};
GN   Synonyms=wsh3 {ECO:0000303|PubMed:15936270}; ORFNames=SPBC1706.01;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TEA1 AND WIN1.
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   [4] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH FOR3; TEA1 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35; SER-36 AND TYR-40, 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: Cell polarity factor essential for the bipolar localization
CC       and function of structures containing the cell-end marker tea1 during
CC       the normal cell cycle. Regulates cell polarity in complex with tea1 and
CC       together with the stress signaling MAPK cascade, contributes to cell
CC       polarity maintenance under stress conditions. Required for the
CC       localization of for3 at the cell tip specifically during initiation of
CC       bipolar growth. During the new end take off (NETO), formation of a
CC       protein complex that includes tea1, tea4 and for3 is necessary and
CC       sufficient for the establishment of cell polarity and localized actin
CC       assembly at new cell ends. {ECO:0000269|PubMed:15809031,
CC       ECO:0000269|PubMed:15936270}.
CC   -!- SUBUNIT: An essential component of the tea1 cell-end complex. Interacts
CC       with win1, tea1 and for3. Interacts with tip1 in the presence of tea1.
CC       {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270}.
CC   -!- INTERACTION:
CC       O60132; P13681: dis2; NbExp=2; IntAct=EBI-1099982, EBI-4320127;
CC       O60132; O94532: for3; NbExp=5; IntAct=EBI-1099982, EBI-1102572;
CC       O60132; Q09690: pom1; NbExp=5; IntAct=EBI-1099982, EBI-4319163;
CC       O60132; P87061: tea1; NbExp=10; IntAct=EBI-1099982, EBI-875376;
CC       O60132; O74304: win1; NbExp=2; IntAct=EBI-1099982, EBI-1099995;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270}.
CC       Note=Through it's binding with tea1, is transported by the cytoplasmic
CC       microtubule system and is localized at cell tips, microtubule plus ends
CC       and cytoplasmic dots.
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DR   EMBL; CU329671; CAA19002.2; -; Genomic_DNA.
DR   PIR; T39626; T39626.
DR   RefSeq; NP_595240.2; NM_001021146.2.
DR   AlphaFoldDB; O60132; -.
DR   SMR; O60132; -.
DR   BioGRID; 276197; 44.
DR   IntAct; O60132; 7.
DR   STRING; 284812.O60132; -.
DR   iPTMnet; O60132; -.
DR   MaxQB; O60132; -.
DR   PaxDb; 4896-SPBC1706-01-1; -.
DR   EnsemblFungi; SPBC1706.01.1; SPBC1706.01.1:pep; SPBC1706.01.
DR   GeneID; 2539642; -.
DR   KEGG; spo:SPBC1706.01; -.
DR   PomBase; SPBC1706.01; tea4.
DR   VEuPathDB; FungiDB:SPBC1706.01; -.
DR   eggNOG; ENOG502R17J; Eukaryota.
DR   HOGENOM; CLU_376493_0_0_1; -.
DR   InParanoid; O60132; -.
DR   OMA; WWLVKIC; -.
DR   PRO; PR:O60132; -.
DR   Proteomes; UP000002485; Chromosome II.
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:0097575; C:lateral cell cortex; IDA:PomBase.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-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:0008093; F:cytoskeletal anchor activity; IMP:PomBase.
DR   GO; GO:0061171; P:establishment of bipolar cell polarity; IMP:PomBase.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR   GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IMP:PomBase.
DR   GO; GO:0097248; P:maintenance of protein location in cell cortex of cell tip; IMP:PomBase.
DR   GO; GO:1903067; P:negative regulation of protein localization to cell tip; IMP:PomBase.
DR   GO; GO:2000784; P:positive regulation of establishment of cell polarity regulating cell shape; EXP:PomBase.
DR   GO; GO:1903068; P:positive regulation of protein localization to cell tip; EXP:PomBase.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:PomBase.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR47775; BUD SITE SELECTION PROTEIN 14; 1.
DR   PANTHER; PTHR47775:SF1; BUD SITE SELECTION PROTEIN 14; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..821
FT                   /note="Tip elongation aberrant protein Tea4"
FT                   /id="PRO_0000259412"
FT   DOMAIN          130..191
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..821
FT                   /note="Interaction with tea1"
FT   REGION          529..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..821
FT                   /note="Interaction with win1"
FT   REGION          664..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         35
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         40
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   821 AA;  90794 MW;  B1DC53794E56D73E CRC64;
     MLHMNSASSA DSMEIMESHF DPTQQNDSTI IESRYSPEEY LEQSFEIQRI ISGENSEPQT
     VASQEISDSQ EEDTTLTSSQ FEDCGTEYNE VVEDDEFRSE DEDDFMDEEE EYALYEAELS
     SSPSIHEEVI DCNFVHAIRG FEATVEGQVD ATKGDMMILL DDSNSYWWLV KMCKNLAIGY
     LPAEYIETPS ERLARLNKYK NSETSNSQQS VTLPPLDIVE KTLEAPSPNF RIKRVTFTCS
     SNSSDDEMDS ENDYEAMVNR TVAENGLEIE FSDSSDSSLS AEYRSESEDH VTDSPAYVDL
     TELEGGFNQF NSTSFQSTSP LGLEIVETEI NGSSTTADSK NSHSPYSKFS SAYPDAENSN
     ISKINISIAG NKELYGNATQ SDPSLYSTWI ANKHKTASSA TVDSPLRRSL SVDAMQSNAS
     FSSYSSTSNT DKSLRPSSYS AVSESSNFTH DVSRDNKEIS LNAPKSIIVS QSDSFDTSNV
     TQDAPNDVEK EPISGQMPNN LSVQSLKQLE VYPIRHSVSI EMPSEKLLSP RLYSSSTPSS
     PTKGFQKDDE EDSENRKQAD KVELSPSSLL RQMSLPVDSS SQSDAQCTTS SVYITAERKA
     FSQSSIDLST LSNHHVNNEI NRRSFAGGFT SLADELSEMR ELLHESPAPL ECNEEMVIPT
     PELDASSAIP SSSISHDEDL LPRKNTEEST SSSSFSSLIT SPASLQYDEN PFKQSVVAEL
     NNNSSSVPFV DSAHASDIHA YDNDHVSTKN KEFNRRLREF ILDPDSLSGL YWSVKSAGVR
     ASRRVSRNIE GESVSSDLDD IFANVLKGLS DEMASLLNTN R
//