TEA4_SCHPO
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 03-AUG-2022, entry version 127.
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.
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; 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; 4896.SPBC1706.01.1; -.
DR iPTMnet; O60132; -.
DR MaxQB; O60132; -.
DR PaxDb; O60132; -.
DR PRIDE; O60132; -.
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:0051523; P:cell growth mode switching, monopolar to bipolar; IMP:PomBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; 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: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 GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1902486; P:protein localization to growing cell tip; IMP:PomBase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 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
