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O60132 (TEA4_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tip elongation aberrant protein Tea4
Alternative name(s):
Cell polarity protein tea4
Win1-interacting SH3 domain protein
Gene names
Name:tea4
Synonyms:wsh3
ORF Names:SPBC1706.01
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell polarity factor essential for the bipolar localization and function of structures containing the cell-end marker tea1 during the normal cell cycle. Regulates cell polarity in complex with tea1 and together with the stress signaling MAPK cascade, contributes to cell polarity maintenance under stress conditions. Required for the localization of for3 at the cell tip specifically during initiation of bipolar growth. During the new end take off (NETO), formation of a protein complex that includes tea1, tea4 and for3 is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends. Ref.3 Ref.4

Subunit structure

An essential component of the tea1 cell-end complex. Interacts with win1, tea1 and for3. Interacts with tip1 in the presence of tea1. Ref.3 Ref.4

Subcellular location

Cytoplasmcytoskeleton. Note: Through it's binding with tea1, is transported by the cytoplasmic microtubule system and is localized at cell tips, microtubule plus ends and cytoplasmic dots. Ref.3 Ref.4

Sequence similarities

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainSH3 domain
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of bipolar cell growth

Inferred from mutant phenotype Ref.4. Source: PomBase

cellular protein localization

Inferred from mutant phenotype Ref.4Ref.3. Source: PomBase

establishment or maintenance of actin cytoskeleton polarity

Inferred from mutant phenotype Ref.4. Source: PomBase

establishment or maintenance of cell polarity regulating cell shape

Inferred from mutant phenotype Ref.4Ref.3. Source: PomBase

microtubule-based process

Inferred by curator. Source: PomBase

regulation of filamentous growth

Inferred from mutant phenotype PubMed 19542312. Source: PomBase

   Cellular_componentTea1 cell-end complex

Inferred from direct assay Ref.3. Source: PomBase

cell cortex of cell tip

Inferred from direct assay Ref.4. Source: PomBase

cell tip

Inferred from direct assay PubMed 19646873PubMed 20870879. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

microtubule cytoskeleton

Inferred from direct assay Ref.4. Source: PomBase

non-growing cell tip

Inferred from direct assay PubMed 20870879. Source: PomBase

nucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

   Molecular_functionprotein binding

Inferred from physical interaction Ref.4Ref.3. Source: UniProtKB

protein binding, bridging

Inferred from physical interaction Ref.4. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 821821Tip elongation aberrant protein Tea4
PRO_0000259412

Regions

Domain130 – 19162SH3
Region527 – 821295Interaction with tea1
Region599 – 821223Interaction with win1
Compositional bias108 – 1114Poly-Glu
Compositional bias272 – 704433Ser-rich

Amino acid modifications

Modified residue351Phosphotyrosine Ref.5
Modified residue361Phosphoserine Ref.5
Modified residue401Phosphotyrosine Ref.5

Sequences

Sequence LengthMass (Da)Tools
O60132 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: B1DC53794E56D73E

FASTA82190,794
        10         20         30         40         50         60 
MLHMNSASSA DSMEIMESHF DPTQQNDSTI IESRYSPEEY LEQSFEIQRI ISGENSEPQT 

        70         80         90        100        110        120 
VASQEISDSQ EEDTTLTSSQ FEDCGTEYNE VVEDDEFRSE DEDDFMDEEE EYALYEAELS 

       130        140        150        160        170        180 
SSPSIHEEVI DCNFVHAIRG FEATVEGQVD ATKGDMMILL DDSNSYWWLV KMCKNLAIGY 

       190        200        210        220        230        240 
LPAEYIETPS ERLARLNKYK NSETSNSQQS VTLPPLDIVE KTLEAPSPNF RIKRVTFTCS 

       250        260        270        280        290        300 
SNSSDDEMDS ENDYEAMVNR TVAENGLEIE FSDSSDSSLS AEYRSESEDH VTDSPAYVDL 

       310        320        330        340        350        360 
TELEGGFNQF NSTSFQSTSP LGLEIVETEI NGSSTTADSK NSHSPYSKFS SAYPDAENSN 

       370        380        390        400        410        420 
ISKINISIAG NKELYGNATQ SDPSLYSTWI ANKHKTASSA TVDSPLRRSL SVDAMQSNAS 

       430        440        450        460        470        480 
FSSYSSTSNT DKSLRPSSYS AVSESSNFTH DVSRDNKEIS LNAPKSIIVS QSDSFDTSNV 

       490        500        510        520        530        540 
TQDAPNDVEK EPISGQMPNN LSVQSLKQLE VYPIRHSVSI EMPSEKLLSP RLYSSSTPSS 

       550        560        570        580        590        600 
PTKGFQKDDE EDSENRKQAD KVELSPSSLL RQMSLPVDSS SQSDAQCTTS SVYITAERKA 

       610        620        630        640        650        660 
FSQSSIDLST LSNHHVNNEI NRRSFAGGFT SLADELSEMR ELLHESPAPL ECNEEMVIPT 

       670        680        690        700        710        720 
PELDASSAIP SSSISHDEDL LPRKNTEEST SSSSFSSLIT SPASLQYDEN PFKQSVVAEL 

       730        740        750        760        770        780 
NNNSSSVPFV DSAHASDIHA YDNDHVSTKN KEFNRRLREF ILDPDSLSGL YWSVKSAGVR 

       790        800        810        820 
ASRRVSRNIE GESVSSDLDD IFANVLKGLS DEMASLLNTN R 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Comparative functional genomics of the fission yeasts."
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K. expand/collapse author list , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL.
[3]"Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of Tea1 and protects cell polarity under environmental stress in S. pombe."
Tatebe H., Shimada K., Uzawa S., Morigasaki S., Shiozaki K.
Curr. Biol. 15:1006-1015(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TEA1 AND WIN1.
[4]"Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity."
Martin S.G., McDonald W.H., Yates J.R. III, Chang F.
Dev. Cell 8:479-491(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FOR3; TEA1 AND TIP1, SUBCELLULAR LOCATION.
[5]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35; SER-36 AND TYR-40, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA19002.2.
PIRT39626.
RefSeqNP_595240.2. NM_001021146.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276197. 35 interactions.
IntActO60132. 7 interactions.
MINTMINT-4677492.
STRING4896.SPBC1706.01-1.

Proteomic databases

MaxQBO60132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1706.01.1; SPBC1706.01.1:pep; SPBC1706.01.
GeneID2539642.
KEGGspo:SPBC1706.01.

Organism-specific databases

PomBaseSPBC1706.01.

Phylogenomic databases

eggNOGNOG291368.
OrthoDBEOG7MSMZD.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
PfamPF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800796.

Entry information

Entry nameTEA4_SCHPO
AccessionPrimary (citable) accession number: O60132
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 3, 2012
Last modified: June 11, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names