Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O60132 (TEA4_SCHPO)

Last modified November 24, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.2 Ref.3

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.2 Ref.3

Subcellular location

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.2 Ref.3

Sequence similarities

Contains 1 SH3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 809809Tip elongation aberrant protein Tea4
PRO_0000259412

Regions

Domain118 – 17962SH3
Region515 – 809295Interaction with tea1 Ref.3
Region587 – 809223Interaction with win1 Ref.2
Compositional bias96 – 994Poly-Glu
Compositional bias260 – 692433Ser-rich

Amino acid modifications

Modified residue231Phosphotyrosine Ref.4
Modified residue241Phosphoserine Ref.4
Modified residue281Phosphotyrosine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O60132-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 2D1386C6BE0A046B

FASTA80989,562
        10         20         30         40         50         60 
MEIMESHFDP TQQNDSTIIE SRYSPEEYLE QSFEIQRIIS GENSEPQTVA SQEISDSQEE 

        70         80         90        100        110        120 
DTTLTSSQFE DCGTEYNEVV EDDEFRSEDE DDFMDEEEEY ALYEAELSSS PSIHEEVIDC 

       130        140        150        160        170        180 
NFVHAIRGFE ATVEGQVDAT KGDMMILLDD SNSYWWLVKM CKNLAIGYLP AEYIETPSER 

       190        200        210        220        230        240 
LARLNKYKNS ETSNSQQSVT LPPLDIVEKT LEAPSPNFRI KRVTFTCSSN SSDDEMDSEN 

       250        260        270        280        290        300 
DYEAMVNRTV AENGLEIEFS DSSDSSLSAE YRSESEDHVT DSPAYVDLTE LEGGFNQFNS 

       310        320        330        340        350        360 
TSFQSTSPLG LEIVETEING SSTTADSKNS HSPYSKFSSA YPDAENSNIS KINISIAGNK 

       370        380        390        400        410        420 
ELYGNATQSD PSLYSTWIAN KHKTASSATV DSPLRRSLSV DAMQSNASFS SYSSTSNTDK 

       430        440        450        460        470        480 
SLRPSSYSAV SESSNFTHDV SRDNKEISLN APKSIIVSQS DSFDTSNVTQ DAPNDVEKEP 

       490        500        510        520        530        540 
ISGQMPNNLS VQSLKQLEVY PIRHSVSIEM PSEKLLSPRL YSSSTPSSPT KGFQKDDEED 

       550        560        570        580        590        600 
SENRKQADKV ELSPSSLLRQ MSLPVDSSSQ SDAQCTTSSV YITAERKAFS QSSIDLSTLS 

       610        620        630        640        650        660 
NHHVNNEINR RSFAGGFTSL ADELSEMREL LHESPAPLEC NEEMVIPTPE LDASSAIPSS 

       670        680        690        700        710        720 
SISHDEDLLP RKNTEESTSS SSFSSLITSP ASLQYDENPF KQSVVAELNN NSSSVPFVDS 

       730        740        750        760        770        780 
AHASDIHAYD NDHVSTKNKE FNRRLREFIL DPDSLSGLYW SVKSAGVRAS RRVSRNIEGE 

       790        800 
SVSSDLDDIF ANVLKGLSDE MASLLNTNR 

« 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"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: 15936270] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TEA1 AND WIN1.
[3]"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: 15809031] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FOR3; TEA1 AND TIP1, SUBCELLULAR LOCATION.
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-23; SER-24 AND TYR-28, MASS SPECTROMETRY.

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAA19002.1.
PIRT39626.
RefSeqNP_595240.1.

3D structure databases

HSSPHSSP built from PDB template 1N5Z based on UniProtKB P80667.
ModBaseSearch...

Protein-protein interaction databases

IntActO60132. 4 interactions.
STRINGO60132.

Genome annotation databases

GeneID2539642.
GenomeReviewsGene locus tea4 in contig CU329671_GR.
KEGGspo:SPBC1706.01.
NMPDRfig|4896.1.peg.1106.

Organism-specific databases

GeneDB_SpombeSPBC1706.01.

Phylogenomic databases

OrthoDBEOG93V1C5.

Gene expression databases

ArrayExpressO60132.

Family and domain databases

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

Entry information

Entry nameTEA4_SCHPO
AccessionPrimary (citable) accession number: O60132
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: August 1, 1998
Last modified: November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents