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Q9P6L5 (SLA2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endocytosis protein end4
Alternative name(s):
SLA2 protein homolog
Gene names
Name:end4
Synonyms:sla2
ORF Names:SPAC688.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1102 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cellular morphogenesis and polarization of the cortical cytoskeleton. Required for establishment of new polarized growth zones where it acts in actin organization. Involved plasma membrane internalization and is essential for fluid-phase endocytosis. Ref.4 Ref.5

Subcellular location

Cytoplasmcytoskeleton. Note: Localizes at cell ends during interphase and to the medial ring at cell division. Ref.5

Sequence similarities

Belongs to the SLA2 family.

Contains 1 ENTH (epsin N-terminal homology) domain.

Contains 1 I/LWEQ domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasm
Cytoskeleton
   DomainCoiled coil
   LigandActin-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1 to G0 transition

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

actin cytoskeleton organization

Inferred from mutant phenotype Ref.4. Source: PomBase

activation of bipolar cell growth

Inferred from mutant phenotype Ref.5. Source: PomBase

cellular protein localization

Inferred from mutant phenotype PubMed 15975911. Source: PomBase

cellular response to nitrogen starvation

Inferred from mutant phenotype PubMed 19366728. Source: PomBase

cortical actin cytoskeleton organization

Inferred from mutant phenotype Ref.5. Source: PomBase

endocytosis

Inferred from mutant phenotype Ref.4PubMed 21652630. Source: PomBase

establishment or maintenance of actin cytoskeleton polarity

Inferred from mutant phenotype Ref.5. Source: PomBase

fungal-type cell wall organization or biogenesis

Inferred from mutant phenotype PubMed 15975911. Source: PomBase

membrane raft distribution

Inferred from mutant phenotype PubMed 18346214. Source: PomBase

   Cellular_componentactin cortical patch

Inferred from direct assay Ref.5. Source: PomBase

cell cortex of cell tip

Inferred from direct assay Ref.5. Source: PomBase

cell division site

Inferred from direct assay Ref.5PubMed 15975911. Source: PomBase

cytoplasm

Inferred from direct assay PubMed 16823372. Source: PomBase

   Molecular_functionphosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence model. Source: PomBase

protein binding, bridging

Inferred from sequence or structural similarity. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11021102Endocytosis protein end4
PRO_0000071944

Regions

Domain9 – 139131ENTH
Domain858 – 1100243I/LWEQ
Coiled coil338 – 661324 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9P6L5 [UniParc].

Last modified April 18, 2012. Version 2.
Checksum: 9101E230871A5DD0

FASTA1,102124,373
        10         20         30         40         50         60 
MSSFRLQSDH MQSDASLMTS VRKATSIDET APKRKHVRSC IIFTWDHHTA RPFWTAIKVQ 

        70         80         90        100        110        120 
PLLANEVQTF KALITIHRVL QEGHKSALVD SQSEKGWLKT CERQYDGESS PKGYSDLIRD 

       130        140        150        160        170        180 
YVDYLLDKLS FHAQHPEFNG TFEYKEYISL RQVDDPNEGY ETVYDMMNLQ DHIDEFQKQL 

       190        200        210        220        230        240 
FSNFKRSNKN ECRIAALVPL VQESYGIYRF LTSMLRALYS TVDAPETLEP LKHRYKSQHH 

       250        260        270        280        290        300 
RLRQFYADCS NLRYLTSLIS VPRLPHDPPD LEGDDNIPDL PKRPASIAPQ PTGASTIAPQ 

       310        320        330        340        350        360 
PTGTSPSPPV EMNFPDTSDI TPAYSEPEPI QDFWSDPTLD QQLAAQQAAQ QAAQQQAELA 

       370        380        390        400        410        420 
AQQAAAQQAQ LAAQQAAEME RQRMAAQQHQ QALEAIQMAQ AEQQRIAQEQ LAQQQFQMQT 

       430        440        450        460        470        480 
QGQLAELEQQ LLATRGQLEQ SNVLLNQYDA RVRTLENELS QAGVNLQEQI HQNDDLIESL 

       490        500        510        520        530        540 
KNQILTWKNK YEALAKLYTQ LRQEHLDLLS KYKQIQLKAS SAQEAIDKKE KMEREMKNKN 

       550        560        570        580        590        600 
LELADMILER DRARHELETM HRSQRDKQES TERELRLLQE KAASLERNKS SEVSNLLSRY 

       610        620        630        640        650        660 
NTEVAHLEDA LHSKDRELAN LGVELKSTEN RYRQLLQEKE EELEIQKAAV DESLLQLSKL 

       670        680        690        700        710        720 
QLDRNDIDQA MDTQIDELLK SQLEKLDDIV DSVLATGIQR LDTSLYELDS PMHAGNQYAT 

       730        740        750        760        770        780 
PEFILSTIEN ASNNATDFST AFNNYFADGP NADHSEVING VNLFSTAIYE VANNAKGLSR 

       790        800        810        820        830        840 
TTGDDQGSDR FVGLSRDLVN MAKRFLSSLF SVNTRKMDVN VKTDLVIGEN IELQRYLQQL 

       850        860        870        880        890        900 
TQYSEKFLNK ESENTVGLLN APGENIEELV DNQLAETAQA IQQAILRLQN IAAKPKDDSL 

       910        920        930        940        950        960 
SPSELQVHDS LLSASIAITE AIARLIKAAT ASQAEIVAQG RGSSSRGAFY KKHNRWTEGL 

       970        980        990       1000       1010       1020 
ISAAKAVARA TTTLIETADG VVNGTSSFEH LIVACNGVSA ATAQLVAASR VKANFASKVQ 

      1030       1040       1050       1060       1070       1080 
DHLEDAAKAV TEACKALVRQ VESVALKAKE VQHEDFSSLG VHEYRRKEIE QQVQILKLEN 

      1090       1100 
DLVAARRRLF DMRKTSYHVA EE 

« 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]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1102.
Strain: PR745.
[4]"Characterization of end4+, a gene required for endocytosis in Schizosaccharomyces pombe."
Iwaki T., Tanaka N., Takagi H., Giga-Hama Y., Takegawa K.
Yeast 21:867-881(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"End4/Sla2 is involved in establishment of a new growth zone in Schizosaccharomyces pombe."
Castagnetti S., Behrens R., Nurse P.
J. Cell Sci. 118:1843-1850(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Augmented annotation of the Schizosaccharomyces pombe genome reveals additional genes required for growth and viability."
Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L., Hagan I.M., Miller C.J.
Genetics 187:1207-1217(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVISION OF GENE MODEL, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB90777.2.
D89267 mRNA. Translation: BAA13928.1.
PIRT43195.
RefSeqNP_594069.2. NM_001019493.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279759. 9 interactions.
MINTMINT-4704247.
STRING4896.SPAC688.11-1.

Proteomic databases

PaxDbQ9P6L5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC688.11.1; SPAC688.11.1:pep; SPAC688.11.
GeneID2543336.
KEGGspo:SPAC688.11.

Organism-specific databases

PomBaseSPAC688.11.

Phylogenomic databases

eggNOGNOG280957.
HOGENOMHOG000193921.
OrthoDBEOG7G1VG0.

Family and domain databases

Gene3D1.20.1410.10. 1 hit.
1.25.40.90. 1 hit.
InterProIPR011417. ANTH_dom.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
IPR002558. ILWEQ_dom.
[Graphical view]
PfamPF07651. ANTH. 1 hit.
PF01608. I_LWEQ. 1 hit.
[Graphical view]
ProDomPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00273. ENTH. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMSSF109885. SSF109885. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804352.

Entry information

Entry nameSLA2_SCHPO
AccessionPrimary (citable) accession number: Q9P6L5
Secondary accession number(s): P78916
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: April 18, 2012
Last modified: April 16, 2014
This is version 99 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