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Reviewed, UniProtKB/Swiss-Prot Q10197 (ALP1_SCHPO)

Last modified November 24, 2009. Version 66. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tubulin-folding cofactor D
Alternative name(s):
    Altered polarity protein 1
Gene names
Name: alp1
ORF Names: SPBC11C11.04c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has a function in the folding of beta-tubulin. Microtubule-associated protein that is essential to direct polarized cell growth and to position the nucleus and septum to the center of the cell during mitosis. Ref.1

Subunit structure

Interacts with alp21. Ref.3

Subcellular location

Cytoplasmcytoskeleton. Note: Microtubule-associated. Ref.1

Sequence similarities

Contains 1 HEAT repeat.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Molecular functionChaperone
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processestablishment or maintenance of cell polarity Ref.1

Inferred from mutant phenotype. Source: GeneDB_SPombe

microtubule cytoskeleton organization Ref.1

Inferred from genetic interaction. Source: GeneDB_SPombe

protein folding Ref.1

Traceable author statement. Source: GeneDB_SPombe

   Cellular componentastral microtubule Ref.1

Inferred from direct assay. Source: GeneDB_SPombe

cell division site

Inferred from direct assay. Source: GeneDB_SPombe

cytosol

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionprotein binding Ref.3

Inferred from physical interaction. Source: GeneDB_SPombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11211121Tubulin-folding cofactor D
PRO_0000064568

Regions

Repeat313 – 35139HEAT

Amino acid modifications

Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation8851N-linked (GlcNAc...) Potential
Glycosylation10991N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict988 – 100114Missing in CAA20686. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q10197-1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: DCF045E3B81213A2

FASTA1,121128,187
        10         20         30         40         50         60 
MEEEESLEGI ISIDESLITS RLSQILDDVL DDRSSSHSVE KLKDVAVKYL QFCQFQPTLL 

        70         80         90        100        110        120 
DKLLSKYVPN LASYLLKVKN IGKCNSITVI LYQFCKIRGY KAVRVLFPVG VQYIKELYTL 

       130        140        150        160        170        180 
LNESSNNTWH FHYIVLLWLS QALNTPFPLN SLDDSLDVKK TIYTIAIKYL ENSGIDKEAS 

       190        200        210        220        230        240 
CLVLSRLFSR DDGLDLLLGF LHHCESSWFK RSIFYKIGCL FSLSSFLKIC PRNDCLQTVD 

       250        260        270        280        290        300 
VAFQFLNVAR EDLVGQENSA LRKLLCKCYT RLGIVLLPVN SSPNWKYSIS NPDSFFQLPD 

       310        320        330        340        350        360 
DSNEEVHIYL EVIVDFLLSS VSDIDSFVRW SAAKGLAKII SRLPWNLAEQ VIDAIIELMT 

       370        380        390        400        410        420 
ENMFLNPIEN TVNISITSPL VWHGAILFFA KLAGAGLIKY SKCLHILPLI EVGLSYEVRY 

       430        440        450        460        470        480 
GTRVTGQSIR DASCYFVWSF YHCYSKSAIE GLQTNLILCL LQTVLFDNEI NVRRAATAAL 

       490        500        510        520        530        540 
FEVIGRHASI PDGLSLISHI NYVSVTDISN CYGDLCMKVA HFPQFRSCVF QRLFTNLQHW 

       550        560        570        580        590        600 
DVKVQQLSAF SLRQLSIKYP KELSIYLPPI LDYLSVGNAD FIFGYTIGLA SIIGGFLSIS 

       610        620        630        640        650        660 
FPFDINRIHD LLSHKNLLSL KKFSRQQQTK IILGILKGIQ QIFANDIRVD RAFFSEAFSV 

       670        680        690        700        710        720 
IIAAIDLQEE TIIKDISDAY SVLVKFDDME ETLEVLLDYI RKCSTSKEAR IVYIILQNLP 

       730        740        750        760        770        780 
NISFRYQKKI CKLLLDIYPQ LHSIDYQAPV ANALQNIIPF TYEKTESIEE FVKELLQVCS 

       790        800        810        820        830        840 
NYLTDTRGDV GSWIRKPAMK AISSLLVKDS SGKKLSEDIV WCCISYIIRQ TFDKIDSLRG 

       850        860        870        880        890        900 
LAYQALEQIR VHYLIRRCEA LTNIINRISF RNNPNMDGEV LNELNISLLE IPNLRLQAFY 

       910        920        930        940        950        960 
GITVFTADGF GSDLAVKCFE FYLSYVYQLE DSFKKSNSRY GKRDLLQLYI DILSSEDEIA 

       970        980        990       1000       1010       1020 
RFYFPIMKSF TSLLAYGCFT DFQNVKGYVF LHFVQNTNDI SMSKAIFIVQ RRALTCKSPG 

      1030       1040       1050       1060       1070       1080 
GLSAILELYR TLFLSKNELL RHHALKYTAN LLLNPIEKVR YQAADTLLYA KSIGLLTFLP 

      1090       1100       1110       1120 
NELNQKLLTL DWFVPVSQNA TFVKQLRNII QKQIDKLIAD R 

« Hide

References

« Hide 'large scale' references
[1]"Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast."
Hirata D., Masuda H., Eddison M., Toda T.
EMBO J. 17:658-666(1998) [PubMed: 9450991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: 972 / HM123.
[2]"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.
[3]"Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast."
Radcliffe P.A., Hirata D., Vardy L., Toda T.
Mol. Biol. Cell 10:2987-3001(1999) [PubMed: 10473641] [Abstract]
Cited for: INTERACTION WITH ALP21.

Cross-references

Sequence databases

Y10106 Genomic DNA. Translation: CAA71193.1.
CU329671 Genomic DNA. Translation: CAA20686.1.
PIRS67381. T39319.
RefSeqNP_596393.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ10197.

Genome annotation databases

GeneID2539669.
GenomeReviewsGene locus alp1 in contig CU329671_GR.
KEGGspo:SPBC11C11.04c.

Organism-specific databases

GeneDB_SpombeSPBC11C11.04c.

Phylogenomic databases

OrthoDBEOG9Z6454

Gene expression databases

ArrayExpressQ10197.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR000357. HEAT.
[Graphical view]
PfamPF02985. HEAT. 1 hit.
[Graphical view]
PROSITEPS50077. HEAT_REPEAT. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALP1_SCHPO
AccessionPrimary (citable) accession number: Q10197
Secondary accession number(s): P78749
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: November 24, 2009
This is version 66 of the entry and version 2 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents