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UniProtKB/Swiss-Prot entry P17119


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KAR3_YEAST
Primary accession number P17119
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 94)
Name and origin of the protein
Protein name Kinesin-like protein KAR3
Synonym Nuclear fusion protein
Gene name
Name: KAR3
OrderedLocusNames: YPR141C
ORFNames: P9659.16
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=MY1124;
DOI=10.1016/0092-8674(90)90351-E; PubMed=2138512 [NCBI, ExPASy, EBI, Israel, Japan]
Meluh P.B., Rose M.D.;
"KAR3, a kinesin-related gene required for yeast nuclear fusion.";
Cell 60:1029-1041(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
MUTANTS KAR3.
PubMed=8224825 [NCBI, ExPASy, EBI, Israel, Japan]
Hoyt M.A., He L., Totis L., Saunders W.S.;
"Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1 is suppressed by KAR3 motor domain mutations.";
Genetics 135:35-44(1993).
[4]
CHARACTERIZATION.
PubMed=7912193 [NCBI, ExPASy, EBI, Israel, Japan]
Endow S.A., Kang S.J., Satterwhite L.L., Rose M.D., Skeen V.P., Salmon E.D.;
"Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends.";
EMBO J. 13:2708-2713(1994).
[5]
INTERACTION WITH CIK1 AND VIK1, AND SUBCELLULAR LOCATION.
DOI=10.1083/jcb.144.6.1219; PubMed=10087265 [NCBI, ExPASy, EBI, Israel, Japan]
Manning B.D., Barrett J.G., Wallace J.A., Granok H., Snyder M.;
"Differential regulation of the Kar3p kinesin-related protein by two associated proteins, Cik1p and Vik1p.";
J. Cell Biol. 144:1219-1233(1999).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11729143 [NCBI, ExPASy, EBI, Israel, Japan]
Shanks R.M.Q., Kamieniecki R.J., Dawson D.S.;
"The Kar3-interacting protein Cik1p plays a critical role in passage through meiosis I in Saccharomyces cerevisiae.";
Genetics 159:939-951(2001).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-21, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21 AND SER-68, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 383-729.
DOI=10.1021/bi972504o; PubMed=9485302 [NCBI, ExPASy, EBI, Israel, Japan]
Gulick A.M., Song H., Endow S.A., Rayment I.;
"X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg.ADP to 2.3-A resolution.";
Biochemistry 37:1769-1776(1998).
Comments
  • FUNCTION: Essential for yeast nuclear fusion during mating. KAR3 is a bifunctional protein having a kinesin-like motor domain joined to a distinct microtubule binding domain. It may mediate microtubule sliding during nuclear fusion and possibly mitosis. May interact with spindle microtubules to produce an inwardly directed force acting upon the poles. KAR3 function antagonizes CIP8 and KIP1 outward force action. KAR3 motor activity is directed toward the microtubule's minus end.
  • SUBUNIT: Interacts with CIK1 and VIK1.
  • INTERACTION:
    Q12045:VIK1; NbExp=3; IntAct=EBI-9499, EBI-38784;
  • SUBCELLULAR LOCATION: Nucleus, spindle pole body. Nucleus. Cytoplasm. Note=Cytoplasmic microtubules.
  • INDUCTION: By alpha factor.
  • MISCELLANEOUS: KAR3 contains two globular domains separated by an alpha-helical coiled coil. The N-terminal portion of KAR3 contains a microtubule association domain distinct from the kinesin-like C-terminal domain.
  • MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the kinesin-like protein family. NCD subfamily.
  • SIMILARITY: Contains 1 kinesin-motor domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31719; AAA34715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U40829; AAB68281.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34796; A34796.
RefSeq NP_015467.1; -.
3D structure databases
PDB
1F9T; X-ray; 1.50 A; A=373-729.[ExPASy / RCSB / EBI]
1F9U; X-ray; 1.70 A; A=384-729.[ExPASy / RCSB / EBI]
1F9V; X-ray; 1.30 A; A=384-729.[ExPASy / RCSB / EBI]
1F9W; X-ray; 2.50 A; A/B=384-729.[ExPASy / RCSB / EBI]
3KAR; X-ray; 2.30 A; A=385-729.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F9T; -.
1F9U; -.
1F9V; -.
1F9W; -.
3KAR; -.
ModBase P17119.
Protein-protein interaction databases
DIP DIP:75N; -.
IntAct P17119; -.
Organism-specific databases
CYGD YPR141c; -.
SGD S000006345; KAR3.
Yeast-GFP YPR141C.
Gene expression databases
ArrayExpress P17119; -.
GermOnline YPR141C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005874; Cellular component: microtubule (traceable author statement from SGD).
GO:0005816; Cellular component: spindle pole body (inferred from direct assay from SGD).
GO:0003777; Molecular function: microtubule motor activity (traceable author statement from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000742; Biological process: karyogamy during conjugation with cellular fusion (inferred from mutant phenotype from SGD).
GO:0007126; Biological process: meiosis (inferred from direct assay from SGD).
GO:0007064; Biological process: mitotic sister chromatid cohesion (inferred from genetic interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001752; Kinesin_motor.
Graphical view of domain structure.
Gene3D G3DSA:3.40.850.10; kinesin_motor; 1.
Pfam PF00225; Kinesin; 1.
Pfam graphical view of domain structure.
PRINTS PR00380; KINESINHEAVY.
SMART SM00129; KISc; 1.
SMART graphical view of domain structure.
PROSITE PS00411; KINESIN_MOTOR_DOMAIN1; 1.
PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P17119.
Proteomic databases
PeptideAtlas P17119; -.
Genome annotation databases
Ensembl YPR141C; Saccharomyces cerevisiae. [Contig view]
GeneID 856263; -.
GenomeReviews U00094_GR; YPR141C.
KEGG sce:YPR141C; -.
NMPDR fig|4932.3.peg.6606; -.
Phylogenomic databases
HOGENOM P17119; -.
Other
LinkHub P17119; -.
ProtoNet P17119.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Karyogamy; Microtubule; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   729  729     Kinesin-like protein KAR3. PRO_0000125391
DOMAIN   358   729  372     Kinesin-motor. 
NP_BIND   474   481  8     ATP (By similarity). 
REGION   1   109  109     Globular. 
COILED   110   357  248     Potential. 
MOD_RES   19    19        Phosphothreonine. 
MOD_RES   21    21        Phosphoserine. 
MOD_RES   68    68        Phosphoserine. 
MOD_RES   304   304        Phosphothreonine. 
VARIANT   378   378  1     N -> K (in KAR3-894). 
VARIANT   462   462  1     S -> L (in KAR3-891). 
VARIANT   521   521  1     E -> D (in KAR3-893). 
VARIANT   550   550  1     R -> S (in KAR3-899). 
VARIANT   558   558  1     T -> A (in KAR3-8912). 
VARIANT   650   650  1     N -> K (in KAR3-898). 
VARIANT   659   659  1     V -> L (in KAR3-897). 
MUTAGEN   479   479        G->E: Poisons nuclear fusion. 
STRAND   386   393  8      
TURN   398   400  3      
STRAND   406   410  5      
TURN   415   418  4      
STRAND   419   426  8      
HELIX   427   429  3      
STRAND   433   442  10      
HELIX   448   459  12      
HELIX   460   464  5      
STRAND   468   473  6      
HELIX   480   485  6      
TURN   487   489  3      
HELIX   491   506  16      
HELIX   507   509  3      
STRAND   512   523  12      
STRAND   526   529  4      
STRAND   549   552  4      
TURN   553   556  4      
STRAND   557   560  4      
HELIX   571   573  3      
HELIX   574   581  8      
HELIX   596   598  3      
STRAND   599   610  12      
STRAND   617   626  10      
HELIX   635   637  3      
HELIX   640   663  24      
HELIX   675   677  3      
HELIX   679   688  10      
STRAND   693   700  8      
HELIX   704   706  3      
HELIX   707   720  14      
TURN   723   725  3      
Sequence information
Length: 729 AA [This is the length of the unprocessed precursor] Molecular weight: 84004 Da [This is the MW of the unprocessed precursor] CRC64: BAEF98BC783ABDB9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESLPRTPTK GRSTQHLSTP SPKNDILAMN GHKRRNTTTP PPKHTLLKPQ RTDIHRHSLA 

        70         80         90        100        110        120 
SQSRISMSPN RELLKNYKGT ANLIYGNQKS NSGVTSFYKE NVNELNRTQA ILFEKKATLD 

       130        140        150        160        170        180 
LLKDELTETK EKINAVNLKF ETLREEKIKI EQQLNLKNNE LISIKEEFLS KKQFMNEGHE 

       190        200        210        220        230        240 
IHLKQLAASN KKELKQMENE YKTKIEKLKF MKIKQFENER ASLLDKIEEV RNKITMNPST 

       250        260        270        280        290        300 
LQEMLNDVEQ KHMLEKEEWL TEYQSQWKKD IELNNKHMQE IESIKKEIEN TLKPELAEKK 

       310        320        330        340        350        360 
KLLTEKRNAY EAIKVKVKEK EEETTRLRDE VALKQKTNLE TLEKIKELEE YIKDTELGMK 

       370        380        390        400        410        420 
ELNEILIKEE TVRRTLHNEL QELRGNIRVY CRIRPALKNL ENSDTSLINV NEFDDNSGVQ 

       430        440        450        460        470        480 
SMEVTKIQNT AQVHEFKFDK IFDQQDTNVD VFKEVGQLVQ SSLDGYNVCI FAYGQTGSGK 

       490        500        510        520        530        540 
TFTMLNPGDG IIPSTISHIF NWINKLKTKG WDYKVNCEFI EIYNENIVDL LRSDNNNKED 

       550        560        570        580        590        600 
TSIGLKHEIR HDQETKTTTI TNVTSCKLES EEMVEIILKK ANKLRSTAST ASNEHSSRSH 

       610        620        630        640        650        660 
SIFIIHLSGS NAKTGAHSYG TLNLVDLAGS ERINVSQVVG DRLRETQNIN KSLSCLGDVI 

       670        680        690        700        710        720 
HALGQPDSTK RHIPFRNSKL TYLLQYSLTG DSKTLMFVNI SPSSSHINET LNSLRFASKV 


NSTRLVSRK 

P17119 in FASTA format

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