Reviewed, UniProtKB/Swiss-Prot P17119 (KAR3_YEAST)

Names and origin

Protein names

Recommended name:
    Kinesin-like protein KAR3
Alternative name(s):
    Nuclear fusion protein

Gene names

Name:	KAR3
Ordered Locus Names:	YPR141C
ORF Names:	P9659.16

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1 Ref.6
Subunit structure	Interacts with CIK1 and VIK1. Ref.5
Subcellular location	Nucleus › spindle pole body. Nucleus. Cytoplasm. Note: Cytoplasmic microtubules. Ref.6 Ref.5
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. Present with 3250 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the kinesin-like protein family. NCD subfamily. Contains 1 kinesin-motor domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Karyogamy
Cellular component	Cytoplasm Microtubule Nucleus
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Ref.6 Inferred from direct assay. Source: SGD mitotic sister chromatid cohesion Inferred from genetic interaction. Source: SGD nuclear migration during conjugation with cellular fusion Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasmic microtubule Ref.1 Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole body Ref.1 Ref.6 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Traceable author statement. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VIK1	Q12045	3	EBI-9499,EBI-38784

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 729

729

Kinesin-like protein KAR3

PRO_0000125391

Regions

Domain

358 – 729

372

Kinesin-motor

Nucleotide binding

474 – 481

8

ATP By similarity

Region

1 – 109

109

Globular

Coiled coil

110 – 357

248

Potential

Amino acid modifications

Modified residue

19

1

Phosphothreonine Ref.9 Ref.10

Modified residue

21

1

Phosphoserine Ref.9 Ref.10

Modified residue

68

1

Phosphoserine Ref.10

Modified residue

304

1

Phosphothreonine Ref.8

Natural variations

Natural variant

378

1

N → K in KAR3-894.

Natural variant

462

1

S → L in KAR3-891.

Natural variant

521

1

E → D in KAR3-893.

Natural variant

550

1

R → S in KAR3-899.

Natural variant

558

1

T → A in KAR3-8912.

Natural variant

650

1

N → K in KAR3-898.

Natural variant

659

1

V → L in KAR3-897.

Experimental info

Mutagenesis

479

1

G → E: Poisons nuclear fusion.

Secondary structure

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729

Helix Strand Turn

Details...

Beta strand

386 – 393

8

Turn

398 – 400

3

Beta strand

406 – 410

5

Turn

415 – 418

4

Beta strand

419 – 426

8

Helix

427 – 429

3

Beta strand

433 – 442

10

Helix

448 – 459

12

Helix

460 – 464

5

Beta strand

468 – 473

6

Helix

480 – 485

6

Turn

487 – 489

3

Helix

491 – 506

16

Helix

507 – 509

3

Beta strand

512 – 523

12

Beta strand

526 – 529

4

Beta strand

549 – 552

4

Turn

553 – 556

4

Beta strand

557 – 560

4

Helix

571 – 573

3

Helix

574 – 581

8

Helix

596 – 598

3

Beta strand

599 – 610

12

Beta strand

617 – 626

10

Helix

635 – 637

3

Helix

640 – 663

24

Helix

675 – 677

3

Helix

679 – 688

10

Beta strand

693 – 700

8

Helix

704 – 706

3

Helix

707 – 720

14

Turn

723 – 725

3

Sequences

	Sequence		Length	Mass (Da)
	P17119-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: BAEF98BC783ABDB9	FASTA	729	84,004
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"KAR3, a kinesin-related gene required for yeast nuclear fusion." Meluh P.B., Rose M.D. Cell 60:1029-1041(1990) [PubMed: 2138512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: MY1124.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." 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. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1 is suppressed by KAR3 motor domain mutations." Hoyt M.A., He L., Totis L., Saunders W.S. Genetics 135:35-44(1993) [PubMed: 8224825] [Abstract] Cited for: MUTANTS KAR3.
[4]	"Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends." Endow S.A., Kang S.J., Satterwhite L.L., Rose M.D., Skeen V.P., Salmon E.D. EMBO J. 13:2708-2713(1994) [PubMed: 7912193] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Differential regulation of the Kar3p kinesin-related protein by two associated proteins, Cik1p and Vik1p." Manning B.D., Barrett J.G., Wallace J.A., Granok H., Snyder M. J. Cell Biol. 144:1219-1233(1999) [PubMed: 10087265] [Abstract] Cited for: INTERACTION WITH CIK1 AND VIK1, SUBCELLULAR LOCATION.
[6]	"The Kar3-interacting protein Cik1p plays a critical role in passage through meiosis I in Saccharomyces cerevisiae." Shanks R.M.Q., Kamieniecki R.J., Dawson D.S. Genetics 159:939-951(2001) [PubMed: 11729143] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-304, MASS SPECTROMETRY.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-21, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21 AND SER-68, MASS SPECTROMETRY.
[11]	"X-ray crystal structure of the yeast Kar3 motor domain complexed with Mg.ADP to 2.3-A resolution." Gulick A.M., Song H., Endow S.A., Rayment I. Biochemistry 37:1769-1776(1998) [PubMed: 9485302] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 383-729.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M31719 mRNA. Translation: AAA34715.1.
U40829 Genomic DNA. Translation: AAB68281.1.

PIR

A34796.

RefSeq

NP_015467.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F9T	X-ray	1.50	A	373-729	[»]
1F9U	X-ray	1.70	A	384-729	[»]
1F9V	X-ray	1.30	A	384-729	[»]
1F9W	X-ray	2.50	A/B	384-729	[»]
3KAR	X-ray	2.30	A	385-729	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:75N.

IntAct

P17119. 9 interactions.

Proteomic databases

PeptideAtlas

P17119.

Genome annotation databases

Ensembl

YPR141C. Saccharomyces cerevisiae. [Contig view]

GeneID

856263.

GenomeReviews

Gene locus YPR141C in contig U00094_GR.

KEGG

sce:YPR141C.

NMPDR

fig|4932.3.peg.6606.

Organism-specific databases

CYGD

YPR141c.

SGD

S000006345. KAR3.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P17119.

OMA

P17119. FASKVNS.

Gene expression databases

ArrayExpress

P17119.

GermOnline

YPR141C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001752. Kinesin_motor.
IPR019821. Kinesin_motor_CS.
[Graphical view]

Gene3D

G3DSA:3.40.850.10. kinesin_motor. 1 hit.

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

981560.

Entry information

Entry name

KAR3_YEAST

Accession

Primary (citable) accession number: P17119

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)