KAR3_YEAST
ID KAR3_YEAST Reviewed; 729 AA.
AC P17119; D6W4D9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Kinesin-like protein KAR3;
DE AltName: Full=Nuclear fusion protein;
GN Name=KAR3; OrderedLocusNames=YPR141C; ORFNames=P9659.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=MY1124;
RX PubMed=2138512; DOI=10.1016/0092-8674(90)90351-e;
RA Meluh P.B., Rose M.D.;
RT "KAR3, a kinesin-related gene required for yeast nuclear fusion.";
RL Cell 60:1029-1041(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP MUTANTS KAR3.
RX PubMed=8224825; DOI=10.1093/genetics/135.1.35;
RA Hoyt M.A., He L., Totis L., Saunders W.S.;
RT "Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1
RT is suppressed by KAR3 motor domain mutations.";
RL Genetics 135:35-44(1993).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7912193; DOI=10.1002/j.1460-2075.1994.tb06561.x;
RA Endow S.A., Kang S.J., Satterwhite L.L., Rose M.D., Skeen V.P.,
RA Salmon E.D.;
RT "Yeast Kar3 is a minus-end microtubule motor protein that destabilizes
RT microtubules preferentially at the minus ends.";
RL EMBO J. 13:2708-2713(1994).
RN [6]
RP INTERACTION WITH CIK1 AND VIK1, AND SUBCELLULAR LOCATION.
RX PubMed=10087265; DOI=10.1083/jcb.144.6.1219;
RA Manning B.D., Barrett J.G., Wallace J.A., Granok H., Snyder M.;
RT "Differential regulation of the Kar3p kinesin-related protein by two
RT associated proteins, Cik1p and Vik1p.";
RL J. Cell Biol. 144:1219-1233(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11729143; DOI=10.1093/genetics/159.3.939;
RA Shanks R.M.Q., Kamieniecki R.J., Dawson D.S.;
RT "The Kar3-interacting protein Cik1p plays a critical role in passage
RT through meiosis I in Saccharomyces cerevisiae.";
RL Genetics 159:939-951(2001).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 383-729.
RX PubMed=9485302; DOI=10.1021/bi972504o;
RA Gulick A.M., Song H., Endow S.A., Rayment I.;
RT "X-ray crystal structure of the yeast Kar3 motor domain complexed with
RT Mg.ADP to 2.3-A resolution.";
RL Biochemistry 37:1769-1776(1998).
CC -!- FUNCTION: Essential for yeast nuclear fusion during mating. KAR3 is a
CC bifunctional protein having a kinesin-like motor domain joined to a
CC distinct microtubule binding domain. It may mediate microtubule sliding
CC during nuclear fusion and possibly mitosis. May interact with spindle
CC microtubules to produce an inwardly directed force acting upon the
CC poles. KAR3 function antagonizes CIP8 and KIP1 outward force action.
CC KAR3 motor activity is directed toward the microtubule's minus end.
CC {ECO:0000269|PubMed:11729143, ECO:0000269|PubMed:2138512}.
CC -!- SUBUNIT: Interacts with CIK1 and VIK1. {ECO:0000269|PubMed:10087265}.
CC -!- INTERACTION:
CC P17119; P32908: SMC1; NbExp=4; IntAct=EBI-9499, EBI-17402;
CC P17119; Q12045: VIK1; NbExp=4; IntAct=EBI-9499, EBI-38784;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Nucleus. Cytoplasm, cytoskeleton.
CC Note=Cytoplasmic microtubules.
CC -!- INDUCTION: By alpha factor.
CC -!- MISCELLANEOUS: KAR3 contains two globular domains separated by an
CC alpha-helical coiled coil. The N-terminal portion of KAR3 contains a
CC microtubule association domain distinct from the kinesin-like C-
CC terminal domain.
CC -!- MISCELLANEOUS: Present with 3250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; M31719; AAA34715.1; -; mRNA.
DR EMBL; U40829; AAB68281.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11555.1; -; Genomic_DNA.
DR PIR; A34796; A34796.
DR RefSeq; NP_015467.1; NM_001184238.1.
DR PDB; 1F9T; X-ray; 1.50 A; A=372-729.
DR PDB; 1F9U; X-ray; 1.70 A; A=383-729.
DR PDB; 1F9V; X-ray; 1.30 A; A=383-729.
DR PDB; 1F9W; X-ray; 2.50 A; A/B=383-729.
DR PDB; 3KAR; X-ray; 2.30 A; A=385-729.
DR PDB; 4ETP; X-ray; 2.30 A; A=348-729.
DR PDBsum; 1F9T; -.
DR PDBsum; 1F9U; -.
DR PDBsum; 1F9V; -.
DR PDBsum; 1F9W; -.
DR PDBsum; 3KAR; -.
DR PDBsum; 4ETP; -.
DR AlphaFoldDB; P17119; -.
DR SMR; P17119; -.
DR BioGRID; 36310; 636.
DR DIP; DIP-75N; -.
DR IntAct; P17119; 8.
DR MINT; P17119; -.
DR STRING; 4932.YPR141C; -.
DR iPTMnet; P17119; -.
DR MaxQB; P17119; -.
DR PaxDb; P17119; -.
DR PRIDE; P17119; -.
DR EnsemblFungi; YPR141C_mRNA; YPR141C; YPR141C.
DR GeneID; 856263; -.
DR KEGG; sce:YPR141C; -.
DR SGD; S000006345; KAR3.
DR VEuPathDB; FungiDB:YPR141C; -.
DR eggNOG; KOG0239; Eukaryota.
DR GeneTree; ENSGT00940000154022; -.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; P17119; -.
DR OMA; THFYREN; -.
DR BioCyc; YEAST:G3O-34276-MON; -.
DR BRENDA; 5.6.1.4; 984.
DR EvolutionaryTrace; P17119; -.
DR PRO; PR:P17119; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P17119; protein.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR GO; GO:0005874; C:microtubule; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000922; C:spindle pole; HDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:SGD.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Karyogamy; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..729
FT /note="Kinesin-like protein KAR3"
FT /id="PRO_0000125391"
FT DOMAIN 386..723
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..109
FT /note="Globular"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..357
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VARIANT 378
FT /note="N -> K (in KAR3-894)"
FT VARIANT 462
FT /note="S -> L (in KAR3-891)"
FT VARIANT 521
FT /note="E -> D (in KAR3-893)"
FT VARIANT 550
FT /note="R -> S (in KAR3-899)"
FT VARIANT 558
FT /note="T -> A (in KAR3-8912)"
FT VARIANT 650
FT /note="N -> K (in KAR3-898)"
FT VARIANT 659
FT /note="V -> L (in KAR3-897)"
FT MUTAGEN 479
FT /note="G->E: Poisons nuclear fusion."
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:4ETP"
FT HELIX 340..384
FT /evidence="ECO:0007829|PDB:4ETP"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 415..418
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 433..442
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 448..459
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 480..485
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 491..506
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 512..523
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:3KAR"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 599..610
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:1F9U"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 640..663
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 668..670
FT /evidence="ECO:0007829|PDB:4ETP"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 679..688
FT /evidence="ECO:0007829|PDB:1F9V"
FT STRAND 693..700
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:1F9V"
FT HELIX 707..720
FT /evidence="ECO:0007829|PDB:1F9V"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:1F9V"
SQ SEQUENCE 729 AA; 84004 MW; BAEF98BC783ABDB9 CRC64;
MESLPRTPTK GRSTQHLSTP SPKNDILAMN GHKRRNTTTP PPKHTLLKPQ RTDIHRHSLA
SQSRISMSPN RELLKNYKGT ANLIYGNQKS NSGVTSFYKE NVNELNRTQA ILFEKKATLD
LLKDELTETK EKINAVNLKF ETLREEKIKI EQQLNLKNNE LISIKEEFLS KKQFMNEGHE
IHLKQLAASN KKELKQMENE YKTKIEKLKF MKIKQFENER ASLLDKIEEV RNKITMNPST
LQEMLNDVEQ KHMLEKEEWL TEYQSQWKKD IELNNKHMQE IESIKKEIEN TLKPELAEKK
KLLTEKRNAY EAIKVKVKEK EEETTRLRDE VALKQKTNLE TLEKIKELEE YIKDTELGMK
ELNEILIKEE TVRRTLHNEL QELRGNIRVY CRIRPALKNL ENSDTSLINV NEFDDNSGVQ
SMEVTKIQNT AQVHEFKFDK IFDQQDTNVD VFKEVGQLVQ SSLDGYNVCI FAYGQTGSGK
TFTMLNPGDG IIPSTISHIF NWINKLKTKG WDYKVNCEFI EIYNENIVDL LRSDNNNKED
TSIGLKHEIR HDQETKTTTI TNVTSCKLES EEMVEIILKK ANKLRSTAST ASNEHSSRSH
SIFIIHLSGS NAKTGAHSYG TLNLVDLAGS ERINVSQVVG DRLRETQNIN KSLSCLGDVI
HALGQPDSTK RHIPFRNSKL TYLLQYSLTG DSKTLMFVNI SPSSSHINET LNSLRFASKV
NSTRLVSRK
