KIP2_ASHGO
ID KIP2_ASHGO Reviewed; 685 AA.
AC Q8J1G1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Kinesin-like protein KIP2;
GN Name=KIP2; OrderedLocusNames=ACR145W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Alberti-Segui C., Dietrich F.S., Philippsen P.;
RT "Identification of kinesin-related proteins in the filamentous fungus
RT Ashbya gossypii.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Required for assembly of the mitotic spindle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AF378570; AAN87140.1; -; Genomic_DNA.
DR EMBL; AE016816; AAS51371.1; -; Genomic_DNA.
DR RefSeq; NP_983547.1; NM_208900.1.
DR AlphaFoldDB; Q8J1G1; -.
DR SMR; Q8J1G1; -.
DR STRING; 33169.AAS51371; -.
DR EnsemblFungi; AAS51371; AAS51371; AGOS_ACR145W.
DR GeneID; 4619679; -.
DR KEGG; ago:AGOS_ACR145W; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_24_1_1; -.
DR InParanoid; Q8J1G1; -.
DR OMA; LCTIHMG; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:1903754; C:cortical microtubule plus-end; IEA:EnsemblFungi.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IEA:EnsemblFungi.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0046785; P:microtubule polymerization; IEA:EnsemblFungi.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:EnsemblFungi.
DR GO; GO:0030473; P:nuclear migration along microtubule; IEA:EnsemblFungi.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..685
FT /note="Kinesin-like protein KIP2"
FT /id="PRO_0000125452"
FT DOMAIN 113..446
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 11..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 464..486
FT /evidence="ECO:0000255"
FT COILED 520..663
FT /evidence="ECO:0000255"
FT COMPBIAS 64..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 685 AA; 74696 MW; A627E5BA4E151DDF CRC64;
MMMVARVATA EHVGSAGASL PQTPGSRSFA LGAHPGPQKR IGGPAQGQTA FITPLVTPDG
IYSRPSSPYM QASPLLKGSE SGGSAGSPQS PDAPSSASGA SVGNAIGSGY TGNVSVAIRI
KPSESSTKDP WYASNDRLIH TEFGEFQFDH VFTKGVCNQE VYQALGVPII DKLFEGYNAT
IFAYGMTGSG KTFTMSGNKQ EPGLIPQCVG NIFDRISSEH HGASLAYEVK VSYLEIYNEK
IYDLLNYVDR QAGSTGQPSR NATGLKIRDD SKYGVKVVDL TEQLVSSHED VMKWIATGDR
NRKTGETDFN TRSSRSHAIV LLRLTRYDLK TGSEATSTLS LCDLAGSERA VTQIVRRKEG
AFINKSLLAL GTVIAKLSML GSQANGLQPS PAAGHIPYRD SKLTRILQPA LTGDSIITTI
CTIDSKAESS TETTNTVRFA SRAKNIALNV RKNEMDSHAE KDTIIQNLRK QLDEQHETIV
MLRRSAAAPS GNGSTSPLDS PGVGGTSLSE RTHNMEKGLL EVENSILKTK LEHCEKLLDK
DMMVLEDPHV REIVEMLPLD IASVLESKVQ GMESQLRQYR VYVQKLESDL LKAQRNIITT
HSVQFNRQST ANVQEKYGSD VDIELLLEEQ EAELMELRNA LKRKDKMIEA LQSARRLRDS
ALSPTTTVLL QRKESVIDPR DPQPV
