KIP1_ASHGO
ID KIP1_ASHGO Reviewed; 1129 AA.
AC Q8J1G4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Kinesin-like protein KIP1;
GN Name=KIP1; OrderedLocusNames=ACR228C;
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. Interacts with
CC spindle microtubules to produce an outwardly directed force acting upon
CC the poles. Following spindle assembly, CIN8 and KIP1 apparently act to
CC oppose a force that draws separated poles back together. This force
CC seems to be mediate by KAR3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Spindle microtubules that lie between the poles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; AF378569; AAN87137.1; -; Genomic_DNA.
DR EMBL; AE016816; AAS51454.1; -; Genomic_DNA.
DR RefSeq; NP_983630.1; NM_208983.1.
DR AlphaFoldDB; Q8J1G4; -.
DR SMR; Q8J1G4; -.
DR STRING; 33169.AAS51454; -.
DR EnsemblFungi; AAS51454; AAS51454; AGOS_ACR228C.
DR GeneID; 4619762; -.
DR KEGG; ago:AGOS_ACR228C; -.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_2_1; -.
DR InParanoid; Q8J1G4; -.
DR OMA; GMEEMYI; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030543; P:2-micrometer plasmid partitioning; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IBA:GO_Central.
DR GO; GO:0007019; P:microtubule depolymerization; IEA:EnsemblFungi.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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 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..1129
FT /note="Kinesin-like protein KIP1"
FT /id="PRO_0000125368"
FT DOMAIN 54..417
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..513
FT /evidence="ECO:0000255"
FT COILED 681..765
FT /evidence="ECO:0000255"
FT COILED 919..948
FT /evidence="ECO:0000255"
FT COMPBIAS 14..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1129 AA; 127690 MW; CFC5B31F932C7059 CRC64;
MLEQAEKLMK RNSSGAMSAP QSKPLARSRS STMPTTTQKR VRSSQQSEGE PEYNIKVYVR
CRSRNEREIR EKSSVVISTL GNNGREVILT NPGTGSNKTY TFDRVFGVES DQESMFNQVA
RAYINEMIEG YNCTVFAYGQ TGTGKTYTMS GDITMMGSSE DDPNFVLLSE HAGIIPRVLV
ELFRELREVS EDYSVKVSFL ELYNEKLRDL LVDDKDVSLE DHNFNGMAPP ESIRIYDSLK
TDRTSPNGYS IFVKGMEEMY IRSAQEGLKL LMDGSLKRKV AATKCNDLSS RSHTIFTITT
NVTKIHPISG EQYVKVGKLN LVDLAGSENI NRSGAENKRA QEAGLINKSL LTLGRVINAL
VDHSQHIPYR ESKLTRLLQD SLGGKTKTCI IATISPAKIS MEETVSTLEY ATRAKSIKNT
PQVNQLMAKE SCIIEYIQEI ERLRKELRAS HSKEGIYITQ EKFETYESNS ILVEEQQAKI
DNLQEQLRRL KEKFLEQTKL IKEKDGQIKE LDVANRKYLE QSKDLTIYIN GIHSKLEDYE
HTMIGIHNNN MKLLEDINDN RGNIHEDLLA KVDHIETCNL IISREITSLI SIRNVLQAYS
DRFKTVLGGV FEELQEKLTQ VGRTTEESQL DVDLSFVDEK FEEVTDIIKA TCENLVRTMD
EHVSNMKLET TDLTSSCASL LEKECQALHG KLQKYVESMK QELNSTLQEM VRDLDMKASS
MLNVVQCTKD GLISHKKELE ADLESQKREH FDIAQTMEEQ LQKIVGKERQ NIQESMKASY
DFLMKQMVET ELRQKNFEES IVSKVKGLLS HSNNGMSKMS SYAVGRLYDS AIGGVNSIEN
TVSSATFSMK NDLQEFQMDI SPICDSRRFG DEFTAVETRI SEAIREELTP KLQDITSKAC
NLIGLGVQDI NQKALGVSDD QRRELRSVIN NTNNHADRLR SEIGTLVNYV SQEHRDNIMQ
ISQTQDEILQ EQIASIGRTF DVLGNINKPD ANVRTSVPIE HELNSAINEL PPLYMPQRPL
SLCSHGRQLL DEAYSGNENL SPSTGKFSNF PTPCGDMSAQ TPTTPMPVPD QPLTKMPVPQ
TISSLRSLRR LTMDICEHSA DMTLGSIHES QKAMDSSRRY TLEPRLFEK
