(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 96.
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. Interact 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}.
DR   EMBL; AF378569; AAN87137.1; -; Genomic_DNA.
DR   EMBL; AE016816; AAS51454.1; -; Genomic_DNA.
DR   RefSeq; NP_983630.1; NM_208983.1.
DR   SMR; Q8J1G4; -.
DR   STRING; 33169.AAS51454; -.
DR   PRIDE; Q8J1G4; -.
DR   EnsemblFungi; AAS51454; AAS51454; AGOS_ACR228C.
DR   GeneID; 4619762; -.
DR   KEGG; ago:AGOS_ACR228C; -.
DR   HOGENOM; HOG000113228; -.
DR   InParanoid; Q8J1G4; -.
DR   KO; K10398; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; 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:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase 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: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; IEA:EnsemblFungi.
DR   GO; GO:0007019; P:microtubule depolymerization; IEA:EnsemblFungi.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
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;
DR   PRODOM; Q8J1G4.
DR   SWISS-2DPAGE; Q8J1G4.
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   NP_BIND         139..146
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          422..513
FT                   /evidence="ECO:0000255"
FT   COILED          681..765
FT                   /evidence="ECO:0000255"
FT   COILED          919..948
FT                   /evidence="ECO:0000255"
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
//

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