(data stored in ACNUC7421 zone)

SWISSPROT: CIN8_ASHGO

ID   CIN8_ASHGO              Reviewed;         945 AA.
AC   Q8J1G7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=Kinesin-like protein CIN8;
GN   Name=CIN8; OrderedLocusNames=ACR010C;
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 mediated 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; AF378568; AAN87133.1; -; Genomic_DNA.
DR   EMBL; AE016816; AAS51237.1; -; Genomic_DNA.
DR   RefSeq; NP_983413.1; NM_208766.1.
DR   SMR; Q8J1G7; -.
DR   STRING; 33169.AAS51237; -.
DR   EnsemblFungi; AAS51237; AAS51237; AGOS_ACR010C.
DR   GeneID; 4619538; -.
DR   KEGG; ago:AGOS_ACR010C; -.
DR   HOGENOM; HOG000248614; -.
DR   InParanoid; Q8J1G7; -.
DR   KO; K10398; -.
DR   OMA; HTIFTIM; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
DR   GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005828; C:kinetochore microtubule; IEA:EnsemblFungi.
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:0008569; F:ATP-dependent microtubule motor activity, minus-end-directed; IBA:GO_Central.
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: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; -; 2.
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; 2.
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; Q8J1G7.
DR   SWISS-2DPAGE; Q8J1G7.
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..945
FT                   /note="Kinesin-like protein CIN8"
FT                   /id="PRO_0000125365"
FT   DOMAIN          22..409
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   NP_BIND         114..121
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   COILED          450..562
FT                   /evidence="ECO:0000255"
FT   COILED          634..675
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   945 AA;  106848 MW;  4ECA339E65909854 CRC64;
     MPDHEVQTRK SRMLDDAQEE LNITVAVRCR GRNEREIKAK SSVVVTVPDV TGSNEVSINT
     TDEVGIAAKM NSRTYTVDKV FGPSADQSLI FKEIAEPLFD DFMKGYNCTV LVYGMTSTGK
     TYTMTGDEKL YDGQLSDSAG IIPRIMFKLF DALEATDSDF LVKCSYIELY NEELKDLLDE
     SHDSSKRLRI FDSSSMNHSS RASSQSNSPR EPEVAHNGFS RRRQRPPPVK ANRMSATKQQ
     LSESGSGIYV QNVQEFHIIN AREGINVLQK GLKHRQVAST KMNDFSSRSH TIFTIMLYKN
     CDGELFRVSK MNLVDLAGSE NISRSGAQNQ RAKEAGSINQ SLLTLGRVIN SLADKSIHIP
     FRESKLTRLL QDSLGGNTKT ALIATISPAK INADETSSTL EYAAKAKNIK NRPQLGALMM
     KDILVKNISS ELAKIKSDFL STKSKDGIYM SHEHYQEIVN DLENCQTEIQ ESKRQIESLT
     SQNNLLLKDK KASQEVTELQ NSKIKKLQST IEYLYDKIER QHHNETELAT TIHKLKEALH
     TMQGSLKSYE THELRLQNDI KEVLYQGITS YRESMNQHLE KVKVSMLDKN LSIKENINNI
     TTIFDDTLKS VEANGSDMCD TLVKLIKETP SMYLKEFNET VSSLKSELSS YSNALTNKLT
     EISEENNHLR EYLDQHLFKN STQEVLDLRM ESVYQKVKND SDQLLSKLVS MVGAHVEESR
     TLMVNSMKDT VNEIIDNERS LFQPIRDRWI ASCDNINQCD ASHQNFEAKS TSGLDKLKEL
     SDASLKSSED AVNKAKHRTD SFHDFVQKLC CDQSLKKQMH DISDKHRMLE DHFDDNVKYF
     KESSKGFEDM DCSIKKIIHE MSPEVGDIKS VETLMERINA RTFSPVRPTG KTPSRQVLKN
     AITSKASSRS MSPIKTLDTN VRIISPVKRG TIEFGAEGPP TKKVR
//

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