ID   KIFC1_CRIGR             Reviewed;         622 AA.
AC   Q60443;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Kinesin-like protein KIFC1;
DE   AltName: Full=CHO2 antigen;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA58559.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7744954; DOI=10.1083/jcb.129.4.1049;
RA   Kuriyama R., Kofron M., Essner R., Kato T., Dragas-Granoic S., Omoto C.K.,
RA   Khodjakov A.;
RT   "Characterization of a minus end-directed kinesin-like motor protein from
RT   cultured mammalian cells.";
RL   J. Cell Biol. 129:1049-1059(1995).
CC   -!- FUNCTION: Minus end-directed microtubule-dependent motor required for
CC       bipolar spindle formation (PubMed:7744954). May contribute to movement
CC       of early endocytic vesicles (By similarity). Regulates cilium formation
CC       and structure (By similarity). {ECO:0000250|UniProtKB:Q9QWT9,
CC       ECO:0000269|PubMed:7744954}.
CC   -!- SUBUNIT: Binds NUBP1 and NUBP2. Interacts with PPP1R42 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7744954}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:7744954}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:7744954}. Early endosome
CC       {ECO:0000250|UniProtKB:Q9QWT9}. Note=Associated with nucleus during
CC       interphase, centrosomes in early and spindle in later mitosis.
CC       {ECO:0000250|UniProtKB:Q9QWT9, ECO:0000269|PubMed:7744954}.
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; X83576; CAA58559.1; -; mRNA.
DR   PIR; A57281; A57281.
DR   AlphaFoldDB; Q60443; -.
DR   SMR; Q60443; -.
DR   STRING; 10029.XP_007623248.1; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Endosome; Microtubule; Mitosis; Motor protein;
KW   Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN           1..622
FT                   /note="Kinesin-like protein KIFC1"
FT                   /id="PRO_0000302088"
FT   DOMAIN          260..612
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          95..264
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         360..367
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         309
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW19"
SQ   SEQUENCE   622 AA;  68821 MW;  C40B01ECC79B6DBF CRC64;
     MKEALEPAKK RTRGLGAVTK IDTSRSKGPL LSSLSQPQGP TAAQKGPKKT GPRGCTAVGS
     VLKNQKLAPT APAQKPVRKR PGKRPDWDLK GQLCDLTEEL KCYREKTQKL DQENQGLQEQ
     LKEAQEQAAA LGTERNTLEG ELASVRTQAE QCQQKLEALC ARVLELEEWL GTKENLIQEL
     QKEQLELQEE RKALATRLEE QERRLQASEA ALLSNESEVV CLRQKTAAQV TLLAEQGDRL
     HGLEMERRRL HNQLQELKGN IRVFCRVRPV LAGEPTPSPG FLLFPHGPAG PSDPPTRLSL
     SRSDDRRSTL TRAPAPTTRH DFSFDRVFPP GSKQEEVFEE ISMLVQSALD GYPVCIFAYG
     QTGSGKTFTM EGRPGGDPQL EGLIPRRMRH LFSVAQEMSG QGWTYSFVAS YVEIYNETVR
     DLLATGTRKG QGECEIRRAR PGSEELTVTN ARYVPVSCER EVEALLHLAH QNRAVARTAQ
     NERSSRSHSV FQLQISGEHA ARGLQCVAPL NLVDLAGSER LDPGLTLGPG ERDRLRETQS
     INSSLSTLGL VIMALSNKES HVPYRNSKLT YLLQNSLGGS AKMLMFVNIS PLEENVSESL
     NSLRFASKVN QCVIGTAQAN KK