KIF10_DICDI
ID KIF10_DICDI Reviewed; 1238 AA.
AC Q6S002; Q54C36;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Kinesin-related protein 10;
DE AltName: Full=Kinesin family member 10;
DE AltName: Full=Kinesin-8;
GN Name=kif10; ORFNames=DDB_G0293198;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND NOMENCLATURE.
RC STRAIN=AX4;
RX PubMed=14641909; DOI=10.1186/1471-2164-4-47;
RA Kollmar M., Gloeckner G.;
RT "Identification and phylogenetic analysis of Dictyostelium discoideum
RT kinesin proteins.";
RL BMC Genomics 4:47-47(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION.
RX PubMed=18430243; DOI=10.1186/1471-2121-9-21;
RA Nag D.K., Tikhonenko I., Soga I., Koonce M.P.;
RT "Disruption of four kinesin genes in dictyostelium.";
RL BMC Cell Biol. 9:21-21(2008).
CC -!- FUNCTION: Microtubule-associated force-producing protein that plays a
CC role in organelle transport. Its motor activity is directed toward the
CC microtubule's plus end (By similarity). Cooperates with kif8 and dynein
CC to organize interphase microtubules. {ECO:0000250,
CC ECO:0000269|PubMed:18430243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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; AY484463; AAR39439.1; -; Genomic_DNA.
DR EMBL; AAFI02000200; EAL60798.1; -; Genomic_DNA.
DR RefSeq; XP_629230.1; XM_629228.1.
DR AlphaFoldDB; Q6S002; -.
DR SMR; Q6S002; -.
DR STRING; 44689.DDB0215386; -.
DR PaxDb; Q6S002; -.
DR PRIDE; Q6S002; -.
DR EnsemblProtists; EAL60798; EAL60798; DDB_G0293198.
DR GeneID; 8629112; -.
DR KEGG; ddi:DDB_G0293198; -.
DR dictyBase; DDB_G0293198; kif10.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_267010_0_0_1; -.
DR InParanoid; Q6S002; -.
DR OMA; KGTHIRE; -.
DR PRO; PR:Q6S002; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0003777; F:microtubule motor activity; IDA:dictyBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; 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;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..1238
FT /note="Kinesin-related protein 10"
FT /id="PRO_0000365585"
FT DOMAIN 16..374
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 417..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 527..602
FT /evidence="ECO:0000255"
FT COMPBIAS 417..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..499
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1238 AA; 139012 MW; A741AE4FC63D593F CRC64;
MNNNNNNNNN KTTMNSMIVT VRIRPESQSE ILNKNCKTIV RVIDDNMLVF DPNDIDIGAF
NNNRNNKQSQ QPVEQKYIFD RVFDQYATQE EVFENTTKEL VSYVISGHNA SVFAYGASGA
GKTHTMVGGI NTGPGIMVLT MKELFSLIEK DRSNQYIVSM SYLEVYNETI RDLLITNTGG
GGNSNNKVLE LCEDENKQIV IRDLSWEYPT SADQVFKLLK YGNLNRKQSP TQTNQTSSRS
HAVLQITVKQ QNLQDKSKIS FGKLSLIDLA GSERASKTLN TGDRLKEGTS INKSLLALGN
CIKALGELCK NQQSQQQSSN PNFIPYRDSK LTRILKDSLT GSCKTIMIAN ISPNSSSFEE
THNTLKYAQR AKSIKTQITK NVFASSTNLI TQYNEIIKEQ REEIKQLKLK LIQATSNNNN
SNNNNNNNNN NYFSNSFGSC GNKNQPIKQP TPPTSLFHQQ NQKYYRNDDD DDDDNDQEEN
NDEVLINEDD EEVDGEDSNN RDNDESMIQQ LEEMSLLINS NLQDTLTLKK TQSIQRQRKR
ELENELKSLE KQQQSILNEN NNVDIIKRTN EIGSQILKIK TLESSINEKL EMNNQWRRKL
QSELTLKFVN SPKNLKILIQ QARAATLELD RFDLTERMID DRSKLNLKTN ECKSLKDSLS
WMFGILSDGF KLLTENNLAT DDFLKDFLKS GDLINNLDNS FIINENNDSN NNNIIENDDI
DLSFNNDINN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNVPLNCN
NSNSNINNKN QNIINPSPLK PRRIMSGSNN IIKSTNSNSR MTSTATTTAA STATATTTTI
GKEKKGEIRS IVNPINKISS STSLLPSSST KISNTTPLYS RTSILRKRTL EIDDSTDSNP
RTKKINVSSP VVTKPKQLLP STTTATTTTL SSPLVNKPKQ ILPTTSSLQP KPHTKIQPHK
NNNNNNNNIA PQMNMNIQIP NPIPIPIPMH VQIPISNPIP MPSPSSMNLK EKLDSLSQLC
NNRSAKNENY NHNNSFNSQN PFVHPLQMHP PQLQLPLHPP QTMIMQSNMD LKMKLDSLSF
FNNNNNNHQA QNDLSFDYGQ NTLSNENLIL HNKIASLSST LINQPHPMRV KKLTPTSTIS
SSISTRPITT STTTSTTVPS VVSNRIKSLV HSNSPIKENL YKEKLSSTAS ATLTPNRNNS
QIVQPFKRGV LGNGPTSSSS RLLPSSRTTV NTSRKIIK
