KIF8_DICDI
ID KIF8_DICDI Reviewed; 1873 AA.
AC Q6S003; Q54PI6; Q94500;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Kinesin-related protein 8;
DE AltName: Full=Kinesin family member 8;
DE AltName: Full=Kinesin-4;
GN Name=kif8; Synonyms=K8, ksnH; ORFNames=DDB_G0284471;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 13-350, AND INDUCTION.
RC STRAIN=AX3;
RX PubMed=9693369; DOI=10.1091/mbc.9.8.2093;
RA de Hostos E.L., McCaffrey G., Sucgang R., Pierce D.W., Vale R.D.;
RT "A developmentally regulated kinesin-related motor protein from
RT Dictyostelium discoideum.";
RL Mol. Biol. Cell 9:2093-2106(1998).
RN [4]
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 kif10 and
CC dynein to organize interphase microtubules. {ECO:0000250,
CC ECO:0000269|PubMed:18430243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:9693369}.
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; AY484462; AAR39438.1; -; Genomic_DNA.
DR EMBL; AAFI02000066; EAL65162.1; -; Genomic_DNA.
DR EMBL; U69985; AAB09083.1; -; mRNA.
DR RefSeq; XP_638546.1; XM_633454.1.
DR AlphaFoldDB; Q6S003; -.
DR SMR; Q6S003; -.
DR STRING; 44689.DDB0191403; -.
DR PaxDb; Q6S003; -.
DR PRIDE; Q6S003; -.
DR EnsemblProtists; EAL65162; EAL65162; DDB_G0284471.
DR GeneID; 8624639; -.
DR KEGG; ddi:DDB_G0284471; -.
DR dictyBase; DDB_G0284471; kif8.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_236383_0_0_1; -.
DR InParanoid; Q6S003; -.
DR OMA; HKQRVIQ; -.
DR PRO; PR:Q6S003; -.
DR Proteomes; UP000002195; Chromosome 4.
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: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; IBA:GO_Central.
DR GO; GO:0003777; F: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:0000226; P:microtubule cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..1873
FT /note="Kinesin-related protein 8"
FT /id="PRO_0000365583"
FT DOMAIN 13..413
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1506..1546
FT /note="WD 1"
FT REPEAT 1548..1587
FT /note="WD 2"
FT REPEAT 1589..1628
FT /note="WD 3"
FT REPEAT 1636..1673
FT /note="WD 4"
FT REPEAT 1677..1714
FT /note="WD 5"
FT REPEAT 1805..1842
FT /note="WD 6"
FT REPEAT 1844..1873
FT /note="WD 7"
FT REGION 231..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 715..933
FT /evidence="ECO:0000255"
FT COMPBIAS 231..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 13
FT /note="C -> G (in Ref. 3; AAB09083)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="KK -> MF (in Ref. 3; AAB09083)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> F (in Ref. 3; AAB09083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1873 AA; 208948 MW; B6B51952C63C3A32 CRC64;
MSSPILNTDD NNCVRVALRV RPLSKKEEAE RSMEVVKYVD GEPQVIMGDN NQTFTFDYVF
NGKSRQQEIF DDCVANLVDC LFEGYNSTIL AYGQTGSGKT FTMGTTSTIG IPTEELGVIP
RVIDFIYDKI DRKKDTHQLV LKVSFLELYN EEIRDMLNPY PTAGGLPIRE KSNGEVYIPG
LVEQIVRSRQ QMEEALIRGS QSRTTGSTLM NSHSSRSHAI FSIIVEQTPI NSPVTSSSTS
STSTSSSSDD KKQSKGKKKK KSSSPDSLSP NKDDDSSIMI DEDEEDDEED EDDDIMSMDE
RNPSIRSMFH FVDLAGSERV KKTKAEGQRL KEGININGGL LALGNVISAL GDTRRATTKP
KHIPYRDSKL TRMLQSSLGG NSKTLMIACV SPADSNFEET LNTLKYAYRA RNIMNKPVVN
IDPVTQQILT YKTQIQTLKE LLEKCTCRDI GDINSILASI PTVSIPPAPP LSTPTLTNNN
NNNSSSNNNN NSNNNKLNVG GNNSGFSRTP SSSSLPPTNS SKSSIVKMNN SRNISSSSSS
SSSSSSSSSL TTTPSITNNT ATPSPTSVIV TNLSKEKEKE IFDLGMKVSQ LEFENNMLQD
ISNKITSKYK ALANRSRQLE EISQNFINNF SPNKDQTYFN ELFEQFNSVL NQPTISPITP
MMAAVSTQIS SSNVIINSNS LLPMAEDNLL PGGKLESINN NNNNNNNSSE GIELFENDSE
ELSDLNQYIS EKEEELELIS KTKQQYQQMK EQFDQKVKEL QSQLEEVTVE KDQALKELDK
DKDKDKDNKD KDQYYEDEKL RLTQHYEKKL NELKQQLDQH AGSNKKDYQR LLDLKRKSEE
KIDSLQQDIK DTKRQKSDLL KKMRDELKKR DDAKQTQAKE LDALKREARK TEVIIDQLKN
QSKKKDLLLQ KKTDESESYK KKLKEIEVHK QRVIQPINSK SIPSNNNNNN SSGSVKSSNG
STASSASSAN SSSSSSSSSS TNTSTTSTSA TNNTTTSTST STPTTEQLNR KLLHRKSINV
PYWREWLIHQ IQKNLEKNEL TELLQREFKN KEIFVRQAND LKKAFTSVPS KLSKSEYNEQ
SQFLETNIKL QNEKILKSQK DLTIISNDCL DSPEILRMVS NTSFDKLPKL IQSSIELCIE
YAEINRKNQQ IKFINVPTPP TLQSQQQHQK SQHFYIQPPQ PLQSQQQQQE KQQKQSNSEQ
VLEQRSSTSD LLEGIKLAIS ESNNKNNINN NNNNVNIAKS QPILPSQQQL SSSQELAEEY
TSPSTSSLGM KLDQLLDEIK LDKEKREKNK LLNGYPPMSG INYFNPPTPQ PLSASSFLTS
AAATTTTTTT TTTTTNKQQV PKSFAPLNNT NNNNNNNNSS PLLLISDDKL DHSVFDKDLL
DVDILGNDSS NNGFSVININ SNNNITIKKP PSSPTRPHRK TTSLQSSPLS LSLESGLATA
LANNGNNNNN SNNNDVFTRL ASQPRPDSRL KKYRDKLNTD DYLMAIKRNM NREDENFMRC
NWTFNGHDGG LLTLVLDEQN PSTLYSGGSD KNIKLWDLHT GDNMLDLSSP GPVRSLCING
SSGCMFSGGA ERTVKVWDIR SPGNTNLCIF KTPSDVNCLV TYGNYVVSGL ENGTFKVWDI
RHMQKPLKTP LTTTPHHTGT IFSMSVTSKY LVTGSRDHTI NLFHRDSFVL AQKLQPPHHD
GVTSIAVLDD VIYSGSRDRT IKRWDVSSIN NLINNNGENN SNNLITTQLA QQTVPILSNT
PSNSNLIINN NNNIINNNNN NNNSSNNNKS SSAPSSTTSS LSSSLDNSTF SLLNQYQQNR
LLNNAHNDWV NCLCIHNGMI FSGGKDSNIK GWDPLLSSNS LLLGHESSIS CLTSSKEFLF
SGSTDKCIKI WKC
