KIF4_DICDI
ID KIF4_DICDI Reviewed; 1922 AA.
AC Q54NP8; O15719; Q869B8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Kinesin-related protein 4;
DE AltName: Full=Kinesin family member 4;
DE AltName: Full=Kinesin-7;
GN Name=kif4; Synonyms=K4, ksnD; ORFNames=DDB_G0285101;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-252,
RP 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 [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 IDENTIFICATION, AND NOMENCLATURE.
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 dynein in
CC organizing spindle assembly during cell division. {ECO:0000250,
CC ECO:0000269|PubMed:18430243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- INDUCTION: During the developmental stage.
CC {ECO:0000269|PubMed:9693369}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins,
CC vesicles and membranous organelles. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Significantly impairs the rate of cell growth
CC and, when combined with a previously characterized dynein inhibition,
CC results in dramatic defects in mitotic spindle assembly.
CC {ECO:0000269|PubMed:18430243}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC56912.1; Type=Miscellaneous discrepancy; Note=The cDNA sequence misses the fragment coding for residues 1006 to 1042 localized between two repeated sequences and probably lost during cloning.; Evidence={ECO:0000305};
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DR EMBL; AB102780; BAC56912.1; ALT_SEQ; mRNA.
DR EMBL; AF015713; AAB66583.1; -; Genomic_DNA.
DR EMBL; AAFI02000074; EAL64863.1; -; Genomic_DNA.
DR RefSeq; XP_639868.1; XM_634776.1.
DR AlphaFoldDB; Q54NP8; -.
DR SMR; Q54NP8; -.
DR STRING; 44689.DDB0191404; -.
DR PaxDb; Q54NP8; -.
DR EnsemblProtists; EAL64863; EAL64863; DDB_G0285101.
DR GeneID; 8624939; -.
DR KEGG; ddi:DDB_G0285101; -.
DR dictyBase; DDB_G0285101; kif4.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_235364_0_0_1; -.
DR InParanoid; Q54NP8; -.
DR OMA; YCEKISD; -.
DR PhylomeDB; Q54NP8; -.
DR Reactome; R-DDI-983189; Kinesins.
DR PRO; PR:Q54NP8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043515; F:kinetochore binding; ISS:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; ISS:dictyBase.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IGI:dictyBase.
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; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..1922
FT /note="Kinesin-related protein 4"
FT /id="PRO_0000365579"
FT DOMAIN 22..343
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 448..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 562..1712
FT /evidence="ECO:0000255"
FT COMPBIAS 490..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 490
FT /note="D -> A (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="N -> H (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="K -> Q (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 536..537
FT /note="LN -> FP (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 546..547
FT /note="TI -> QL (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 559..563
FT /note="ISGQV -> FQVKL (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="E -> R (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1006..1042
FT /note="Missing (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="N -> S (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420..1422
FT /note="KFE -> NLK (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1760
FT /note="I -> T (in Ref. 1; BAC56912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1922 AA; 222483 MW; C51EC7287E165BB2 CRC64;
MDNNNNNNNN NNDKNDKNEL NKIKVAIRVR PLNSRELGID QKIPWSISKD TISLSQNPNI
NFTYDYVFGI DSNTIDVYNA IAKSIVNSSL NGINGTIFAY GQTSSGKTFS MRGTESIPGI
IKLSIKDIFK SIEDSILEKD YLLKVSYLEI YNEEIKDLLN PTISNKKKLK IHEDIYKGVV
VANLKEEIVI SPDQIFALMN FGEERRHIGS TMMNDSSSRS HTIFRMQIQS TCKQNGTIQM
STLTLVDLAG SERVSSTGAE GVRLKEGTHI NKSLMTLSKV ISKLSEEKTQ QHVPYRDSKL
TRILQPSLGG NSKTAILCTI TPATTHQEES ISTLQFAKRA KRVKTNYKIN QVADANTMLK
KYESEILELQ NQLVKSEEIN SLLRNTISTQ EISSNNFKLG MKRFNDAIIG GSLINENKKK
KKRRNTLDPS YLLKDKIIKK KIRKSENQKI KKIKNSENNI SSSSSNSSGE EDDDDKDDEN
NYSINQDDKD DSNYEDDDDE DEDDDEESDT DNEDDEDNDE DNDDDDDDDD EFKDNLNLIE
PLDDETIKKI KDLDDSLGIS GQVKVKREDL DLIYEELEEN KKLIEEYEST LELLNNQLDE
KEIEHKELLI IIDQWEQECT NRENQNQELL EIDQQSKQSI QQLNDKLLET KQQSKQSIDQ
LNLQLIDIES ESSKNKKSFE NVLGVFEKSY RLAERLEDKY FTKEIESKKQ IETLANSYLQ
LETTYQQQLN INQQSQQKIQ SLNNDIEQFK LVWVPLKDQV NGYFQENQMF KQYIIELEEK
YNTLIDLQKE VEQNYLTNTL EQQRNDQYQI EINQLTTEYN NQIQQLESTN QKLQTQLYNL
LANATQSTQT LEQQLQTSKQ EIDTLTNEIE QLKNQYDIIR VDNDNLSKES LELKQILLSK
TQQLEEQLSL AQQQKGNIEI IQQLESIIVD NQQSIDQLKI EFDQSQQDNQ SIKQSYNQLE
STLTLAQSEN QRLLTENKQF ITSLNEIKSL FNSIQQQKET IQLEFNQRLQ SWSLDSEKYK
EIISTLEQSN QKSIESYESK SLEFQEKENQ FDSLLTNYNQ LFSKYNDLAT SNESNRLEFD
QFKKDSNQSI QSLESLERSL KSENDNLLQQ SNLLKSQLES IEKQKQDQLI PIQLELESKK
CELSKLSSQF SEQTKQVTQL LISVDQYKIS TNKLESQISD RNEEINNLKL KAIEINALKE
ENISLKDQLT KLKKAPKSQT DREKDMIKKE LEKLREKFNA IDAKLKQAIQ DKQTIQSEKQ
SLEREIKDLK RSHTSTETEL DKLKKTHLAA DVKSKDFIAL NKSVEILTKS QEQLKSTIIE
LESDLSKKNI ELEKKQEELV TLNQDKLEKE KKTNQLESDH SSATIKLENY ENQITQLTSE
IIDLKSKFQE FKSESESNIK QQEINLKESN DLNQQLTNDK FELTKQLSDL KVEFDKSKQL
WSTRSSESND TIKELQESII SKDKERQLTS EQLVKLTDQI NLKTWEYNDL NSQCQQLTKT
LQNVKSSNEQ QEQSIVSLES QTSAKIKSLE LEISQIQENH RLEVLELNRC KNQLSEKQTL
MEQDNIQLNE RIIQLLHQKT KHENEILSME SNIIDLENQT KELKSKIETA QQDFEIEKNY
HTGLNETNTT TIKTMNEELT RSNQTIQQLL FKISKLEQTS LQTQQQQELQ QATISAQQQK
QQQLADDQEK QQLYQKIKLI EKELESTKQK NLYITEQFTL KESEYLDTIT DYVCKEKEFE
KSKASLKTSA TKIQALNDII KKLQEEKPQQ QPVVKVSSSQ VVNQNGQPIK SILKKPKLVI
IPREQLQQPP QFKELTLSTL NSNDSNCEPE SVSASSTLTS LQSISKYIGK RSEQTTLEHD
LTSSTLNLPL QQQNKKVRLV ITKNNKTSTD NLTTTSTSLK SKSSSNGENK ENQNNNIIIK
NN
