KIF3_DICDI
ID KIF3_DICDI Reviewed; 1193 AA.
AC Q54UC9; O15720; Q6S005; Q8I825;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Kinesin-related protein 3;
DE AltName: Full=Kinesin family member 3;
DE AltName: Full=Kinesin-1;
GN Name=kif3; Synonyms=K3, ksnC; ORFNames=DDB_G0280967;
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 1-1190, AND IDENTIFICATION.
RX PubMed=12952062; DOI=10.1023/a:1024403006680;
RA Klopfenstein D.R., Holleran E.A., Vale R.D.;
RT "Kinesin motors and microtubule-based organelle transport in Dictyostelium
RT discoideum.";
RL J. Muscle Res. Cell Motil. 23:631-638(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-129.
RC STRAIN=AX2;
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 [5]
RP PROTEIN SEQUENCE OF 230-240, AND FUNCTION.
RX PubMed=10545495; DOI=10.1083/jcb.147.3.493;
RA Pollock N., de Hostos E.L., Turck C.W., Vale R.D.;
RT "Reconstitution of membrane transport powered by a novel dimeric kinesin
RT motor of the Unc104/KIF1A family purified from Dictyostelium.";
RL J. Cell Biol. 147:493-506(1999).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18160177; DOI=10.1016/j.ejcb.2007.11.001;
RA Rohelk C., Rohlfs M., Leier S., Schliwa M., Liu X., Parsch J., Woehlke G.;
RT "Properties of the Kinesin-1 motor DdKif3 from Dictyostelium discoideum.";
RL Eur. J. Cell Biol. 87:237-249(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. The maximal velocity in an inverted motility
CC assay (moving microtubules on fixed motors) was 1.96 um/s.
CC {ECO:0000269|PubMed:10545495, ECO:0000269|PubMed:18160177}.
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:18160177}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18160177}. Note=Local concentrations were found in
CC vesicular structures around the nucleus in live cells.
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY484460; AAR39436.1; -; Genomic_DNA.
DR EMBL; AAFI02000040; EAL66780.1; -; Genomic_DNA.
DR EMBL; AY162212; AAN86033.1; -; mRNA.
DR EMBL; AF015714; AAB66584.1; -; Genomic_DNA.
DR RefSeq; XP_640847.1; XM_635755.1.
DR AlphaFoldDB; Q54UC9; -.
DR SMR; Q54UC9; -.
DR STRING; 44689.DDB0216174; -.
DR PaxDb; Q54UC9; -.
DR PRIDE; Q54UC9; -.
DR EnsemblProtists; EAL66780; EAL66780; DDB_G0280967.
DR GeneID; 8622903; -.
DR KEGG; ddi:DDB_G0280967; -.
DR dictyBase; DDB_G0280967; kif3.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_3_0_1; -.
DR InParanoid; Q54UC9; -.
DR OMA; FIVKASY; -.
DR PhylomeDB; Q54UC9; -.
DR PRO; PR:Q54UC9; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
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:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..1193
FT /note="Kinesin-related protein 3"
FT /id="PRO_0000365578"
FT DOMAIN 3..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 377..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..962
FT /evidence="ECO:0000255"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 17..20
FT /note="ELAQ -> TRNS (in Ref. 4; AAB66584)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="S -> K (in Ref. 1; AAR39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..129
FT /note="NI -> RN (in Ref. 4; AAB66584)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="I -> G (in Ref. 1; AAR39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="T -> P (in Ref. 1; AAR39436 and 3; AAN86033)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="K -> E (in Ref. 1; AAR39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="YI -> FF (in Ref. 1; AAR39436)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="A -> V (in Ref. 3; AAN86033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1193 AA; 130532 MW; 6DCE1269BDB6930A CRC64;
MSSIRVVCRF RPQNKLELAQ GGDSIVSIAP ENDSVTINGS ESNHSFSFDY VFPSNTTQRD
VYDHAAKPVI EDIMAGYNGT LFVYGQTGSG KTFSMTGIND PNGDQELRGI VPRMIETVFE
FISNADENIE FIVKASYIEI YMERIRDLLD TRKDNLKVRE EKGKGVWVEG TSEVYIYREE
DILDVINTGI SNRAIAETRM NAESSRSHSI FILTIQQKNL KVGSIKTGKL YLVDLAGSEK
ISKTGAQGTT LDEAKMINKS LSSLGNVINA LTDGKSTHIP YRDSKLTRVL QESLGGNSRT
TLIINCSPSS YNEAETISTL RFGSRAKNIK NKAKINQERS AAELKILLSK AENEIENLKG
YIKELETVSG VTVSNLKSSG SGSGSGSGSS SSSSGSSGGS GSGGSSNLSN SVNSTSNLNT
SSNTSSSNVN ANANVITTSV SAPTSPKDTE LIKVLQEKCI QLEKQLFKKE EEKKEILEQL
EQQQEQIQDK DQEIEGLNSM IESSNNINSL YQNSTNENSV LNVQLSELKL ALEKSRFEAT
EQSLTIEGLN EENQSIKSQL EILKDRIAQS GDSSIASLVP STPKSSAEMD PLATASKHAD
EWNEKAEQLK LLQRTPSKAV GSSKSNTATS SPIISLNISE SDNIGSGATT TTNNNNATIT
PATSSNNNVE QQQQQVEELL PSVNEQLLES ENQKLQKRIQ EIELEFETYK IAKENLTMQK
DLEIEQLLES QRISSSFVVD PRNLDDELPA EMMLQAEQIR KLIAENSEQK VHFEATKNEN
SKLKNRIEMI EEETRQRMEE ELNVLREQTN QKLSEFGSLK ESLIRDLENR CQKVIDLELV
LDELQDRIVT LNERLKRVNK PGGGDQEAAF VQSKLDEITA VKHQLVIENN KHKTEVERLK
KLLSHRGEHI LILEKTMAIN QESLFKLALN HNALTIEHDR AKNELEKLNN LLSQVGVDAQ
NTGGARVARV IRGGGGNNQL KKFNHSSSSS TSSSSALNHS SINNNHTTPT PLSANLYSNT
KRSTKELNTG VKAEPLSLSG SPFNTSIPSS PNHTSSNNIN NNSNNNNNNN NNNNIGNSGN
IGGVGNNNSS ISNSNNNSSS NLNANLNGNT PVKITSENSS SSLWNIFKKK SPSSTPPSST
NNLSPQSPQT PSHLSADGSG NISPNLSPPI PVNFSYTPAV VTSSTINKDQ QKD
