ID KIF9_DICDI Reviewed; 1222 AA.
AC Q555I8; Q86HL6; Q86SA4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Kinesin-related protein 9;
DE AltName: Full=Kinesin family member 9;
GN Name=kif9; Synonyms=kin2; ORFNames=DDB_G0274603;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Suyama E., Sutoh K.;
RT "Kinesin-related proteins from Dictyostelium.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
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 [4]
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).
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. 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; AB102779; BAC56911.1; -; mRNA.
DR EMBL; AAFI02000012; EAL70194.1; -; Genomic_DNA.
DR RefSeq; XP_644079.1; XM_638987.1.
DR AlphaFoldDB; Q555I8; -.
DR SMR; Q555I8; -.
DR STRING; 44689.Q555I8; -.
DR TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR PaxDb; 44689-DDB0185204; -.
DR EnsemblProtists; EAL70194; EAL70194; DDB_G0274603.
DR GeneID; 8619508; -.
DR KEGG; ddi:DDB_G0274603; -.
DR dictyBase; DDB_G0274603; kif9.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_268575_0_0_1; -.
DR InParanoid; Q555I8; -.
DR OMA; HDECEKI; -.
DR PhylomeDB; Q555I8; -.
DR Reactome; R-DDI-983189; Kinesins.
DR PRO; PR:Q555I8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; 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; IBA:GO_Central.
DR GO; GO:0007098; P:centrosome cycle; IMP:dictyBase.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:dictyBase.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:dictyBase.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:dictyBase.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR PANTHER; PTHR24115:SF1002; KINESIN-RELATED PROTEIN 9; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1222
FT /note="Kinesin-related protein 9"
FT /id="PRO_0000365584"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 350..719
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 724..1026
FT /evidence="ECO:0000255"
FT COMPBIAS 75..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 438..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 935
FT /note="E -> V (in Ref. 1; BAC56911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1222 AA; 136066 MW; 2C14E8F6F00D5E39 CRC64;
MDNNNNNFST PKQPTINSTT GGQLRSRSNS SPSTSSISTP RNGSTTATTS SITNSIGKGS
LVFSTMENAK KTLNMDSLST PMSQSSKKRL SMNSSLLPPS SIPLPPSQQL SAKKDPSKRH
SSFISTTTTT SLGSRPSTPQ PNHTTNNNNN NNNGSNGNNV TSTNISSMLE SNNSEILSQN
QKVTLSTSSN TAFSSLPSST NNGNNPLSNS GGGNGNHHLV NSNSSTSTPS PTMFISTTSP
PPELSLMEGF NQHNLTTTTT TTTTTTNNTL NTSNGINSNS LSPSSHLNNG SNNNNNNNHL
NLNNRSSSPS PTPSSSSISG RRTPIQNFNS VGGVNITSKT QPLFSDREES IQAVCRFRPE
TAAEQTLGPS EKQLTIGTDQ TTIHITPTSS SSSSMAQAFR FSKVYQPNTT QESFYNEVGK
PLIDNIVNGY NVGIIAYGQT GAGKTFSLGF SGGEGNDSYN SYCNRSEFYN NSHYLYGSQQ
QQQQQQLLPS SWGIMPRIIK DLFIKQDEQQ SMNTPQRIKF TTKISYLEVY KEKVYDLLSE
GGVNDIEIRM ADGGFIVPDA VQSSIQTFTD FLTHLQHIEK NRKIAETKKN MASSRSHAIF
IVSLLKEDLE NKMTVTSLLY LVDLAGSESA SKIDGTTSKI EETKSINKSL YALGGVIEDM
SKNSKHVRYR DSKLTQLLQQ CFGGNSKTCL IVNCSSSNHE SVIRETIQSL NFGQRAQSVK
NKPLQNVEES HSELKAKLRE LNKDIETYKK FIEKISINSG VIPPSSVATY ITQLQNACEE
LKKKNDRLQE DIINLEEENS DLPKKFNVLN KNNVSQIEIL TQELELSKQI NQEQLLKIEQ
YSQKYQATNE EIQKSFNHRQ QLVNDLHDSN EKSKQLELKL KDALLNSKSE SDEIRLKLTK
ALEESTDKDQ RINTLESNKQ KWKSKCNEVV RQSKELQDRL NILQSTYSNS VDSLSNSSLN
NNNNESLEEI KKLKLNISSL TNQHIEREKS LQKEIDLARS KHTEQTLILK NLKTQIDTLT
NKLEIQFPTI VNNNQQQQQS TQSSSSSSIE SNLIISMNTI EVLFEKICKN QEQTNTIIST
NVESIMGKLV EIDENEEFIR KEKDRERERA ENLKNTLEDA QSNFLKQQEE IKQFIETQLK
NKNNINNNNN IKNNNNNNKL KSKKVGSSSS SSSNIGSSIC INILFFLIIL VILFFLMVAV
GLTIQNQDYN SQYRSSYFFK TT
//
