KIF13_DICDI
ID KIF13_DICDI Reviewed; 1265 AA.
AC Q6RZZ9; Q54J21;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Kinesin-related protein 13;
DE AltName: Full=Kinesin family member 13;
DE AltName: Full=Kinesin-5;
GN Name=kif13; ORFNames=DDB_G0288361;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [4]
RP FUNCTION.
RX PubMed=18712789; DOI=10.1002/cm.20307;
RA Tikhonenko I., Nag D.K., Martin N., Koonce M.P.;
RT "Kinesin-5 is not essential for mitotic spindle elongation in
RT Dictyostelium.";
RL Cell Motil. Cytoskeleton 65:853-862(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 to
CC control the spindle elongation rate, but is dispensable for mitosis.
CC {ECO:0000250, ECO:0000269|PubMed:18712789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. BimC 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; AY484466; AAR39442.1; -; Genomic_DNA.
DR EMBL; AAFI02000111; EAL63277.1; -; Genomic_DNA.
DR RefSeq; XP_636780.1; XM_631688.1.
DR AlphaFoldDB; Q6RZZ9; -.
DR SMR; Q6RZZ9; -.
DR IntAct; Q6RZZ9; 1.
DR STRING; 44689.DDB0201557; -.
DR PaxDb; Q6RZZ9; -.
DR EnsemblProtists; EAL63277; EAL63277; DDB_G0288361.
DR GeneID; 8626583; -.
DR KEGG; ddi:DDB_G0288361; -.
DR dictyBase; DDB_G0288361; kif13.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_264479_0_0_1; -.
DR InParanoid; Q6RZZ9; -.
DR OMA; RHEISSM; -.
DR PhylomeDB; Q6RZZ9; -.
DR Reactome; R-DDI-983189; Kinesins.
DR PRO; PR:Q6RZZ9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IMP:dictyBase.
DR GO; GO:0007051; P:spindle organization; IMP: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 1: Evidence at protein 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..1265
FT /note="Kinesin-related protein 13"
FT /id="PRO_0000365588"
FT DOMAIN 23..350
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 918..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..459
FT /evidence="ECO:0000255"
FT COMPBIAS 929..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1265 AA; 142748 MW; A9A1AF17F098BB86 CRC64;
MITGLSIHNQ INKKNEPVKK EQNIQAFVRV RPFSVYELNQ GVTTVPIRVS DSSKEVLCEY
KGTTRQYKFD HVFDQDSIQS EVFNIAVKPI CDEVLLGFNG TIFVYGQTGT GKTHTMEGKH
GSNEDMGIIP RTINYLFQCL EQSGADYNIR ASHLEIYKEE IFDLLACNGN ENLNKPLGMF
DTQKGFKIPE LEEIVVNDRQ SILNVLAKSC KRRQTAETQY NKQSSRSHCI FSITVHVKET
SVGGEDLIKI GKLNLVDLAG SENAEKSGNN DRLREAALIN KSLLTLGKVI TDLTNNEKHI
PYRSSQLTKI LQDSLGGKTK TSIIATVSPS LVNLEETINT LEYALKAKNI KNTPQINQRM
SKNSLLKEQS SEIAHLKQLL QAAYDKNGVY LTIDVYEQMK RELEEKCSQQ SITEHKMEAQ
RHEISSMRKS FDEQTMLFEE AMNELESSKK QQQEKQKFID QFISQDTMLR SNLGSAVQDL
SKLHEKLDTM KSTERENQKS IIDSKSILSK RLTDLNQMLV SKLQMGQNEL LESLSVQLKV
VHDQQTKSNQ LIGKRINNLS QLIDSSVLQI QQLNNDDKQQ TQPLLKLNKE SNDLFMKLDK
TIQQLSDQIK IILSDFSLPF FNSNNNNSNN GDEIIDDSLI NNCFKLINDH VNKSDLIVSQ
QNKLIQEFSE SMSQWMLHQS QYIIEQRDYQ KQLKEKQILN NTQWEKKLLS KLGQVIQQFS
KNFTDSTSVY YDTMDNNLQH FEKQFNSINN HSRQQVESLS NNLQQSSTLS HQFESTVKSV
LNDHHANNKK VDPKLIESIE KAKKRINQLT DGCIDLSQRQ RQCTNQFNEA FTDFTFGIQS
QKDILDRVII EKNQVHEILP LIEKSKSTFK ENIDTLIHSL DSRKSIIQSS TNECSNQLNS
LISSIPSYLD SAIKVTSKSG ETPSKKHFDI PSPISTSSSS SSSSSISSIH SNAGGKENNH
QSINNSIKSN NFDGSKSINC DNMKIDTPQK SSTIPITPKS LKLNLNSTPK SVSKNLKSSQ
QQQPLIVPSS NQLTLSAKKL SNKEYQRLQQ QQQQQQQEQQ QQQSAKKKKL AIEKQLMITT
SPTLSLVNES PFSSPKLSKQ KILQDQIQPP QPPSILSQLN STPISFLQPQ QPQQQPPSFF
NNLNGSFNRG NNSIDFSLLD DDSDSDNSDD DVRSLLSSNK KSSRASKNAV VSKKVGLTPS
RKLKGVNSSA NQSLNVKKSK PILTSLSKKQ NISTPIIHSS KPSIFGGGST ISSKLKSLKQ
QTPLK
